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Proteins are used in routine laboratory procedures such as binding enzymes or coupling peptides to carrier proteins. These kits, mixture solutions, and collagen matrices fulfill a myriad of essential laboratory functions for developing relationships between proteins and other cellular components. The stimulating proteins offered have various amino acid arrangements and functions to fulfill any sample manipulation for testing purposes in any field.
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Description:
Wnt signaling plays a critical role in embryonic development, and genetic aberrations. Frizzled2 (Fzd2) is a receptor for wingless-type MMTV integration site family members (Wnts), the aberrant overexpression of which has been noted to contribute to cancer metastasis. Frizzled2 (Fzd2) and its ligands Wnt5a/b are elevated in metastatic liver, lung, colon, and breast cancer cell lines and in high-grade tumors and that their expression correlates with markers of epithelial-mesenchymal transition (EMT). It is also shown that Frizzled-2 expression is greater in embryonic than adult tissues, with heart, brain, lung, kidney and gut showing the highest levels.
Description:
T cell immunoglobulin and mucin domain-3 (TIM3), also called hepatitis A virus cellular receptor 2 (HAVCR2), is a transmembrane glycoprotein of the TIM family of immune regulating molecules and plays an important role in the Th1-mediated immune response. TIM3 is expressed on the Th1 cells, CD8 T-cells, monocytes, and dendritic cells, but not on Th2 cells. TIM3 expressed by monocytes and dendritic cells facilitates phagocytosis of apoptotic cells and up-regulates cross-presentation of apoptotic cell-associated antigens through interaction with phosphatidylserine. Engagement of TIM3 by its ligand galectin-9 induces a range of immunosuppressive functions which enhance immune tolerance and inhibit anti-tumor immunity. Stimulation of TIM3 with an agonistic antibody promotes inflammation through the activation of innate immune cells. TIM3 is also regarded as a potential target molecule for immunotherapy. TIM3 and programmed cell death 1 (PD-1) as two important coinhibitory regulators of T cell responses, have been implicated with the T-cell dysfunction or exhaustion associated with chronic HBV infection including HBV-related HCC.
Description:
V-set and immunoglobulin domain-containing protein 4(VSIG4) is a transmembrane protein contains a signal peptide, a V-type Ig-like domain, a C2-type Ig-like domain, several potential O-glycosylation sites, and an intracellular domain with 2 potential phosphorylation sites and is structurally related to the B7 family of immune regulatory proteins. This protein is also a receptor for the complement component 3 fragments C3b and iC3b.The main function is strong negative regulator of T-cell proliferation and IL2 production and it is also potent inhibitor of the alternative complement pathway convertases. It abundantly expressed in several fetal tissues such as adult tissues, highest expression in lung and placenta and it also expressed in resting macrophages.
Description:
Hepatitis A virus cellular receptor 2(HAVCR2)is a single-pass type I membrane protein and it contains 1 Ig-like V-type (immunoglobulin-like) domain. The protein belongs to the immunoglobulin superfamily, and TIM family of proteins. The protein regulates macrophage activation. It inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and promotes immunological tolerance. It may be also involved in T-cell homing and it is receptor for LGALS9. CD4 (MIM 186940)-positive T helper lymphocytes can be divided into types 1 (Th1) and 2 (Th2) on the basis of their cytokine secretion patterns. Th1 cells and their associated cytokines are involved in cell-mediated immunity to intracellular pathogens and delayed-type hypersensitivity reactions, whereas Th2 cells are involved in the control of extracellular helminthic infections and the promotion of atopic and allergic diseases. The 2 types of cells also cross-regulate the functions of the other. TIM3 is a Th1-specific cell surface protein that regulates macrophage activation and enhances the severity of experimental autoimmune encephalomyelitis in mice.
Description:
TMX2 is a single-pass type I membrane protein and contains 1 thioredoxin domain. Thioredoxin plays an important role in various cellular processes through redox regulation. The molecular cloning and characterisation of one member of the thioredoxin superfamily, designated as TMX2.The TMX2 cDNA consists of 1644 nucleotides and contains an open reading frame encoding a protein of 372 amino acids with a predicted molecular mass of 42.5 kDa and an isoelectric point of 8.94. The TMX2 protein may possess an N-terminal signal peptide, a potential transmembrane domain, an Myb DNA-binding domain repeat signature, a thioredoxin consensus pattern, an endoplasmic reticulum (ER) membrane retention signal (KKXX-like motif), and a dileucine motif in the tail.
Description:
Inducible Co-Stimulator Ligand (ICOSLG) belongs to the immunoglobulin superfamily. ICOSLG contains Ig-like C2-type (immunoglobulin-like) domain and 1 Ig-like V-type (immunoglobulin-like) domain. ICOSLG acts as a costimulatory signal for T-cell proliferation and cytokine secretion, it also induces B-cell proliferation and differentiation into plasma cells. It could play an important role in mediating local tissue responses to inflammatory conditions, as well as in modulating the secondary immune response by co-stimulating memory T-cell function. ICOSLG is widely expressed lymph nodes, leukocytes and spleen, detected on activated monocytes and dendritic cells.
Description:
BTLA is a type I transmembrane glycoprotein of the CD28 family of T cell costimulatory molecules. BTLA functions as a coinhibitor on activated T cells and on B cells and dendritic cells. The extracellular domain (ECD) of this Ig superfamily protein contains one V-type Ig-like domain, which interacts with HVEM.
Description:
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.
Description:
Herpesvirus entry mediator (HVEM) is also known as TNFRSF14, TR2 (TNF receptorlike molecule) and ATAR (another TRAF associated receptor), is a type I membrane protein belonging to the TNF/NGF receptor superfamily. HVEM expression has been detected in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. The extracellular domain of HVEM has been shown to interact directly with the herpes simplex virus envelope glycoprotein D (gD). Two TNF superfamily ligands, including the secreted TNFβ (lymphotoxin α) and the membrane protein LIGHT (lymphotoxins, exhibits inducible expression, and competes with HSV glycoprotein D for HVEM, a receptor expressed by T lymphocytes), have been shown to be the cellular ligands for HVEM. Besides HVEM, LIGHT can also interact with LTβR, the receptor for lymphotoxin αβ heterotrimer. The role of the HVEM LIGHT /LTβ receptor ligand pair in immune function and herpesvirus pathobiology remains to be elucidated.
Description:
Interleukin-1 receptor antagonist protein (Il1rn), also known as IL-1ra, IRAP or IL1 inhibitor, is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1 alpha (IL1A) and interleukin 1 beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. The mouse Il1rn gene encodes a 178 amino acids (aa) protein with a 26 aa signal peptide. Mouse Il1rn protein shares 26% and 19% identity with its homologues IL-1 beta and IL-1 alpha, respectively. Il1rn can Inhibits the activity of interleukin-1 by binding to receptor IL1R1 and preventing its association with the coreceptor IL1RAP for signalling, but has no interleukin-1 like activity. Recently, an recombinant human Il1rn protein is used in the treatment of rheumatoid arthritis, an autoimmune disease in which IL-1 plays a key role.
Description:
Vascular endothelial growth factor (VEGF/VEGF-A ) is originally known as vascular permeability factor (VPF). It belongs to the PDGF family with a cysteine-knot structure comprised of eight conserved cysteine residues, and reckoned as a potent mediator in the process of angiogenesis and vasculogenesis in either fetus or adult. VEGF is particularly expressed in supraoptic , paraventricular nuclei and the choroid plexus of the pituitary, and abundant in the corpus luteum of the ovary and in kidney glomeruli. The rat VEGF protein contains a putative 20 amino acids (aa) signal peptide, and alternative splicing of rat VEGF gene produces isoforms of 120, 144, 164 and 188 aa. Rat VEGF164 respectively displays 97% and 88% aa identity with that regions of mouse and human VEGF. VEGF can bind to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin, and play important roles in inducing endothelial cell proliferation, promoting cell migration, inhibiting apoptosis and inducing permeabilisation of blood vessels.
Description:
The IL-17 family include IL-17A, IL-17B, IL-17C, IL-17D, IL-17E (also called IL-25), and IL-17F. The family is comprised of at least six proinflammatory cytokines that share a conserved cysteine-knot structure but diverge at the N-terminus. All members of the IL-17 family have a similar protein structure, with four highly conserved cysteine residues critical to their 3-dimensional shape, yet they have no sequence similarity to any other known cytokines. IL-17 family members are glycoproteins secreted as dimers that induce local cytokine production and recruit granulocytes to sites of inflammation. IL-17 is induced by IL-15 and IL-23, mainly in activated CD4+ T cells distinct from Th1 or Th2 cells. IL-17F is the most homologous to IL-17, but is induced only by IL-23 in activated monocytes.
Description:
IL-5 is expressed in eosinophils, NK cells, TC2 CD8+ T cells, mast cells, CD45+ CD4+ T cells, gamma delta T cells and IL-1 beta activated endothelial cells. IL-5 acts as a growth and differentiation factor for both B cells and eosinophils. Relative to B cells, IL-5 appears to induce the differentiation of activated conventional B-2 cells into Ig-secreting cells. In addition, it induces the growth of B-1 progenitors as well as IgM production by B-1 cells.IL-5 appears to perform a number of functions on eosinophils. These include the down modulation of Mac-1,the upregulation of receptors for IgA and IgG,the stimulation of lipid mediator (leukotriene C4 and PAF) secretion and the induction of granule release.IL-5 also promotes the growth and differentiation of eosinophils.
Description:
Interleukin-2 (IL-2) is a 133 amino acid glycoprotein with one intramolecular disulfide bond and variable glycosylation. It is secreted by activated T cells and induces proliferation and maturation of activated T cells, natural killer cells, and lymphokine activated killer cells. IL-2 also stimulates proliferation of antibody-producing B cells, activates neutrophils, and induces mononuclear cells to secrete IFN-gamma and TNF-alpha and -beta. Moreover, studies have shown that IL-2 is required for activation-induced apoptosis, an important hemeostatic mechanism in the immune system, which is involved in the maintenance of peripheral tolerance to self-antigens.
Description:
Interleukin-2 (IL-2) is a 133 amino acid glycoprotein with one intramolecular disulfide bond and variable glycosylation. It is secreted by activated T cells and induces proliferation and maturation of activated T cells, natural killer cells and lymphokine activated killer cells. IL-2 also stimulates proliferation of antibody-producing B cells, activates neutrophils and induces mononuclear cells to secrete IFN-gamma and TNF-alpha and -beta. Moreover, studies have shown that IL-2 is required for activation-induced apoptosis, an important hemeostatic mechanism in the immune system, which is involved in the maintenance of peripheral tolerance to self-antigens.
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