You searched for: Proteins and Peptides

Supplier: Thermo Scientific Chemicals

CAS No.: 198284-64-9
Molecular Formula: C60H101N15O17
Formula Weight: 1305.54
Storage Temperature: -30°C to -10°C
Physical Form: Solid
Appearance: White to off-white
Solubility: Soluble at 1mg/ml in 1% acetic acid
MDL No.: MFCD03456920

Supplier: Prosci

4-1BB is also known as CD137, tumor necrosis factor receptor superfamily member 9 (TNFRSF9), induced by lymphocyte activation (ILA), is a co-stimulatory molecule of the tumor necrosis factor (TNF) receptor superfamily. CD137 can be expressed by activated T cells, but to a larger extent on CD8 than on CD4 T cells. In addition, CD137 expression is found on dendritic cells, follicular dendritic cells, natural killer cells, granulocytes and cells of blood vessel walls at sites of inflammation. The best characterized activity of CD137 is its costimulatory activity for activated T cells. Crosslinking of CD137 enhances T cell proliferation, IL-2 secretion survival and cytolytic activity. Further, it can enhance immune activity to eliminate tumors in mice. CD137 can enhance activation-induced T cell apoptosis when triggered by engagement of the TCR/CD3 complex. In addition, 4-1BB/4-1BBL co-stimulatory pathway has been shown to augment secondary CTL responses to several viruses, and meanwhile augment anti-tumor immunity. 4-1BB thus is a promising candidate for immunotherapy of human cancer. CD137 has been shown to interact with TRAF2.

Supplier: Prosci

Interleukin-12 (IL12) is also known as natural killer cell stimulatory factor (NKSF), cytotoxic lymphocyte maturation factor (CLMF) , is a heterodimeric cytokine encoded by two separate genes, IL-12A (p35) and IL-12B (p40). IL12 is naturally produced by dendritic cells, macrophages and human B-lymphoblastoid cells (NC-37) in response to antigenic stimulation. IL-12 is involved in the differentiation of naive T cells into Th0 cells and plays an important role in the activities of natural killer cells and T lymphocytes.IL-12 also has anti-angiogenic activity, which means it can block the formation of new blood vessels. Interleukin-12 subunit alpha (IL12A) also known as NKSF1, CLMF1 and P35, IL12A shows significant sequence similarity to IL-6, G-CSF, and exerts biological activities only when the IL12B is co-expressed. IL12B deficient mice are resistant to the induction of experimental chronic inflammatory diseases whereas IL12A knock-out mice develop more severe forms, suggesting opposite functions of the two subunits in the outcome of chronic inflammatory diseases.

Supplier: G-Biosciences

A selection of individual protease inhibitors are offered for researchers who wish to design their own cocktails, supplement existing cocktails, or screen for specific proteases

Supplier: G-Biosciences

A selection of individual protease inhibitors are offered for researchers who wish to design their own cocktails, supplement existing cocktails, or screen for specific proteases

Supplier: Prosci

The EGFR subfamily of receptor tyrosine kinases is composed of EGFR, ErbB2, ErbB3 and ErbB4. The EGFR shares 43% - 44% aa sequence identity with the ECD of human EGFR subfamily. All these family members are type I transmembrane glycoproteins with an extracellular ligand binding domain. The extracellular ligand binding domain is containing two cysteine-rich domains separated by a spacer region and a cytoplasmic domain containing a membrane-proximal tyrosine kinase domain. Ligand binding could induce EGFR homodimerization and heterodimerization with ErbB2, resulting in cell signaling, heterodimerization tyrosine phosphorylation and kinase activation. It can bind EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, HB-EGF, epigen, and so on. Its signaling regulates multiple biological functions including cell proliferation, differentiation, motility, and apoptosis. EGFR can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGFR is overexpressed in different tumors. Several anti-cancer drugs use EGFR as target.

Supplier: Prosci

CD80 (B7-1) and CD86 (B7-2) together with their receptors CD28 and CTLA-4 constitute one of the dominant costimulatory pathways that regulate T cell and B cell responses. Although both CTLA-4 and CD28 can bind to the same ligands, CTLA-4 binds to B7-1 and B7-2 with a 20-100 fold higher affinity than CD28 and is involved in the down-regulation of the immune response. B7-1 is expressed on activated B cells, activated T cells and macrophages. B7-2 is constitutively expressed on interdigitating dendritic cells, Langerhans cells, peripheral blood dendritic cells, memory B cells, and germinal center B cells. Additionally, B7-2 is expressed at low levels on monocytes and can be up-regulated through interferon-gamma. B7-1 and B7-2 are both members of the immunoglobulin superfamily. It has been observed that both human and mouse B7-1 and B7-2 can bind to either human or mouse CD28 and CTLA-4, suggesting that there are conserved amino acids which form the B7-1/B7-2/CD28/CTLA-4 critical binding sites.

Supplier: Prosci

CD80 (B7-1) and CD86 (B7-2) together with their receptors CD28 and CTLA-4 constitute one of the dominant costimulatory pathways that regulate T cell and B cell responses. Although both CTLA-4 and CD28 can bind to the same ligands, CTLA-4 binds to B7-1 and B7-2 with a 20-100 fold higher affinity than CD28 and is involved in the down-regulation of the immune response. B7-1 is expressed on activated B cells, activated T cells, and macrophages. B7-2 is constitutively expressed on interdigitating dendritic cells, Langerhans cells, peripheral blood dendritic cells, memory B cells and germinal center B cells. Additionally, B7-2 is expressed at low levels on monocytes and can be up-regulated through interferon-gamma. B7-1 and B7-2 are both members of the immunoglobulin superfamily. It has been observed that both human and mouse B7-1 and B7-2 can bind to either human or mouse CD28 and CTLA-4, suggesting that there are conserved amino acids which form the B7-1/B7-2/CD28/CTLA-4 critical binding sites.

Supplier: Prosci

Interleukin-21 (IL-21) is a key factor in the transition between innate and adaptive immune responses secreted by activated T cells. The IL-21 receptor (IL-21R) is expressed in lymphoid tissue, in particular by NK, B, T and dendritic cells, macrophages and endothelial cells. Recent evidence suggests that IL-21 plays a supportive role in the proliferation of T and B cells and influences the cytolytic activity of natural killer cells. IL-21 has been shown to up-regulate genes associated with innate immunity and to inhibit the differentiation of naive T helper cells. IL-21 specifically inhibits IFN-gamma production from developing TH1 cells and is preferentially expressed by TH2 cells. Furthermore IL-21 has been identified as a growth and survival factor for human myeloma cells. IL-21/IL-21R interactions have a unique role in sequentially activating both innate and adaptive immune responses against poorly immunogenic tumors, leading to tumor rejection that is perforin dependent but IFN-gamma independent.

Supplier: New England Biolabs (NEB)

Sodium Orthovanadate (Vanadate, Na3VO4) is a commonly used general inhibitor for protein phosphotyrosyl phosphatases (PTPs). It is a competitive inhibitor. The inhibition by Vanadate is completely reversible upon the addition of EDTA or by dilution. Vanadate is activated for maximal inhibition of PTPs following the procedure described by J.A.Gordon. The PTP activities are conveniently separable from the protein phosphoseryl and phosphothreonyl phosphatase (PSP) activities inhibited by Fluoride and EDTA. Routinely Vanadate is used to preserve the protein tyrosyl phosphorylation state in cells, cell lysates, and protein tyrosine kinase assays.

Supplier: Thermo Scientific

Poly-HRP Streptavidin consists of streptavidin protein that is covalently conjugated to a polymerized form of horseradish peroxidase (HRP) enzyme. Streptavidin binds to biotin and the conjugated HRP polymer provides a high level of activity for detection using an appropriate substrate system. This particular Poly-HRP Streptavidin product has been used primarily in sandwich ELISA applications to improve the signal provided by typical (non-Poly) streptavidin-HRP conjugates.

Supplier: Prosci

BAFF is mainly produced by innate immune cells such as neutrophils, monocytes, macrophages, dendritic cells, follicular dendritic cells. T cells, activated B cells, some malignant B cells and also non-lymphoid cells like astrocytes, synoviocytes and epithelial cells can also produce BAFF. BAFF binds three distinct receptors (BAFF-R, TACI and BCMA) expressed predominantly on B cells, although activated T cells also express BAFF-R. BAFF is a master regulator of peripheral B cell survival, and together with IL-6, promotes Ig class-switching and plasma cell differentiation. Besides its major role in B cell biology, BAFF co-stimulates activated T cells. Deregulated expression of BAFF leads to autoimmune disorders in mice. In humans, elevated levels of soluble BAFF have been detected in the serum of patients with various autoimmune diseases such as Sjoegren syndrome, Rheumatoid arthritis (RA), Multiple sclerosis (MS) and Systemic Lupus Erythematosus (SLE). BAFF has also increased levels in some lymphoid cancers.

Supplier: Prosci

BAFF is mainly produced by innate immune cells such as neutrophils, monocytes, macrophages, dendritic cells, follicular dendritic cells. T cells, activated B cells, some malignant B cells and also non-lymphoid cells like astrocytes, synoviocytes and epithelial cells can also produce BAFF. BAFF binds three distinct receptors (BAFF-R, TACI and BCMA) expressed predominantly on B cells, although activated T cells also express BAFF-R. BAFF is a master regulator of peripheral B cell survival, and together with IL-6, promotes Ig class-switching and plasma cell differentiation. Besides its major role in B cell biology, BAFF co-stimulates activated T cells. Deregulated expression of BAFF leads to autoimmune disorders in mice. In humans, elevated levels of soluble BAFF have been detected in the serum of patients with various autoimmune diseases such as Sjoegren syndrome, Rheumatoid arthritis (RA), Multiple sclerosis (MS) and Systemic Lupus Erythematosus (SLE). BAFF has also increased levels in some lymphoid cancers.

Supplier: Prosci

Human VEGF121, also known as Vascular endothelial growth factor A, VEGFA, Vascular permeability factor, VPF and VEGF, is a homodimeric, heparin-binding glycoprotein which belongs to the platelet-derived growth factor (PDGF)/vascular endothelial growth factor (VEGF) family. VEGF-A is a glycosylated mitogen that specifically acts on endothelial cells and has various effects, including mediating increased vascular permeability, inducing angiogenesis, vasculogenesis, permeabilization of blood vessels and endothelial cell growth, increasing microvascular permeability, promoting cell migration and inhibiting apoptosis. Alternatively spliced transcript variants of VEGF-A encod either secreted or cell-associated isoforms. The lymphangiogenesis may be promoted by upregulation of VEGF121, which may in turn act in part via induction of VEGF-C. It binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth.

Supplier: G-Biosciences

A selection of individual protease inhibitors are offered for researchers who wish to design their own cocktails, supplement existing cocktails, or screen for specific proteases

Supplier: Prosci

C-X-C chemokine receptor type 4 is also known as fusin or CD184 (cluster of differentiation 184), CXCR4, CD184, D2S201E, FB22, HM89, HSY3RR, LAP3, LCR1, LESTR, NPY3R, NPYR, NPYRL, NPYY3R or WHIM. CXCR-4 is an alpha-chemokine receptor specific for stromal-derived-factor-1 (SDF-1 also called CXCL12), a molecule endowed with potent chemotactic activity for lymphocytes. This receptor is one of several chemokine receptors that HIV isolates can use to infect CD4+ T cells. HIV isolates that use CXCR4 are traditionally known as T-cell tropic isolates. Typically, these viruses are found late in infection. It is unclear as to whether the emergence of CXCR4 using HIV is a consequence or a cause of immunodeficiency.CXCR4 is upregulated during the implantation window in natural and hormone replacement therapy cycles in the endometrium, producing, in presence of a human blastocyst, a surface polarization of the CXCR4 receptors suggesting that this receptor is implicated in the adhesion phase of human implantation. SDF-1 and CXCR4 were believed to be a relatively "monogamous" ligand-receptor pair (other chemokines tend to use several different chemokine receptors in a fairly "promiscuous" manner). Recent evidence demonstrates ubiquitin is also a natural ligand of CXCR4. Chronic exposure to THC increased T lymphocyte CXCR4 expression on both CD4+ and CD8+ T lymphocytes. Drugs that block the CXCR4 receptor appear to be capable of "mobilizing" hematopoietic stem cells into the bloodstream as peripheral blood stem cells.

Supplier: MilliporeSigma

A potent, cell-permeable, and irreversible inhibitor of caspase-3 as well as caspase-6, caspase-7, caspase-8, and caspase-10.

Supplier: Prosci

Insulin-like growth factor 1 (IGF-1) is also known as somatomedin C, IGF1A, IGFI, sulfation factor, and is a hormone similar in molecular structure to insulin. It plays an important role in childhood growth and continues to have anabolic effects in adults. A synthetic analog of IGF-1, mecasermin is used for the treatment of growth failure. IGF-1 consists of 70 amino acids in a single chain with three intramolecular disulfide bridges. IGF-1 has a molecular weight of 7649 daltons. IGF-1 is produced primarily by the liver as an endocrine hormone as well as in target tissues in a paracrine/autocrine fashion. IGF-1 binds to at least two cell surface receptors: the Insulin-like growth factor 1 receptor, abbreviated as "IGF1R", and the insulin receptor. The IGF-1 receptor seems to be the "physiologic" receptor - it binds IGF-1 at significantly higher affinity than the IGF-1 that is bound to the insulin receptor. Like the insulin receptor, the IGF-1 receptor is a receptor tyrosine kinase - meaning it signals by causing the addition of a phosphate molecule on particular tyrosines. Its primary action is mediated by binding to its specific receptor IGF1R, present on many cell types in many tissues. Binding to the IGF1R, a receptor tyrosine kinase, initiates intracellular signaling; IGF-1 is one of the most potent natural activators of the AKT signaling pathway, a stimulator of cell growth and proliferation, and a potent inhibitor of programmed cell death. Insulin-like growth factor 1 has been shown to bind and interact with all the IGF-1 Binding Proteins (IGFBPs), of which there are six (IGFBP1-6). Specific references are provided for interactions with IGFBP3, IGFBP4 and IGFBP7.

Supplier: Prosci

Interleukin-33 (IL-33) was initially discovered as a nuclear factor NF-HEV abundantly expressed in high endothelial venules. It is a 30-32 kD pro-inflammatory protein with intracellular and extracellular activities and a chromatin-associated cytokine of the IL-1 family with high sequence and structural similarity to IL-1 and IL-18. IL-33 is highly and selectively expressed by high endothelial venule endothelial cells (HEVECs) in human tonsils, Peyers's patches, and lymph nodes. It contains a bipartite nuclear localization signal at the C-terminus, and is targeted to the nucleus when ectopically expressed in human umbilical vein endothelial cells (HUVECs) and HeLa cells. The C-terminal fragment, corresponding to mature IL-33, binds and triggers signaling. IL-33 mediates its biological effects via Toll-interleukin 1 (IL-1) receptor (TIR) domain-containing receptor ST2, activates NF-kappaB and MAP kinases, and drives production of T(H)2-associated cytokines from in vitro polarized T(H)2 cells. In vivo, IL-33 induces the expression of IL-4, IL-5, and IL-13 and leads to severe pathological changes in mucosal organs. Human IL-33 is 270 amino acids in length.

Supplier: Thermo Scientific Chemicals

Molecular Formula: C63H83N17O14
Formula Weight: 1302.44
Storage Temperature: -30°C to -10°C
Physical Form: Powder
Appearance: White to off-white
Solubility: Soluble in water at 1mg/ml
MDL No.: MFCD03452696

Supplier: New England Biolabs (NEB)

Fetuin is a glycoprotein containing sialylated N-linked and O-linked glycans that can be used as a positive control for endoglycosidase enzymes.

Supplier: Prosci

CD28 and CTLA-4 together with their ligands, CD80 (B7-1) and CD86 (B7-2), constitute one of the dominant costimulatory pathways that regulate T and B cell responses. CD28 and CTLA-4 are structurally homologous molecules that are members of the immunoglobulin (Ig) gene superfamily. Both CD28 and CTLA-4 are composed of a single Ig V-like extracellular domain, a transmembrane domain and an intracellular domain. CD28 and CTLA-4 are both expressed on the cell surface as disulfide-linked homodimers or as monomers. The genes encoding these two molecules are closely linked on human chromosome 2 and mouse chromosome 1. Mouse CD28 is expressed constitutively on virtually 100% of mouse T cells and on developing thymocytes. Cell surface expression of mouse CD28 is downregulated upon ligation of CD28 in the presence of PMA or PHA. In contrast, CTLA-4 is not expressed constitutively but is upregulated rapidly following T cell activation and CD28 ligation. Cell surface expression of mouse CTLA-4 peaks approx.y 48 hours after activation. Although both CTLA-4 and CD28 can bind to the same ligands, CTLA-4 binds to B7-1 and B7-2 with a 20-100 fold higher affinity than CD28. CD28/B7 interaction has been shown to prevent apoptosis of activated T cells via the upregulation of bcl-XL. CD28 ligation has also been shown to regulate Th1/Th2 differentiation.

Supplier: Prosci

Interleukin-15 (IL-15) has a broad spectrum of biological activities. It is crucial for the development, proliferation, survival and differentiation of multiple cells from both innate and adaptive immune systems. IL-15 up-regulation has a central role in the development of several autoimmune or chronic inflammatory disorders. Targeting IL-15 or its receptor may have a valuable impact on the treatment of immune-mediated diseases. IL-15 participates in the development of important immune antitumor mechanisms. It activates CD8(+) T cells, natural killer (NK) cells, NK T cells, and can promote the formation of antitumor antibodies. IL-15 can also protect T effector cells from the action of T regulatory cells and reverse tolerance to tumor-associated antigens. In pre-clinical studies IL-15 has been found to demonstrate potentiated antitumor effects following pre-association with IL-15Ralpha, or when used in combination with chemotherapy, adoptive therapy, monoclonal antibodies, and tumor vaccines.

Supplier: Prosci

CD152 (CTLA-4) and CD28, together with their ligands B7-1 and B7-2, constitute one of the dominant costimulatory pathways that regulate T and B cell responses. CD152 and CD28 are structurally
homologous molecules that are members of the immunoglobulin (Ig) gene superfamily. Both CD152 and CD28 are composed of a single Ig V-like extracellular domain, a transmembrane domain and an
intracellular domain. CD152 and CD28 are both expressed on the cell surface as disulfide-linked homodimers or as monomers. CD152 was originally identified as a gene that was specifically expressed by
cytotoxic T lymphocytes. However, CD152 transcripts have since been found in both Th1 and Th2, and CD4+ and CD8+ T cell clones. Whereas, CD28 expression is constitutive on the surfaces of 95% of CD4+
T cells and 50% of CD8+ T cells and is down regulated upon T cell activation, CD152 expression is upregulated rapidly following T cell activation and peaks approximately 24 hours following activation.
Although both CD152 and CD28 can bind to the same ligands, CD152 binds to B71 and B72 with 20-100-fold higher affinity than CD28.

Supplier: Prosci

Tumor Necrosis Factor- alpha (TNF- alpha) is secreted by macrophages, monocytes, neutrophils, T-cells, and NK-cells following stimulation by bacterial LPS. Cells expressing CD4 secrete TNF- alpha while cells that express CD8 secrete little or no TNF- alpha. Synthesis of TNF- alpha can be induced by many different stimuli including interferons, IL2, and GM-CSF. The clinical use of the potent anti-tumor activity of TNF- alpha has been limited by the proinflammatory side effects such as fever, dose-limiting hypotension, hepatotoxicity, intravascular thrombosis, and hemorrhage. Designing clinically applicable TNF- alpha mutants with low systemic toxicity has been of intense pharmacological interest. Human TNF- alpha that binds to murine TNF-R55 but not murine TNF-R7, exhibits retained anti-tumor activity and reduced systemic toxicity in mice compared with murine TNF- alpha, which binds to both murine TNF receptors. Based on these results, many TNF- alpha mutants that selectively bind to TNF-R55 have been designed. These mutants displayed cytotoxic activities on tumor cell lines in vitro and have exhibited lower systemic toxicity in vivo. Recombinant Human TNF- alpha High Active Mutant differs from the wild-type by amino acid subsitution of amino acids 1-7 with Arg8, Lys9, Arg10 and Phe157. This mutant form has been shown to have increased activity with less inflammatory side effects in vivo.

Supplier: Prosci

PDGFs are disulfide-linked dimers consisting of two 12.0-13.5 kDa polypeptide chains, designated PDGF-A and PDGF-B chains. The three naturally occurring PDGFs; PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGFs are stored in platelet α-granules and are released upon platelet activation. The PDGFs are involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGFs have been identified and named PDGFR-α and PDGFR-β. PDGFR-α is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-β interacts with only PDGF-BB and PDGF-AB. Recombinant human PDGF-BB is a 24.3 kDa disulfide-linked homodimer of two B chains (218 total amino acids). Recombinant murine PDGF-BB is a 24.4 kDa disulfide-linked homodimer of two B chains (218 total amino acids).

Supplier: Thermo Scientific Chemicals

CAS No.: 169332-60-9
Molecular Formula: C20H30N4O11
Formula Weight: 502.47
Storage Temperature: -30°C to -10°C
Physical Form: Powder
Appearance: White
MDL No.: MFCD00671412

Supplier: Prosci

Interleukin-27 (IL-27) is a heterodimeric group 2 receptor ligand molecule that belongs to the IL-6/IL-12 family of long type I cytokines. It is composed of EBI3 (EBV-induced gene 3), a 34 kDa glycoprotein that is related to the p40 subunit of IL-12 and IL-23, and p28, the cloned 28 kDa glycoprotein that is related to the p35 chain of IL-12. IL-27 is expressed by monocytes, endothelial cells and dendritic cells. IL-27 binds to and signals through a heterodimeric receptor complex composed of WSX1 (TCCR) and gp130. Evidence suggests IL-27 interacts only with WSX-1. IL-27 has both anti- and proinflammatory properties. As an antiinflammatory, IL-27 seems to induce a general negative feedback program that limits T and NK-T cell activity. At the onset of infection, IL-27 induces an IL-12 receptor on naie CD4+ T cells, making them susceptible to subsequent IL-12 activity (and possible Th1 development). Notably, IL-12 family cytokines are both induced and inhibited by bacterial products. Microbes promote IL-27 secretion through TLR4, and also block IL-27 production via C5a induction.

Supplier: Prosci

CD276 (B7-H3) is a member of the B7/CD28 superfamily of costimulatory molecules serving as an accessory modulator of T cell response. B7 family molecules, which are expressed on antigen-presenting cells and display extracellular regions containing immunoglobulin (Ig) variable (V)- and constant (C)-like domains, are known to modulate T cell receptor (TCR)-mediated T cell activation by providing co-signals that are either stimulatory or inhibitory. B7-H3 provides a stimulatory signal to T cells. However, recent studies suggest a negative regulatory role for B7-H3 in T cell responses. B7-H3 inhibited T cell proliferation mediated by antibody to T cell receptor or allogeneic antigen-presenting cells. B7-H3 is a negative regulator that preferentially affects T(H)1 responses. B7-H3 may play an important role in muscle-immune interactions, providing further evidence of the active role of muscle cells in local immunoregulatory processes. Recently, B7-H3 expression has also been found in a variety of different human cancers, including prostate cancer, clear cell renal cell carcinoma (ccRCC), non-small-cell lung cancer (NSCLC), pancreatic cancer, gastric cancer, ovarian cancer, colorectal cancer (CRC) and urothelial cell carcinoma. B7-H3 was expressed in some human cancers and correlated with poor outcome of cancer patients.

Supplier: Prosci

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 (159 aa) and sfTSLP (63 aa) produced by alternative splicing . lfTSLP (159aa) 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. Thymic stromal lymphopoietin (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- alpha chain (IL-7R alpha), 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.