Plays a role in short-term synaptic plasticity in a subset of GABAergic neurons in the brain. LAMP5 Protein, Pongo abelii, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 30.4 kDa and the accession number is Q5R5V2.

BAFF/TNFSF13B Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with N-6xHis tag. The predicted molecular weight is 22 KDa and the accession number is Q9Y275.

BAFF/TNFSF13B Protein, Mouse, Recombinant (mFc) is expressed in HEK293 mammalian cells with N-mFc tag. The predicted molecular weight is 45-60 KDa and the accession number is Q9WU72.

May function in mediating immune cell-cell interactions. May act as a T-cell costimulatory molecule, enhancing anti-CD3-induced proliferation. May play a role in the interaction of dendritic cells with T-cells and the cells of the adaptive immune response. CLECL1P Protein, Human, Recombinant (His & Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag. The predicted molecular weight is 13 kDa and the accession number is Q8IZS7.

B-cell activating factor (BAFF), also known as BLyS, TALL-1, THANK, and TNFSF13B, is a transmembrane glycoprotein in the TNF ligand superfamily. BAFF is a cytokine and serves as a ligand for receptors TNFRSF13B (TACI), TNFRSF17 (BCMA), and TNFRSF13C (BAFFR). BAFF can promotes the survival, proliferation and maturation of B lymphocytes, which are key elements in the pathogenesis of systemic lupus erythematosus (SLE). This cytokine is encoded on TNFSF13B gene, and diverse single-nucleotide polymorphisms have been associated with susceptibility in diferent autoimmune disorders. BAFF is a transmembranal protein expressed on myeloid lineage and some epithelial cells, through diferent stimuli such as IFN-γ, IFN-α, interleukin (IL)-10, Toll-like receptors (TLR)-3, TLR-4 and TLR-7.

Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys.; Functions in L-arginine homeostasis in nonhepatic tissues characterized by the competition between nitric oxide synthase (NOS) and arginase for the available intracellular substrate arginine. Arginine metabolism is a critical regulator of innate and adaptive immune responses. Involved in an antimicrobial effector pathway in polymorphonuclear granulocytes (PMN). Upon PMN cell death is liberated from the phagolysosome and depletes arginine in the microenvironment leading to suppressed T cell and natural killer (NK) cell proliferation and cytokine secretion. In group 2 innate lymphoid cells (ILC2s) promotes acute type 2 inflammation in the lung and is involved in optimal ILC2 proliferation but not survival. Plays a role in the immune response of alternatively activated or M2 macrophages in processes such as wound healing and tissue regeneration, immune defense against multicellular pathogens and parasites, and immune suppression and allergic inflammation; the regulatory outcome seems to be organ specific. In tumor-infiltrating dendritic cells (DCs) and myeloid-derived suppressor cells (MDSCs) plays a role in suppression of T cell-mediated antitumor immunity.

Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia-induced injury, inflammation and epithelial apoptosis in lung.

The immunoglobulin-like transcript (ILT) comprise a family of activating and inhibitory type immunoreceptors whose genes are located in the same locus that encodes killer cell Ig-like receptors (KIR). ILT4, also known as LIR-2 and LILRB2, is a type I transmembrane protein expressed primarily on monocytes and dendritic cells (DC). LILRB2 is a receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C, HLA-G and HLA-F alleles. LILRB2/CD85d/ILT4 Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 48.2 kDa and the accession number is XP_015297203.1.

Interleukin-10 Receptor alpha (IL-10 R alpha), also known as IL-10 R1, is transmembrane glycoprotein member of the class II cytokine receptor family. Interleukin-10 (IL10) is a key anti-inflammatory cytokine that is produced predominantly by leukocytes including T cells, B cells, monocytes, macrophages, and dendritic cells (DCs), as well as by some epithelial cells. The receptor for IL10 is a heterotetramer complex comprising two IL10Ra (also referred to as IL10R1) molecules and two IL10Rb (also referred to as IL10R2) molecules.IL10Ra is expressed on most hematopoietic cells at a basal level but is upregulated by various cells upon activation, suggesting its importance in inhibitory pathways.

B-Cell Differentiation Antigen CD72 (CD72) is a single-pass type II membrane protein. CD72 exists as a disulfide-linked homodimer and contains one C-type lectin domain. CD72 is expressed on B lineage cells, NK cells, monocytes, dendritic cells, and mast cells. CD72 is a ligand for CD5. CD72 associates with CD5, interacts with PTPN6/SHP-1 and plays a role in B-cell proliferation and differentiation. CD72 associates with CD79A in the B cell antigen receptor (BCR) complex following antigen stimulation and dampens BCR signaling through interactions with the phosphatase SHP-1.

V-set and transmembrane domain-containing protein 5 (Vstm5), a cell-adhesion-like molecule belonging to the Ig superfamily, was found in mouse brain. Knock-down of Vstm5 in cultured hippocampal neurons markedly reduced the complexity of dendritic structures, as well as the number of dendritic filopodia. Vstm5 also regulates neuronal morphology by promoting dendritic protrusions that later develop into dendritic spines. VSTM5 Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with C-hFc tag. The predicted molecular weight is 40 kDa and the accession number is A8MXK1.

Signal Regulatory Protein α (SIRPα) is a monomeric approximately 90 kD type I transmembrane glycoprotein. The 504 amino acid human SIRPα contains two Ig-like C1-type domains and one Ig-like V-type domain. SIRPα can express in various tissues, mainly on brain and myeloid cells, including macrophages, neutrophils, dendritic and Langerhans cells. It also can detect in neurons, smooth muscle and endothelial cells. SIRPA is an immunoglobulin-like cell surface receptor for CD47. SIRPα acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. SIRPα shows adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. SIRPα engagement generally produces a negative regulatory signal; it may mediate negative regulation of phagocytosis, mast cell activation and dendritic cell activation

V-set and transmembrane domain-containing protein 5 (Vstm5), a cell-adhesion-like molecule belonging to the Ig superfamily, was found in mouse brain. Knock-down of Vstm5 in cultured hippocampal neurons markedly reduced the complexity of dendritic structures, as well as the number of dendritic filopodia. Vstm5 also regulates neuronal morphology by promoting dendritic protrusions that later develop into dendritic spines. VSTM5 Protein, Mouse, Recombinant (hFc) is expressed in HEK293 mammalian cells with C-hFc tag. The predicted molecular weight is 40.1 kDa and the accession number is Q9D806.

Thymic Stromal Lymphopoietin (TSLP) was originally identified as an activity from the conditioned medium of a mouse thymic stromal cell line that promoted the development of B cells. Cytokine that induces the release of T-cell-attracting chemokines from monocytes and, in particular, enhances the maturation of CD11c dendritic cells. Can induce allergic inflammation by directly activating mast cells. TSLP Protein, Human, Recombinant (R127A & R130A, His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 17.7 kDa and the accession number is Q969D9-1.

Receptor activator of NF-κB(RANK,TNFRSF11A) belongs to one member of tumor necrosis factor receptor family.It is a receptor for TNFSF11/RANKL/TRANCE/OPGL. This gene encodes a type 1 membrane protein with a 30 amino acids (aa) signal peptide, 184 aa extracellular region , a 20 aa transmembrane domain and a 391 aa cytoplasmic region. Human and murine RANK share 81% aa identity in their extracellular domains. RANK is ubiquitous highly expressed in trabecular bone, thymus, small intestine, lung, brain and kidney, but weakly expressed in spleen and bone marrow. After binding its ligand RANKL, RANK can activate signaling pathways such as NF-κB, JNK, ERK, p38, and Akt/PKB, through TRAF protein phosphorylation. RANK/TNFRSF11A signaling is largely considered to be growth promoting and apoptosis reducing such as the effects observed in osteoclasts. RANK/TNFRSF11A was also found to be involved in the regulation of interactions between T-cells and dendritic cells.

Macrophage galactose N-acetyl-galactosamine-specific lectin 2(Mgl2), also known as CD301b, is a 38 kDa member that belongs to the C-type lectin family. Two MGL proteins are encoded by separate genes in the mouse, but share 91% amino acid (aa) identity in the extracellular domain (ECD). Only one MGL occurs in human and rat and this MGL is structurally more similar to mouse MGL1 than MGL2. However, human MGL and mouse MGL2 both bind specifically to terminal GalNAc residues, in contrast with mouse MGL1 which binds Lewis X. GalNAc recognition is likely to be important in dendritic cell-mediated tolerance to self-gangliosides as well as recognition of tumor antigens and parasite glycoproteins.

Thymic Stromal Lymphopoietin (TSLP) was originally identified as an activity from the conditioned medium of a mouse thymic stromal cell line that promoted the development of B cells. Cytokine that induces the release of T-cell-attracting chemokines from monocytes and, in particular, enhances the maturation of CD11c dendritic cells. Can induce allergic inflammation by directly activating mast cells. TSLP Protein (Primary Amine Labeling), Cynomolgus, Recombinant (His), Biotinylated is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 16.3 kDa and the accession number is A0A2K5TXV0-1.

Thymic stromal lymphopoietin (TSLP) is a novel member of the hemopoietic cytokine family that promotes the development of B cells and shares overlapping activity with IL-7. The human TSLP protein comprises a 28 amino acids (aa) signal sequence and 131 aa mature region. Human TSLP has two isoforms lfTSLP and sfTSLP produced by alternative splicing . lfTSLP is expressed in a number of tissues including heart, liver and prostate, and sfTSLP (63aa) is predominantly expressed in keratinocytes of oral mucosa, skin and in salivary glands. In aa sequence level, Human TSLP displays about 43% identity with mouse TSLP.TSLP is a cytokine that functions mainly on myeloid cells; it induces the release of T cell-attracting chemokines from monocytes and enhances the maturation of CD11c(+) dendritic cells.TSLP has proliferative effects on the myeloid cell line and may initiate asthma or atopic dermatitis responses by directly activating mast cells . TSLP signals cells via the interleukin-7 receptor-α chain (IL-7Rα),shared with IL-7, together with the TSLP receptor (TSLPR) subunit. Recent studies indicate that TSLP and its receptor are novel therapeutic targets for rheumatoid arthritis,for increased intraarticular TSLP concentrations in patients has caused chemotaxis and activation of arthritogenic T cells.

Pentraxin-related protein PTX3, also known as Tumor necrosis factor-inducible gene 14 protein (TSG-14), belongs to the pentraxin family. PTX3 plays a role in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility. It’s subunit is a disulfide-linked homooctamer that binds to C1q. PTX3 concentration is elevated in the joint fluid of patients with rheumatoid arthritis (RA), indicating that PTX3 may be a potential mediator of immune response. PTX3 may also function in the regulation of the uptake and clearance of apoptotic cells by dendritic cells. An in vivo study showed that PTX3 transgenic mice are more resistant to sepsis and endotoxemia compared to wild-type during inflammatory injury.

SIRPα is a type I transmembrane glycoprotein.It contains two Ig-like C1-type domains and one Ig-like V-type domain. Mouse SIRP alpha ECD shares 61%, 75%, 62%, 61%, and 59% aa sequence identity with human, rat, equine, bovine, and porcine SIRP alpha, respectively.SIRPα can express in various tissues, mainly on brain and myeloid cells, including macrophages, neutrophils, dendritic and Langerhans cells. It also can detect in neurons, smooth muscle and endothelial cells. SIRPA is an immunoglobulin-like cell surface receptor for CD47. SIRPα acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. SIRPα shows adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. SIRPα engagement generally produces a negative regulatory signal; it may mediate negative regulation of phagocytosis, mast cell activation and dendritic cell activation.

Monocyte Chemoattractant Proteins 4 (MCP-4/CCL13) is a member of a distinct, structurally-related subclass of CC chemokines mainly involved in recruitment of eosinphils to inflammatory sites. CCL13/MCP-4, is a CC family chemokine that is chemoattractant for eosinophils, basophils, monocytes, macrophages, immature dendritic cells, and T cells, and its capable of inducing crucial immuno-modulatory responses through its effects on epithelial, muscular and endothelial cells. Similar to other CC chemokines, CCL13 binds to several chemokine receptors (CCR1, CCR2 and CCR3), allowing it to elicit different effects on its target cells. A number of studies have shown that CCL13 is involved in many chronic inflammatory diseases, in which it functions as a pivotal molecule involved in the selective recruitment of cell lineages to the inflamed tissues and their subsequent activation. MCP-4/CCL13 is secreted from chondrocytes and activates the proliferation of rheumatoid synovial cells, thereby leading to joint destruction in RA. The interferon-gamma in combination with interleukin-1beta/tumor necrosis factor-alpha activates the production of MCP-4/CCL13 from chondrocytes in RA joints, and that secreted MCP-4/CCL13 enhances fibroblast-like synoviocyte proliferation by activating the extracellular signal-regulated kinase mitogen-activated protein kinase cascade. CCL13 may have some role in the pathogenesis of systemic sclerosis (SSc).

S100 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are disulfide-linked homodimer, and is normally present in cells derived from theneural crest, chondrocytes, macrophages, dendritic cells, etc. S100 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. Protein S100-A14, also known as S100 calciumbinding protein A14, S114 and S100A14, is a cytoplasm protein which belongs to the S-100 family. It is expressed at highest levels in colon and at moderate levels in thymus, kidney, liver, small intestine, and lung. Low expression in heart and no expression is seen in brain, skeletal muscle, spleen, placenta and peripheral blood leukocytes.

Trem-like transcript 1 protein, also known as Triggering receptor expressed on myeloid cells-like protein 1, TREML1 and TLT-1, is a cytoplasm and single-pass type I membrane protein. TREML1 / TLT-1 is expressed exclusively in platelets and megakaryocytes (MKs) and that its expression is up-regulated dramatically upon platelet activation. It is a receptor that may play a role in the innate and adaptive immune response. TREML1 / TLT-1 contains the characteristic single V-set immunoglobulin (Ig) domain, its longer cytoplasmic tail is composed of both a proline-rich region and an immune receptor tyrosine-based inhibitory motif, the latter known to be used for interactions with protein tyrosine phosphatases. The triggering receptors expressed on myeloid cells (TREMs) have drawn considerable attention due to their ability to activate multiple cell types within the innate immune system, including neutrophils, monocyte / macrophages, and dendritic cells, via their association with DAP12. TREML1 / TLT-1 is prepackaged, along with CD62P, into both MK and platelet alpha-granules. Differences in thrombin-induced redistribution of CD62P and TREML1 indicate that TREML1 is not simply cargo of alpha-granules but may instead regulate granule construction or dispersal. TREML1 / TLT-1 does not function to inhibit members of the TREM family but instead may play a role in maintaining vascular hemostasis and regulating coagulation and inflammation at sites of injury.

Serine/threonine-protein kinase TAO3, also known as cutaneous T-cell lymphoma-associated antigen HD-CL-9, CTCL-associated antigen HD-CL-9, Dendritic cell-derived protein kinase, JNK / SAPK-inhibitory kinase, Jun kinase-inhibitory kinase, Kinase from chicken homolog A, Thousand and one amino acid protein 3, JIK, TAOK3 and MAP3K18, is cytoplasm and peripheral membrane protein which belongs to the protein kinase superfamily, STE Ser/Thr protein kinase family and STE2 subfamily. Protein kinases are pivotal regulators of cell signaling that modulate each other's functions and activities through site-specific phosphorylation events. TAOK3 / JIK contains one protein kinase domain. TAOK3 / JIK is ubiquitously expressed at a low level, and highly expressed in peripheral blood leukocytes (PBLs), thymus, spleen, kidney, skeletal muscle, heart and liver. TAOK3 / JIK inhibits the basal activity of Jun kinase. It is negatively regulated by epidermal growth factor (EGF). When overexpressed, TAOK3 / JIK may activate ERK1 / ERK2 and JNK / SAPK.

The eotaxin subfamily of CC chemokines consists of eotaxin-1/CCL11, eotaxin-2/CCL24 and eotaxin-3/CCL26. All eotaxins induce the trafficking of eosinophils to the sites of inflammation via CC chemokine receptor 3 (CCR3), which is also expressed by several different cell types, including basophils, dendritic cells, smooth muscle cells, epithelial cells and fibroblasts. The sequence similarity between the three eotaxins is limited (<4%), but their functional properties are very similar. Eotaxin-1 and -2 are expressed by both haematopoietic and non-haematopoietic cells, but eotaxin-3 expression has been reported to be limited to non-haematopoietic cells. Interleukin (IL)-4 is the main inducer for eotaxin-3 expression, whereas eotaxin-1 is up-regulated by IL-4 and the proinflammatory cytokine tumour necrosis factor (TNF)-α. Eotaxin-3 is expressed in vascular endothelial cells and human dermal fibroblasts after IL-4 and IL-13 stimulation, and this is dependent upon the IL-4-/IL-13-specific transcription factor, signal transducers and activator of transcription (STAT)-6. Eotaxin-3 is expressed on the surface of IL-4-stimulated endothelial cells and promotes eosinophil transmigration.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy

Functional viral IL-10 homolog. Can bind to the human IL-10 receptor and compete with human IL-10 for binding sites. Requires both subunits of the human IL-10 receptor complex to induce signal transduction events and biological activities. IL-10 signaling pathway has several immunosuppressive activities that are exploited by the virus. Inhibits TLR-induced type I interferon production in host plasmacytoid dendritic cells. Human cytomegalovirus (HCMV) (strain Merlin) Viral interleukin-10 homolog is expressed in E. coli expression system. The predicted molecular weight is 17.5 kDa and the accession number is F5HC71.

Catalyzes the de novo synthesis of acetyl-CoA in vitro. Promotes acetylation of CTTN, possibly by providing the acetyl donor, ensuring correct dendritic spine morphology and synaptic transmission. Binds to follistatin-related protein FSTL1 and may act as a cell surface receptor for FSTL1, contributing to AKT activation and subsequent FSTL1-induced survival and function of endothelial cells and cardiac myocytes.

RNA-binding protein that is involved in the post-transcriptional regulation of mRNAs. Plays a role in the regulation of mRNA stability, alternative splicing and translation. Binds to AU-rich element (ARE) sequences in the 3' untranslated region (UTR) of target mRNAs, including GAP43, VEGF, FOS, CDKN1A and ACHE mRNA. Many of the target mRNAs are coding for RNA-binding proteins, transcription factors and proteins involved in RNA processing and/or neuronal development and function. By binding to the mRNA 3'UTR, decreases mRNA deadenylation and thereby contributes to the stabilization of mRNA molecules and their protection from decay. Also binds to the polyadenylated (poly(A)) tail in the 3'UTR of mRNA, thereby increasing its affinity for mRNA binding. Mainly plays a role in neuron-specific RNA processing by stabilization of mRNAs such as GAP43, ACHE and mRNAs of other neuronal proteins, thereby contributing to the differentiation of neural progenitor cells, nervous system development, learning and memory mechanisms. Involved in the negative regulation of the proliferative activity of neuronal stem cells and in the positive regulation of neuronal differentiation of neural progenitor cells. Promotes neuronal differentiation of neural stem/progenitor cells in the adult subventricular zone of the hippocampus by binding to and stabilizing SATB1 mRNA. Binds and stabilizes MSI1 mRNA in neural stem cells. Exhibits increased binding to ACHE mRNA during neuronal differentiation, thereby stabilizing ACHE mRNA and enhancing its expression. Protects CDKN1A mRNA from decay by binding to its 3'-UTR. May bind to APP and BACE1 mRNAS and the BACE1AS lncRNA and enhance their stabilization. Plays a role in neurite outgrowth and in the establishment and maturation of dendritic arbors, thereby contributing to neocortical and hippocampal circuitry function. Stabilizes GAP43 mRNA and protects it from decay during postembryonic development in the brain. By promoting the stabilization of GAP43 mRNA, plays a role in NGF-mediated neurite outgrowth. Binds to BDNF long 3'UTR mRNA, thereby leading to its stabilization and increased dendritic translation after activation of PKC. By increasing translation of BDNF after nerve injury, may contribute to nerve regeneration. Acts as a stabilizing factor by binding to the 3'UTR of NOVA1 mRNA, thereby increasing its translation and enhancing its functional activity in neuron-specific splicing. Stimulates translation of mRNA in a poly(A)- and cap-dependent manner, possibly by associating with the EIF4F cap-binding complex. May also negatively regulate translation by binding to the 5'UTR of Ins2 mRNA, thereby repressing its translation. Upon glucose stimulation, Ins2 mRNA is released from ELAVL4 and translational inhibition is abolished. Also plays a role in the regulation of alternative splicing. May regulate alternative splicing of CALCA pre-mRNA into Calcitonin and Calcitonin gene-related peptide 1 (CGRP) by competing with splicing regulator TIAR for binding to U-rich intronic sequences of CALCA pre-mRNA.

Specifically recognizes and binds N6-methyladenosine (m6A)-containing mRNAs, and regulates their stability. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Acts as a regulator of mRNA stability by promoting degradation of m6A-containing mRNAs via interaction with the CCR4-NOT complex. The YTHDF paralogs (YTHDF1, YTHDF2 and YTHDF3) shares m6A-containing mRNAs targets and act redundantly to mediate mRNA degradation and cellular differentiation. Required to facilitate learning and memory formation in the hippocampus by binding to m6A-containing neuronal mRNAs. Acts as a regulator of axon guidance by binding to m6A-containing ROBO3 transcripts. Acts as a negative regulator of antigen cross-presentation in myeloid dendritic cells. In the context of tumorigenesis, negative regulation of antigen cross-presentation limits the anti-tumor response by reducing efficiency of tumor-antigen cross-presentation. Promotes formation of phase-separated membraneless compartments, such as P-bodies or stress granules, by undergoing liquid-liquid phase separation upon binding to mRNAs containing multiple m6A-modified residues: polymethylated mRNAs act as a multivalent scaffold for the binding of YTHDF proteins, juxtaposing their disordered regions and thereby leading to phase separation. The resulting mRNA-YTHDF complexes then partition into different endogenous phase-separated membraneless compartments, such as P-bodies, stress granules or neuronal RNA granules.

Acts as an inhibitory receptor for myeloid cells and mast cells. Positively regulates the phagocytosis of apoptotic cells (efferocytosis) via phosphatidylserine (PS) recognition; recognizes and binds PS as a ligand which is expressed on the surface of apoptotic cells. Plays an important role in the maintenance of immune homeostasis, by promoting macrophage-mediated efferocytosis and by inhibiting dendritic cell-mediated efferocytosis. Negatively regulates Fc epsilon receptor-dependent mast cell activation and allergic responses via binding to ceramide and sphingomyelin which act as ligands. May act as a coreceptor for interleukin 4 (IL-4). Associates with and regulates IL-4 receptor alpha-mediated responses by augmenting IL-4- and IL-13-induced signaling. Negatively regulates the Toll-like receptor (TLR) signaling mediated by MYD88 and TRIF through activation of PTPN6/SHP-1 and PTPN11/SHP-2. Inhibits osteoclast formation. Induces macrophage cell death upon engagement.

CD83 is a member of the immunoglobulin (Ig) superfamily and is expressed in membrane bound or soluble forms. Membrane CD83 (mCD83) can be detected on a variety of activated immune cells, although it is most highly and stably expressed by mature dendritic cells (DC). While CD83 is emerging as a promising immune modulator with therapeutic potential, some important aspects such as its ligand/s, intracellular signaling pathways and modulators of its expression are unclear.

The immunoglobulin-like transcript (ILT) comprise a family of activating and inhibitory type immunoreceptors whose genes are located in the same locus that encodes killer cell Ig-like receptors (KIR). ILT4, also known as LIR-2 and LILRB2, is a type I transmembrane protein expressed primarily on monocytes and dendritic cells (DC). LILRB2 is a receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C, HLA-G and HLA-F alleles. LILRB2/CD85d/ILT4 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 50.2 kDa and the accession number is Q8N423-1.

Neural Cell Adhesion Molecule 1 (NCAM-1), a multifunctional member of the immunoglobulin superfamily, is expressed on the surface of neurons, glia, skeletal muscle, and natural killer cells. NCAM-1 has been implicated as having a role in cell-cell adhesion, involved in development of the nervous system, and for cells involved in the expansion of T cells and dendritic cells which play an important role in immune surveillance. NCAM1 Protein, Mouse, Recombinant (aa 20-711, His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 77.75 kDa and the accession number is P13595-1.

Tumor necrosis factor ligand superfamily member 4(TNFSF4/OX40L) is a single-pass type II membrane protein.OX40L is expressed on the surface of activated B cells, T cells, dendritic cells and endothelial cells. OX40L binds to OX40 (CD134), a member of the TNF receptor superfamily that is expressed predominantly on activated CD4+ T cells. OX40-OX40L co-stimulates signal to promote the survival and proliferation of activated CD4+ T cells and prolong the immune response. It involved in T-cell proliferation and cytokine production. Additional, it has been found association with systemic lupus erythematosus, no association with occurrence of atherosclerosis.

The immunoglobulin-like transcript (ILT) comprise a family of activating and inhibitory type immunoreceptors whose genes are located in the same locus that encodes killer cell Ig-like receptors (KIR). ILT4, also known as LIR-2 and LILRB2, is a type I transmembrane protein expressed primarily on monocytes and dendritic cells (DC). LILRB2 is a receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C, HLA-G and HLA-F alleles. LILRB2/CD85d/ILT4 Protein, Cynomolgus, Recombinant (hFc) is expressed in HEK293 mammalian cells with C-hFc tag. The predicted molecular weight is 71.68 kDa and the accession number is XP_015297203.1.

CD40 is a costimulatory protein found on antigen presenting cells and is required for their activation. The binding of CD154 (CD40L) on TH cells to CD40 activates antigen presenting cells and induces a variety of downstream effects.CD40 molecule is a potential target for cancer immunotherapy. There are number of completed and ongoing clinical trials where agonistic anti-CD40 monoclonal antibodies are employed to activate an anti-tumor T cell response via activation of dendritic cells.

NKp30, along with NKp44 and NKp46, constitute a group of receptors termed Natural Cytotoxicity Receptors . These receptors play a major role in triggering NK-mediated killing of most tumor cells lines.NKp30 stimulates NK cells cytotoxicity toward neighboring cells producing these ligands. It controls, for instance, NK cells cytotoxicity against tumor cells. Engagement of NCR3 by BAG6 also promotes myeloid dendritic cells (DC) maturation, both through killing DCs that did not acquire a mature phenotype, and inducing the release by NK cells of TNFA and IFNG which promote DC maturation.

Dendritic cell-associated C-type lectin-1 (Dectin-1), also known as β-glucan receptor is an emerging pattern recognition receptor (PRR) which belongs to the family of C-type lectin receptor (CLR). Dectin-1 signaling axis has been suggested to be targeted as an effective therapeutic strategy for cancers. Dectin-1 has also been elucidated ascetically in the heart, respiratory, intestinal, neurological and developmental disorders.

T cell immunoglobulin and mucin domain 3 is a member of the TIM family of immune regulating molecules. Mature cynomolgus TIM3 consists of a 182 amino acid (aa)extracellular domain (ECD), a 21 aa transmembrane segment, and a 78 aa cytoplasmic tail. TIM3 is up-regulated on several populations of activated myeloid cells (macrophage, monocyte, dendritic cell, microglia, mast cell) and T cells (Th1, CD8+, NK, Treg). Its binding to Galectin9 induces a range of immunosuppressive functions which enhance immune tolerance and inhibit anti-tumor immunity. TIM3 ligation attenuates CD8+ and Th1 cell responses and promotes the activity of Treg and myeloid derived suppressor cells. TIM3 interactions with Galectin-9 can trigger immune stimulatory effects, such as the coactivation of NK cell cytotoxicity.

Interleukin-36 gamma (IL-36γ) is a member of the interleukin 1 cytokine family that includes three closely related genes, IL-36α, β, and γ, formerly known as IL-1F6, F8, and F9 respectively. IL-36α has been detected in both neuronal and synovial tissue, whereas IL-36β and IL-36γ are expressed in both cutaneous and mucosal epithelial cells, including the respiratory tract. IL-36β and IL-36γ stimulate proliferation, maturation and/or cytokine expression by innate immune cells (such as keratinocytes and dendritic cells), and adaptive immune cells (neutrophils and T-cells) in both humans and mice. The activity of IL-36α is mediated by interleukin 1 receptor-like 2 (IL1RL2/IL1R-rp2), and is specifically inhibited by interleukin 1 family, member 5 (IL1F5/IL-1 delta). IL-36γ plays an important role in communicating the cell death to surrounding cells.

Flagellin is the major structural protein monomer of bacterial flagella. Flagellin through binding to its receptor and activation of antigen presenting cells stimulates the innate and adaptive immune responses. Flagellin is used as an effective systemic or mucosal adjuvant to stimulate the immune system. Flagellin is an agonist of Toll-like receptor 5 (TLR5), a pattern recognition receptor (PRR) of the innate immune system expressed on the basolateral surface of intestinal epithelial cells and on the surface of a subset of intestinal dendritic cells. Flagellin is delivered into the cytosol of macrophages by the T3SS-1 of serotype Typhimurium, where it activates the cytosolic interleukin-1 (IL-1) converting enzyme-protease activating factor (IPAF), a nucleotide-binding and oligomerization domain-like receptor (NLR) of the innate immunesystem. Recognition of flagellin by IPAF leads to activation of the inflammasome, followed by proteolytic activation of IL-1 and IL-18.

CD40 Ligand, also known as TNFSF5, CD154, is a type II transmembrane glycoprotein member of the TNF superfamily. Mature mouse CD40 Ligand consists of a 22 amino acid (aa) cytoplasmic domain, a transmembrane segment, and a 214 aa extracellular region. CD40 Ligand is expressed as a homotrimer on platelets and activated T cells and B cells. It is up­regulated following stimulation of basophils, eosinophils, fibroblasts, mast cells, monocytes, natural killer cells, vascular endothelial cells, and smooth muscle cells. CD40 Ligand binds and activates CD40, which is expressed on the surface of B cells, dendritic cells,macrophages, monocytes, platelets, endothelial cells, and epithelial cells. Monomeric, dimeric, and trimeric forms of soluble CD40 Ligand bind to oligomeric CD40 on cell membranes. CD40 ligation by CD40 Ligand promotes B cell activation and T cell­dependent humoral responses. CD40 Ligand dysregulation on T cells and antigen presenting cells contributes to the immune deficiency associated with HIV infection and AIDS. It is also implicated in the pathology of multiple cardiovascular diseases including atherosclerosis, atherothrombosis, and restenosis.

The Glypicans are a small multigene family of GPI-linked proteoglycans that play a key role in growth factor signaling. Human Glypican 1 (GPC1) is synthesized as a 558 amino acid (aa) preproprecursor that contains a 23 aa signal sequence, a 507 aa mature segment, and a 28 aa C-terminal prosegment. There are two potential N-linked and four potential O-linked sites for glycosylation or glycanation. There are potentially two heparan sulfate (HS) modifications on GPC1 that could contribute to a native molecular weight of approximately 200 kDa. Mature human GPC1 shares 91% aa identity with mature mouse GPC1. Cells known to express GPC1 include neurons, smooth and skeletal muscle cells, keratinocytes, osteoblasts, Schwann cells, immature dendritic cells, and tumor, plus tumorassociated vascular endothelial cells. The function of GPC1 is complex and varied. As a proteoglycan, it appears to make use of its HS adduct to impact select growth factor activity. This is accomplished by having juxtramembrane HS attachment sites, and a flexible, GPI-linkage.

Signal Regulatory Protein α (SIRPα) is a monomeric approximately 90 kD type I transmembrane glycoprotein. The 504 amino acid human SIRPα contains two Ig-like C1-type domains and one Ig-like V-type domain. SIRPα can express in various tissues, mainly on brain and myeloid cells, including macrophages, neutrophils, dendritic and Langerhans cells. It also can detect in neurons, smooth muscle and endothelial cells. SIRPA is an immunoglobulin-like cell surface receptor for CD47. SIRPα acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. SIRPα shows adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. SIRPα engagement generally produces a negative regulatory signal; it may mediate negative regulation of phagocytosis, mast cell activation and dendritic cell activation.

Tumor necrosis factor ligand superfamily member 4 (TNFSF4) is also known as glycoprotein Gp34, OX40 ligand (OX40L),which belongs to the tumor necrosis factor family. It is expressed on such cells as DC2s (a subtype of dendritic cells) enabling amplification of Th2 cell differentiation.

Low affinity immunoglobulin gamma Fc region receptor II (CD32B) is a single-pass type I membrane protein and contains 2 Ig-like C2-type (immunoglobulin-like) domains. The inhibitory CD32B is expressed on B cells and myeloid dendritic cells. Ligation of CD32B on B cells downregulates antibody production and may, in some circumstances, promote apoptosis. Co-ligation of CD32B on dendritic cells inhibits maturation and blocks cell activation. CD32B may also be a target formonoclonal antibody therapy for malignancies.

Macrophage colony-stimulating factor 1 receptor (CSF1R) is a member of the type III subfamily of receptor tyrosine kinases that also includes receptors for SCF and PDGF. These receptors each contain five immunoglobulin-like domains in their extracellular domain (ECD) and a split kinase domain in their intracellular region. CSF1R is expressed primarily on cells of the monocyte/macrophage lineage, dendritic cells, stem cells and in the developing placenta. CSF1 and its receptor (CSF1R, product of c-fms proto-oncogene) were initially implicated as essential for normal monocyte development as well as for trophoblastic implantation. It plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone and tooth development. It is required for normal male and female fertility, and for normal development of milk ducts and acinar structures in the mammary gland during pregnancy. Aberrant expression of CSF1 or CSF1R may play a role in inflammatory diseases, such as rheumatoid arthritis, glomerulonephritis, atherosclerosis, and allograft rejection.

Ephrin-A4 is a member of the ephrin ligand family which binds members of the Eph receptor family. All ligands share a conserved extracellular sequence, which most likely corresponds to the receptor binding domain. Ephrin-A4 consists of approximately 125 amino acids and includes four invariant cysteines, It has been shown to bind EphA2, EphA3, EphA4, EphA5, EphA6, EphA7, and EphB1. Ephrin-A4 binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. It may play a role in the interaction between activated B-lymphocytes and dendritic cells in tonsils.

CD47, also known as Integrin‑Associated Protein (IAP) and OA3, is a glycosylated atypical member of the immunoglobulin superfamily. Mouse CD47 is an integral membrane protein that consists of a extracellular domain (ECD) with a single Ig‑like domain, five membrane-spanning regions with short intervening loops, and C‑terminal cytoplasmic tail. CD47 has a role in both cell adhesion by acting as an adhesion receptor for THBS1 on platelets, and in the modulation of integrins. It plays an important role in memory formation and synaptic plasticity in the hippocampus. As a receptor for SIRPA, it binding to which prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. Interaction with SIRPG mediates cellcell adhesion, it enhances superantigen-dependent T-cell-mediated proliferation and costimulates T-cell activation. It may play a role in membrane transport and/or integrin dependent signal transduction. It also prevents premature elimination of red blood cells.

Butyrophilin-like 2 (BTNL2) is a member of the BTN/MOG Ig-superfamily and functions as a negative regulator of immune cell activation. Mouse BTNL2 is type I transmembrane glycoprotein that contains an extracellular domain (ECD), a transmembrane region and a short cytoplasmic domain. The ECD features two V-type Ig-like domains, two C-type Ig-like domains, and four glycosylation sites. BTNL2 is expressed in epithelial cells of the small intestine, colonic dendritic cells, and in cells of the lymph node. BTNL2 expression is upregulated in T cells following activation, a characteristic BTNL2 shares with the homologous B7 family of costimulatory molecules. BTNL2 negatively regulates T cells by inhibiting proliferation and inflammatory cytokine secretion. It also increases the expression of FoxP3 in T cells to promote regulatory T cell development. Single nucleotide polymorphisms in BTNL2 are associated with a risk for sporadic prostate cancer, rheumatoid arthritis, sarcoidosis, ulcerative colitis, and other inflammatory diseases.