keratinocytes

Immunoglobulin Superfamily Member 8 (IGSF8) is a single-pass membrane protein. IGSF8 contains four Ig-like C2 type domains. The Ig-like C2-type domains 3 and 4 are required for interactions with CD81. IGSF8 may regulate proliferation and differentiation of keratinocytes. IGSF8 may participate in the regulation of neurite outgrowth and maintenance of the neural network in the adult brain. It also may play a role on integrin-dependent morphology and motility functions.

Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-9 (gelatinase B) can degrade a broad range of substrates including gelatin, collagen types IV and V, elastin and proteoglycan core protein. It is believed to act synergistically with interstitial collagenase (MMP1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-9 is produced by keratinocytes, monocytes, macrophages and PMN leukocytes. MMP-9 is present in most cases of inflammatory responses. Structurally, MMP-9 may be divided into five distinct domains: a prodomain which is cleaved upon activation, a gelatinbinding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a prolinerich linker region, and a carboxyl terminal hemopexinlike domain.

Podoplanin is a type-1 transmembrane protein that belongs to Podoplanin family. PDPN expressed in various specialized cell types throughout the body. It highly expressed in placenta, lung, skeletal muscle and brain, weakly expressed in brain, kidney and liver. In placenta, PDPN expressed on the apical plasma membrane of endothelium, in lung, expressed in alveolar epithelium. PDPN physiological function is related to its mucin-type character. PDPN may be involved in cell migration and/or actin cytoskeleton organization. When expressed in keratinocytes, induces changes in cell morphology with transfected cells showing an elongated shape, numerous membrane protrusions, and major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion. It requires for normal lung cell proliferation and alveolus formation at birth and Induces platelet aggregation. Nevertheless, it doesn’t have any effect on amino acid transport and the aquaporin-type water channels.

Interleukin-21 receptor (IL-21R) is a type I transmembrane glycoprotein within the class I cytokine receptor family, type 4 subfamily. IL-21R is expressed mainly on B cells, NK cells, and activated T cells, but is also found on dendritic cells, alternatively activated macrophages, intestinal lamina propria fibroblasts and epithelial cells, and keratinocytes. Both IL-21 and IL-4 are necessary for efficient B cell IgG1 production and normal germinal center architecture. B cell IL-21 R engagement induces Blimp-1(which mediates plasma cell differentiation), and is important for memory responses. IL-21R engagement on mouse NK cells enhances their cytotoxic activity and IFN-γ production. IL-21R engagement on CD8+ T cells aids control of viral infection and tumor growth; IL-21R is also necessary for sufficient numbers of regulatory T cells to combat chronic inflammation. IL-21R expression is often up-regulated in allergic skin inflammation, systemic lupus erythematosus and diffuse large B cell lymphoma (DLBCL).

Fatty acid-binding protein, also known as Epidermal-type fatty acid-binding protein, Fatty acid-binding protein 5, Psoriasis-associated fatty acid-binding protein homolog, E-FABP and FABP5, is a cytoplasm protein which Belongs to thecalycin superfamily and Fatty-acid binding protein (FABP) family. Fatty acid-binding proteins ( FABPs ) are postulated to serve as lipid shuttles that solubilize hydrophobic fatty acids and deliver them to appropriate intracellular sites. E-FABP / FABP5 is predominantly expressed in keratinocytes and is overexpressed in the actively proliferating tissue characteristic of psoriasis and wound healing. E-FABP / FABP5 exhibits an important role in binding free fatty acids, as well as regulating lipid metabolism and transport. E-FABP / FABP5 has high specificity for fatty acids. It has highest affinity for C18 chain length. Decreasing the chain length or introducing double bonds reduces the affinity of FABP5. E-FABP / FABP5 may be involved in keratinocyte differentiation.

FGFBP3 is a member of the fibroblast growth factor-binding protein family. Members of this family binds and activates FGF-1 and FGF-2, thereby contributing to tumor angiogenesis. Fibroblast growth factors (FGFs) are important regulators of cell migration, proliferation and differentiation, e.g., during embryogenesis and wound healing, and under several pathological conditions including tumor growth and tumor angiogenesis. Expression of FGF-BP increases after injury to murine and human skin, in particular in keratinocytes. This upregulation is most likely achieved by major keratinocyte mitogens present at the wound site. FGFBP3 is a positive regulator of fibroblast growth factor receptor signaling pathway and vascular permeability. It interacts with 2,3,7,8-tetrachlorodibenzodioxine, benzopyrene and valproic acid. FGFBP3 also exhibits fibroblast growth factor binding (orthology) and heparin binding (orthology).

Interleukin-18 (IL-18）is a protein which belongs to the IL-1 family. It is expressed as a 24 kDa precursor by endothelial and epithelial cells, keratinocytes, gamma δ T cells, and phagocytes. Mature mouse IL-18 shares 63% and 91% amino acid sequence identity with mouse and rat IL-18, respectively. IL-18 binds to the widely expressed IL-18 R alpha which recruits IL-18 R beta to form the signaling receptor complex. Its bioactivity is negatively regulated by interactions with IL-18 binding proteins and virally encoded IL-18BP homologs. It augments natural killer cell activity in spleen cells and stimulates interferon gamma production in T-helper type I cells. In the presence of IL-12 or IL-15, IL-18 enhances anti-viral Th1 immune responses by inducing IFN-gamma production and the cytolytic activity of CD8+ T cells and NK cells. In the absence of IL-12 or IL-15, however, IL-18 promotes production of the Th2 cytokines IL-4 and IL-13 by CD4+ T cells and basophils.

Osteoactivin is an intracellular glycoprotein belongs to the NMB/pMEL-17 family, which is asscociated with cell endosomal/lysomal compartments. Human Osteoactivin is a 560 amino acid type I transmembrane protein, and one alternate splice form shows a 12 amino acid insert between amino acid 339-340. An additional 206 amino acid isoform shows a mutation at position 181 that results in a 26 amino acid substitution for the C-terminal 380 amino acids. Cells knowns to express Osteoactivin include fibroblast, osteoblasts, myeloid dendritic cell, melanocytes, plus fetal chondrocytes and stratum basale keratinocytes, macrophages/keratinocytes.

Mouse Interleukin 33 (IL-33) is a 30 kDa proinflammatory cytokine which may also regulates gene transcription in producer cells. IL-33 is constitutively expressed in smooth muscle and airway epithelia. IL-33 was identified based on sequence and structural homology with IL-1 family cytokines. It is up‑regulated in arterial smooth muscle, dermal fibroblasts, and keratinocytes following IL-1 alpha or IL‑1 beta stimulation. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1. BindingIL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces the expression of IL-4, IL-5, IL-13 and also leads to severe pathological changes in mucosal organs.

β-Defensin 1 (DEFB1) is a member of the β-defensin family, which is highly expressed by epithelial cells. β-defensins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal peptide. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. β-defensin 1 is an antimicrobial peptide implicated in the resistance of epithelial surfaces to microbial colonization. Defects in β-Defensin-1 contribute to asthma diagnosis, with apparent gender-specific effects in human. β-defensin 1 may also play a role in the pathogenesis of severe sepsis. In addition, β-defensin 1 is associated with induction profiles in gingival keratinocytes.

Podoplanin belongs to the podoplanin family, also known as Glycoprotein 38. Podoplanin is synthesized as a 172 amino acid (aa) precursor with a 22 aa signal sequence, a 119 aa extracellular domain (ECD), a 21 aa transmembrane region, and a short, 10 aa cytoplasmic tail. Detected at high levels in lung and brain, at lower levels in kidney, stomach, liver, spleen and esophagus, and not detected in skin and small intestine. Expressed in epithelial cells of choroid plexus, ependyma, glomerulus and alveolus, in mesothelial cells and in endothelia of lymphatic vessels. Also expressed in stromal cells of peripheral lymphoid tissue and thymic epithelial cells. Detected in carcinoma cell lines and cultured fibroblasts. Expressed at higher levels in colon carcinomas than in normal colon tissue. It can interacts with CLEC1B; the interaction is independent of CLEC1B glycosylation and activates CLEC1B. It may be involved in cell migration and/or actin cytoskeleton organization. When expressed in keratinocytes, induces changes in cell morphology with transfected cells showing an elongated shape, numerous membrane protrusions, major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion. Required for normal lung cell proliferation and alveolus formation at birth. Ligand for CLEC1B, a platelet receptor. Induces platelet aggregation. Does not have any effect on folic acid or amino acid transport. Does not function as a water channel or as a regulator of aquaporin-type water channels.

Interleukin 18 binding protein (IL-18BP) is a physiological inhibitor that acts through binding to the receptor-binding site of IL-18. IL-18 stimulates INF-γ, which then stimulates 18BP production via NF-κB. The interaction between IL-18 and IL-18BP has a significant role in the inflammation process. IL-18 BPs have four isoforms, a, b, c and d, which are spliced by different ways. The IL-18 BP isoforms a and c each contain one immunoglobulin (Ig)-like C2-type domain which is essential to the binding and neutralizing properties of the binding proteins. The IL-18 BP isoforms b and d lack a complete Ig domain. The expression of IL-18 and the IL-18BP are indentified in immune tissues such as the spleen, but also in nonimmune cells including keratinocytes.

Mothers against decapentaplegic homolog 3(SMAD3) is a cytoplasm protein which belongs to the dwarfin/SMAD family. Smad proteins undergo rapid nuclear translocation upon stimulation by transforming growth factor and in so doing transduce the signal into the nucleus. Receptor-regulated SMAD is an intracellular signal transducer and transcriptional modulator activated by TGF-beta and activin type 1 receptor kinases. SMAD3 binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. It also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. SMAD3 has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive.

Her3, also called ErbB3, is a type I membrane glycoprotein that is a member of the ErbB family of tyrosine kinase receptors.Her3 is expressed in keratinocytes, melanocytes, skeletal muscle cells, embryonic myoblasts and Schwann cells. Monomeric Her3 serves as a low affinity receptor for the heregulins (HRG). HER3/ERBB3 Protein, Human, Recombinant (His & Avi), FITC-Labeled is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 71.6 kDa and the accession number is P21860-1.

Her3, also called ErbB3, is a type I membrane glycoprotein that is a member of the ErbB family of tyrosine kinase receptors.Her3 is expressed in keratinocytes, melanocytes, skeletal muscle cells, embryonic myoblasts and Schwann cells. Monomeric Her3 serves as a low affinity receptor for the heregulins (HRG). HER3/ERBB3 Protein, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 71.6 kDa and the accession number is P21860-1.

Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane. Sprr2a1 Protein, Mouse, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 13.4 kDa and the accession number is Q9CQK8.

Serpins are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases (serine protease inhibitors). Over 1 serpins have been identified.Mouse SerpinB3, also known as Squamous cell carcinoma antigen 1, SCCA-1, SERPINB3, SCCA and SCCA1, is a cytoplasm protein that belongs to the serpin family and Ov-serpin subfamily. SerpinB3 may act as a protease inhibitor to modulate the host immune response against tumor cells. Mouse SerpinB3a and SerpinB3b, but not Serpinb3c, are functional, inhibiting both serine and cysteine proteinases with different inhibitory profiles due to the difference of two amino acids in their reactive site loops. SerpinB3a is ubiquitously expressed in most tissues, whereas expression of SerpinB3b is limited to keratinocytes. SerpinB3a and SerpinB3b may play different roles by inhibiting intrinsic or extrinsic proteinases with different expression distributions and different inhibitory profiles.

The name Pancreasin because it is transcribed strongly in the pancreas. This secreted, tryptic serine protease, also known as Marapsin or PRSS27 (Protease, serine, 27), is a member of the peptidase S1 family. Pancreasin is inhibited by benzamidine and leupeptin but resists several classic inhibitors of trypsin. Marapsin was constitutively expressed in nonkeratinizing stratified squamous epithelia of human esophagus, tonsil, cervix, larynx, and cornea. In fact, marapsin was the second most strongly up-regulated protease in psoriatic lesions, where expression was localized to the upper region of the hyperplastic epidermis. Similarly, in the hyperproliferative epithelium of regenerating murine skin wounds, marapsin localized to the suprabasal layers, where keratinocytes undergo squamous differentiation. Marapsin's restricted expression, localization, and cytokine-inducible expression suggest a role in the terminal differentiation of keratinocytes in hyperproliferating squamous epithelia.

CALCB, also known as CGPR and calcitonin 2, belongs to the calcitonin family. CALCB is a calcitonin (CT) peptide which may play a role in the mediation of human inflammatory diseases. It is highly expressed in the skin, blood, and cerebrospinal fluid. CGRP immunolabeling (IL) was detected in epidermal keratinocytes at levels that were especially high and widespread in the skin of humans from locations afflicted with postherpetic neuralgia (PHN) and complex region pain syndrome type 1 (CRPS), of monkeys infected with simian immunodeficiency virus, and of rats subjected to L5/L6 spinal nerve ligation, sciatic nerve chronic constriction, and subcutaneous injection of complete Freund's adjuvant. Increased CGRP-IL was also detected in epidermal keratinocytes of transgenic mice with keratin-14 promoter driven overexpression of noggin, an antagonist to BMP-4 signaling. CGPR dilates a variety of vessels including the coronary, cerebral and systemic vasculature.

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.

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.

Protein S100-A7, also known as S100 calcium-binding protein A7, Psoriasin, S100A7, and PSOR1, is a secreted protein which belongs to theS-100 family. S100A7 was first isolated from skin involved by psoriasis, which can be induced in cultured squamous epithelial cells. S100A7 is expressed by both normal cultured and malignant keratinocytes and malignant breast epithelial cells within ductal carcinoma in situ, suggesting an association with abnormal pathways of differentiation. S100A7 plays a role in the pathogenesis of inflammatory skin disease, as a chemotactic factor for hematopoietic cells. It also plays a role in early stages of breast tumor progression in association with the development of the invasive phenotype.

Koebnerisin is also known as protein S100-A7A (S100A7A), S100 calcium-binding protein A7-like 1 (S100A7L1) or S100 calcium-binding protein A15 (S100A15). Human S100A7A / S100A15 is a novel member of the S100 family of EF-hand calcium-binding proteins and was recently identified in psoriasis, where it is significantly upregulated in lesional skin. S100A7 is expressed by both normal cultured and malignant keratinocytes and malignant breast epithelial cells within ductal carcinoma in situ, suggesting an association with abnormal pathways of differentiation. S100A7 plays a role in the pathogenesis of inflammatory skin disease, as a chemotactic factor for hematopoietic cells. It also plays a role in early stages of breast tumor progression in association with the development of the invasive phenotype. The association of the 11.2 kDa S100A7A / S100A15 with psoriasis suggests that it contributes to the pathogenesis of the disease and could provide a molecular target for therapy.

Phosphoserine phosphatase (PSPH) belongs to a subfamily of the phosphotransferases. PSPH is the rate-limiting enzyme in l-serine biosynthesis. It has previously been found that Phosphoserine phosphatase (PSPH) plays a role in epidermal homeostasis. Phosphoserine phosphatase (PSP) catalyzes the hydrolysis of phosphoserine to serine. Phosphoserine phosphatase (PSPH) expression has been examined in human-mouse somatic cell hybrids retaining different combination of human chromosomes. Phosphoserine phosphatase (PSPH) is expressed throughout the proliferative layer of the epidermis and hair follicles in rodent and human skin and is highly induced in SCC. In keratinocytes, Phosphoserine phosphatase (PSPH) is a cytoplasmic protein that primarily localizes to endosomes and is present primarily as a homodimer. Knock down of Phosphoserine phosphatase (PSPH) dramatically diminished SCC cell proliferation and cyclin D1 levels in the presence of exogenous of l-serine production suggesting a non-canonical role for Phosphoserine phosphatase (PSPH) in epithelial carcinogenesis. Phosphoserine phosphatase (PSPH) is highly induced in proliferative normal keratinocytes and skin tumors. Phosphoserine phosphatase (PSPH) appears to be critical for the proliferation of SCC cells; however, this phenomenon may not involve the phosphoserine metabolic pathway.

Human Interleukin 31 (IL-31) is a cytokine containing a four-helix bundle structure. It shares several structural and functional characteristics with IL-6, Oncostatin M, LIF, and Cardiotrophin-1. Human IL-31 cDNA encodes a 164 amino acid precursor that contains a 23 amino acid signal peptide and a 141 amino acid mature protein. Human and mouse IL-31 share 24% sequence identity in the mature region. IL-31 is mainly associated with activated T cells and is preferentially expressed by type 2 helper T cells (Th2). IL-31 signals via a heterodimeric receptor complex composed of a gp130 related molecule termed IL-31RA (also GPL and GLMR) and an Oncostatin M receptor (OSM Rβ). The IL-31 receptor is constitutively expressed by keratinocytes and upregulated by IFNγ on monocytes. GPL/OSMR signaling is a strong activator of STAT3 and STAT5, and can also activate STAT1, Jak1, and Jak2 signaling pathways. IL-31 regulated immune responses have been implicated in skin physiology and inflammatory skin diseases. Studies have shown that IL31 induces severe pruritis (itching) and dermatitis in transgenic mice.

Her3, also called ErbB3, is a type I membrane glycoprotein that is a member of the ErbB family of tyrosine kinase receptors.Her3 is expressed in keratinocytes, melanocytes, skeletal muscle cells, embryonic myoblasts and Schwann cells. Monomeric Her3 serves as a low affinity receptor for the heregulins (HRG). HER3/ERBB3 Protein, Cynomolgus/Rhesus macaque, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 69.54 kDa and the accession number is XP_005571238.1.

Cross-linked envelope protein of keratinocytes. SPRR3 Protein, Human, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 34.0 kDa and the accession number is Q9UBC9.

Calmodulin-like protein 5, also known as Calmodulin-like skin protein, CALML5 and CLSP, is a protein which contains fourEF-hand domains. CALML5 / CLSP is particularly abundant in the epidermis where its expression is directly related to keratinocyte differentiation.The expression is very low in lung. CALML5 / CLSP binds calcium. It may be involved in terminal differentiation of keratinocytes. Coxsackievirus and adenovirus receptor (CAR) is a member of the immunoglobulin (Ig) superfamily and a component of epithelial tight junction. CAR functions as a primary receptor for coxsackievirus B and adenovirus (Ad) infection. CALML5 / CLSP is closely related to CAR. The structure and dynamics of human calmodulin-like skin protein CALML5 / CLSP have been characterized by NMR spectroscopy. The mobility of CALML5 / CLSP has been found to be different for the N-terminal and C-terminal domains. The N-terminal domain is characterized by four stable helices, which experience large fluctuations. This is shown to be due to mutations in the hydrophobic core. The overall N-terminal domain behavior is similar both in the full-length protein and in the isolated domain.

Integrin-linked kinase-associated serine/threonine phosphatase 2C, also known as ILKAP, is a cytoplasm protein that belongs to the PP2C family. ILKAP contains one PP2C-like domain. ILKAP is widely expressed. Highest levels expressed in striated muscle. Much lower levels are evident in various smooth muscle tissues. ILKAP may play a role in the regulation of cell cycle progression via dephosphorylation of its substrates whose appropriate phosphorylation states might be crucial for cell proliferation. ILKAP selectively associates with integrin-linked kinase (ILK), to modulate cell adhesion and growth factor signaling. ILKAP inhibits the ILK-GSK3B signaling axis and may play an important role in inhibiting oncogenic transformation. Integrin-linked kinase ( ILK ) plays key roles in a variety of cell functions, including cell proliferation, adhesion, and migration. Within the cell, ILK localizes to multiple sites, including the cytoplasm, focal adhesion complexes that mediate cell adhesion to extracellular substrates, as well as cell-cell junctions in epidermal keratinocytes. Nuclear ILK can be rapidly exported into the cytoplasm through a CRM1-dependent pathway, and its export is enhanced by the type 2C protein phosphatase ILKAP. Nuclear localization of ILK in epidermal keratinocytes is associated with increased DNA synthesis, which is sensitive to inhibition by ILKAP.

May play a role in the integrity of hemidesmosome and the attachment of basal keratinocytes to the underlying basement membrane.; The 120 kDa linear IgA disease antigen is an anchoring filament component involved in dermal-epidermal cohesion. Is the target of linear IgA bullous dermatosis autoantibodies. COL17A1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 28.4 kDa and the accession number is Q9UMD9.

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) 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.

Fibroblast growth factor 7 (FGF7) is a secreted protein which is mainly located in epithelial cells and belongs to the heparin-binding growth factors family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF7 is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes but not in fibroblasts and endothelial cells. It is possible major paracrine effector of normal epithelial cell proliferation.

Fatty acid-binding protein 5 (FABP5) is a cytoplasm protein that belongs to the fatty-acid binding protein (FABP) family of calycin superfamily. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids. FABP5 can be expressed in keratinocytes, and is highly expressed in psoriatic skin. FABP5 has been shown to be involved in keratinocyte differentiation. FABP5 has high specificity for fatty acids, the highest affinity for C18 chain length. FABP5 can decrease the chain length or introduce double bonds to reduce the affinity.

Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane. SPRR2B Protein, Human, Recombinant (His & Myc) is expressed in yeast with N-10xHis and C-Myc tag. The predicted molecular weight is 12.0 kDa and the accession number is P35325.

SerpinB6, also known as Cytoplasmic antiproteinase, Peptidase inhibitor 6, Placental thrombin inhibitor, SERPINB6 and PI-6, is a cytoplasm protein that belongs to the serpin family and Ov-serpin subfamily. SerpinB6 / PI-6 is an inhibitor of cathepsin G, kallikrein-8 and thrombin. It may play an important role in the inner ear in the protection against leakage of lysosomal content during stress and loss of this protection results in cell death and sensorineural hearing loss. SerpinB6 / PI-6 is expressed in keratinocytes (at protein level). It is also found in placenta, cardiac muscle, lung, liver, kidney and pancreas. SerpinB6 / PI-6 is expressed in the inner ear hair cells. It’s expressed abundantly by normal mast cells in different tissues and by mast cells in mastocytoma lesions. SerpinB6 / PI-6 may be involved in the regulation of serine proteinases present in the brain or extravasated from the blood. Defects in SerpinB6 are the cause of deafness autosomal recessive type 91 which is a form of non-syndromic deafness characterized by progressive and age-dependent sensorineural hearing loss. Vestibular function is normal.