human mast cells

Mouse interleukin-15 receptor subunit alpha, also known as Il15ra, is a high-affinity receptor for interleukin-15. Il15ra associates as a heterotrimer with the IL-2 receptor beta and gamma subunits (Common gamma chain, or gamma c) to initiate signal transduction. It can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells. Il15ra is expressed in special cells including a wide variety of Tand B cells and non-lymphoid cells. Human Il15ra shares 45% amino acid sequence homology with the mouse form of the receptor. Eight isoforms of IL-15 R alpha mRNA have been identified, resulting from alternative splicing events involving different exons.

Interleukin 15 Receptor alpha (IL-15Rα) is a transmembrane glycoprotein that plays a pleiotropic role in immune development and function, including the positive maintenance of lymphocyte homeostasis. IL-15Rα chain can bind soluble IL-15 and “transpresent” cytokine to the cells, allowing them to respond to IL-15. Soluble IL-15Rα can function as a specific high-affinity IL-15 antagonist. The soluble IL-15/IL-15Rα complexes exhibit a strong agonistic activity which is mediated through membrane-bound IL-15 receptor β and γ heterodimers and enables signaling to cells.

CD300a is an inhibitory receptor for mast cells and eosinophils in allergic inflammation (AI); however, the spatiotemporal expression of CD300a and its potential roles in the resolution of AI are still to be determined.CD300a expression on peritoneal cells is regulated from inflammation to resolution. CD300a activation on mouse bone marrow-derived mast cells regulated ALX/FPR2 expression levels following IgE-mediated activation. CD300A Protein, Human, Recombinant (Avi), Biotinylated is expressed in HEK293 mammalian cells with C-Avi tag. The predicted molecular weight is 19.46 kDa and the accession number is Q9UGN4-1.

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.

Interleukin 3 is a pleiotropic factor produced primarily by activated T cells that can stimulate the proliferation and differentiation of pluripotent hematopoietic stem cells as well as various lineage committed progenitors. This CSF induces granulocytes, macrophages, mast cells, stem cells, erythroid cells, eosinophils and megakaryocytes. IL-3 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in E. coli expression system with N-His-Avi tag. The predicted molecular weight is 16.9 kDa and the accession number is P08700.

Granulocyte-Macrophage Colony Stimulating Factor (GM-CSF) was initially characterized as a growth factor that can support the in vitro colony formation of granulocyte-macrophage progenitors. It is produced by a number of different cell types (including activated T cells, B cells, macrophages, mast cells, endothelial cells and fibroblasts) in response to cytokine of immune and inflammatory stimuli. Besides granulocyte-macrophage progenitors, GM-CSF is also a growth factor for erythroid, megakaryocyte and eosinophil progenitors. On mature hematopoietic, monocytes/ macrophages and eosinophils. GM-CSF has a functional role on non-hematopoitic cells. It can induce human endothelial cells to migrate and proliferate. Additionally, GM-CSF can also stimulate the proliferation of a number of tumor cell lines, including osteogenic sarcoma, carcinoma and adenocarcinoma cell lines.

Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. May play a role in innate immunity. TPSB2 Protein, Human, Recombinant (E. coli, His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 31.4 kDa and the accession number is P20231.

IL9R (Interleukin 9 Receptor) is a Protein Coding gene. The protein encoded by this gene is a cytokine receptor that specifically mediates the biological effects of interleukin 9 (IL9). IL9 is involved in mast cell maturation and the enhancement of IgE production by B cells. Furthermore, linkage data in the human and mice have suggested that IL9 may contribute to asthma. The ligand binding of this receptor leads to the activation of various JAK kinases and STAT proteins, which connect to different biologic responses. IL9R is known to be autosomal in mice and is X-linked only in primates. The more recent X linkage and more telomeric position of the IL9R gene may explain its autosomal, 'un-inactivated' transcriptional status.

Siglec-8 is also known as SIGLEC8, SAF2, SIGLEC-8, SIGLEC8L and sialic acid binding Ig like lectin 8, is an approximately 75 kDa transmembrane glycoprotein in the Siglec family of sialic acid-binding immune regulatory molecules. Siglec-8 is expressed on eosinophils, basophils, and mast cells, and it shows a binding preference for the carbohydrate 6-O sulfated sLex. At the tissue level, Siglec-8 mRNA was found to be most highly expressed in lung, PBMCs, spleen, and kidney. Mature human Siglec-8 consists of a 347 amino acid (aa) extracellular domain (ECD) with three Ig-like domains, a 21 aa transmembrane segment, and a 115 aa cytoplasmic domain with two tyrosine based signaling motifs. Alternative splicing generates additional isoforms that either lack most of the second Ig-like domain or have a substituted cytoplasmic domain without the signaling motifs. Cross-linking of Siglec-8 inhibits Fc epsilon RI alpha induced mast cell degranulation. It also induces eosinophil apoptosis, an effect which is enhanced by the eosinophil-activating cytokines IL-5, IL-33, and GM-CSF.

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 (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 17.8 kDa and the accession number is Q969D9-1.

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 (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 17.8 kDa and the accession number is Q969D9-1.

IL-9 is a pleiotropic cytokine that influences various distinct functions of different target cells such as T cells, B cells, mast cells and airway epithelial cells by activating STAT1, STAT3 and STAT5. Because of its pleiotropic functions, IL-9 has been demonstrated to be involved in several diseases, such as cancer, autoimmunity and other pathogen-mediated immune-regulated diseases. In this review, we focus on the role of Th9 and IL-9-producing cells in allergic asthma. IL-9 Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with C-hFc tag. The predicted molecular weight is 40.9 kDa and the accession number is P15248.

Leukotriene C4 synthase, also known as LTC4 synthase, Leukotriene-C(4) synthase, and LTC4S, is a multi-pass membrane protein that belongs to the MAPEG family. LTC4S is detected in the lung, platelets, and the myelogenous leukemia cell line KG-1 (at protein level). LTC4S activity is present in eosinophils, basophils, mast cells, certain phagocytic mononuclear cells, endothelial cells, vascular smooth muscle cells, and platelets. LTC4S is essential for the production of cysteinyl leukotrienes (Cys-LT), critical mediators in asthma. Mutagenic analysis of the conjugation function of human LTC4S has identified R51 and Y93 as critical for acid and base catalysis of LTA4 and reduced glutathione, respectively. A comparison across species for proteins that possess LTC4S activity reveals conservation of both of these residues, whereas R51 is absent in the FLAP molecules. Thus, within the glutathione S-transferase superfamily of genes, alignment of specific residues allows the separation of LTC4S family members from their most structurally similar counterparts, the FLAP molecules. Defects in LTC4S are the cause of leukotriene C4 synthase deficiency (LTC4 synthase deficiency). LTC4 synthase deficiency is a fatal neurometabolic developmental disorder. It is associated with muscular hypotonia, psychomotor retardation, failure to thrive, and microcephaly.

Syntaxin-binding protein 3, also known as Platelet Sec1 protein, Protein unc-18 homolog 3, Protein unc-18 homolog C, Unc-18C, Unc18-3 and STXBP3, is a cytoplasm protein which belongs to the STXBP/unc-18/SEC1 family. STXBP3 is expressed in cells that exhibit granule exocytosis, such as neutrophils, mast cells, platelets and endothelial cells. STXBP3, together with STX4 and VAMP2, may play a role in insulin-dependent movement of GLUT4 and in docking / fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes. STXBP3 participates in the consolidation and secretion of secondary and tertiary granules. STXBP3 contains one SEC1 domain. Phosphorylation at Ser129 may stimulate granule release. Human STXBP3 shares 9% aa identity with mouse STXBP3. STXBP3 interacts with DOC2B; the interaction is direct, occurs at the cell membrane, excludes interaction with STX4 and regulates glucose-stimulated insulin secretion. Interacts with STX4.

Mast Cell Protease 1 (MMCP-1), also known as MCP-1, MCPT-1 and β-chymase, is a member of the Chymase family of chymotrypsin-like serine proteases. MCPT-1 is a 26 kDa β-chymase that is a component of mast cell granules. It is a 226 amino acid (aa) protein that has a conserved pattern of six cysteines and one potential glycosylation site. The granule-derived mouse mast cell proteases-1 and -2 (mMCP-1 and -2) colocalize in similar quantities in mucosal mast cells but micrograms of mMCP-1 compared with nanograms of mMCP-2 are detected in peripheral blood during intestinal nematode infection. mMCP-1 isolated from serum is complexed with serpins and both the accumulation and the longevity of mMCP-1 in the blood is due to complex formation, protecting it from a pathway that rapidly clears mMCP-2, which is unable to form complexes with serpins. The mucosal mast cell (MMC) granule-specific beta-chymase, mouse mast cell protease-1 (mMCP-1), is released systemically into the bloodstream early in nematode infection before parasite-specific IgE responses develop and TGF-beta1 induces the constitutive release of mMCP-1 by homologs of MMC in vitro. Expression of mMCP-1 is largely restricted to intraepithelial MMC and is thought to play a role in the regulation of epithelial permeability. Its activation is completed by the removal of a two residue N-terminal propeptide by a dipeptidyl peptidase (Cathepsin C). MCPT-1 is upregulated in the intestine in response to nematode infection, or systemic mucosa in response to anaphylaxis. Like human α-chymase, MCPT-1 is capable of the conversion of angiotensin I to angiotensin II, which plays a key role in the regulation of arterial pressure. The intestinal inflammation associated with gastrointestinal helminths is partly mediated by mMCP-1.

Interleukin 3 is a pleiotropic factor produced primarily by activated T cells that can stimulate the proliferation and differentiation of pluripotent hematopoietic stem cells as well as various lineage committed progenitors. In addition, IL-3 also affects the functional activity of mature mast cells, basophils, eosinophils and macrophages.Because of its multiple functions and targets, it was originally studied under different names, including mast cell growth factor P-cell stimulating factor, burst promoting activity, multi-colony stimulating factor, thy-1 inducing factor and WEHI-3 growth factor. In addition to activated T cells, other cell types such as human thymic epithelial cells, activated mouse mast cells, mouse keratinocytes and neurons/astrocytes can also produce IL-3. IL-3 exerts its biological activities through binding to specific cell surface receptors. The high affinity receptor responsible for IL-3. signaling is composed of α and βsubunits. IL-3 is capable of supporting the proliferation of abroad range of hematopoietic cell types. It is involved in avariety of cell activities such as cell growth, differentiation and apoptosis. IL-3 has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.

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), Biotinylated 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.

CD300a is an inhibitory receptor for mast cells and eosinophils in allergic inflammation (AI); however, the spatiotemporal expression of CD300a and its potential roles in the resolution of AI are still to be determined.CD300a expression on peritoneal cells is regulated from inflammation to resolution. CD300a activation on mouse bone marrow-derived mast cells regulated ALX/FPR2 expression levels following IgE-mediated activation. CD300A Protein, Human, Recombinant (Avi) is expressed in HEK293 mammalian cells with C-Avi tag. The predicted molecular weight is 19.46 kDa and the accession number is Q9UGN4-1.

Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. May play a role in innate immunity. TPSB2 Protein, Human, Recombinant (His & Myc) is expressed in yeast with C-6xHis-Myc tag. The predicted molecular weight is 31.2 kDa and the accession number is P20231.

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.

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

Lysosomal associated membrane protein 1 (LAMP1) is an approximately 120 kDa transmembrane glycoprotein that is a major protein component of lysosomal membranes. Mature mouse LAMP1 consists of a 346 amino acid (aa) intralumenal domain (ECD), a 24 aa transmembrane segment, and a 12 aa cytoplasmic tail. Its lumenal domain is organized into two heavily N-glycosylated regions separated by a Ser/Pro-rich linker that carries a minor amount of O-linked glycosylation. Within the lumenal domain, mouse LAMP1 shares approximately 64% and 82% aa sequence identity with human and rat LAMP1, respectively. The sorting of LAMP1 to lysosomes relies on a tyrosine motif in the cytoplasmic tail. In cytotoxic T cells and mast cells, LAMP1 is expressed in the membranes of intracellular granules that contain effector molecules such as perforin, granzymes, eicosanoids, and histamine. A glycoform of LAMP1 known as M150 is expressed on the surface of activated macrophages where it promotes T cell co-stimulation and a Th1 biased immune response. Exposure of epithelial cells to pathogenic Neisseria bacteria induces the redistribution of LAMP1 to the cell surface where it can be cleaved by the Neisseria IgA1 protease.

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.

Interleukin 3 is a pleiotropic factor produced primarily by activated T cells that can stimulate the proliferation and differentiation of pluripotent hematopoietic stem cells as well as various lineage committed progenitors. This CSF induces granulocytes, macrophages, mast cells, stem cells, erythroid cells, eosinophils and megakaryocytes. IL-3 Protein, Human, Recombinant (His & Avi) is expressed in E. coli expression system with N-His-Avi tag. The predicted molecular weight is 16.9 kDa and the accession number is P08700.

Interleukin 3 is a pleiotropic factor produced primarily by activated T cells that can stimulate the proliferation and differentiation of pluripotent hematopoietic stem cells as well as various lineage committed progenitors. This CSF induces granulocytes, macrophages, mast cells, stem cells, erythroid cells, eosinophils and megakaryocytes. IL-3 Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with C-hFc tag. The predicted molecular weight is 41.6 kDa and the accession number is P08700.

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.

Interleukin 3 is a pleiotropic factor produced primarily by activated T cells that can stimulate the proliferation and differentiation of pluripotent hematopoietic stem cells as well as various lineage committed progenitors. This CSF induces granulocytes, macrophages, mast cells, stem cells, erythroid cells, eosinophils and megakaryocytes. IL-3 Protein, Human, Recombinant（E. coli） is expressed in E. coli expression system. The predicted molecular weight is 15.09 kDa and the accession number is AAC08706.