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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:
Secreted Protein Acidic and Rich in Cysteine (SPARC) is a secreted, evolutionarily conserved collagen-binding glycoprotein and belongs to the SPARC family. SPARC has 286 amino acids and contains an EF-hand in C-termina domain, a follistatin-like domain with Kazal-like sequences. There are two calcium binding sites, one binds 5 - 8 Ca2+ with a low affinity and other on an EF-hand loop that binds a Ca2+ ion with a high affinity. It is highly expressed in tissues undergoing morphogenesis, remodeling and wound repair. SPARC regulate cell growth through interactions with the extracellular matrix (ECM) and cytokines. SPARC bind to numerous proteins of the ECM, affect ECM protein expression, influence cellular adhesion and migration, and modulate growth factor-induced cell proliferation and angiogenesis. SPARC also binds several types of collagen, albumin, thrombospondin, PDGF and cell membranes.
Description:
Human Fractalkine (CX3CL1) is a member of the CX3C family of chemokines. Human Fractalkine contains both chemokine and mucin domain. The soluble form of Fractalkine is chemotactic for T-cells and monocytes, but not for neutrophils. The membrane bound form of Fractalkine promotes leukocytes adhesion to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid). The mucin-like stalk permits it to bind to the cell surface.
Description:
Interleukin-22 Receptor Subunit alpha-2 (IL22RA2) belongs to the type II cytokine receptor family. IL22RA2 is a secreted protein and contains three fibronectin type-III domains. IL22RA2 is widely expressed in many tissues. IL22RA2 functions as an IL22 antagonist and may be important in the regulation of inflammatory response. Three alternatively spliced transcript variants encoding distinct isoforms have been described.
Description:
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.
Description:
The Fas is also known as FAS receptor (FasR), apoptosis antigen 1 (APO-1 or APT), cluster of differentiation 95 (CD95) or tumor necrosis factor receptor superfamily member 6 (TNFRSF6). is a death receptor on the surface of cells that leads to programmed cell death (apoptosis). It is one of two apoptosis pathways, the other being the mitochondrial pathway. FasR is located on chromosome 10 in humans and 19 in mice. Similar sequences related by evolution (orthologs) are found in most mammals. Fas forms the death-inducing signaling complex (DISC) upon ligand binding. Membrane-anchored Fas ligand trimer on the surface of an adjacent cell causes trimerization of Fas receptor. This event is also mimicked by binding of an agonistic Fas antibody, though some evidence suggests that the apoptotic signal induced by the antibody is unreliable in the study of Fas signaling. To this end, several clever ways of trimerizing the antibody for in vitro research have been employed.Upon ensuing death domain (DD) aggregation, the receptor complex is internalized via the cellular endosomal machinery. This allows the adaptor molecule FADD to bind the death domain of Fas through its own death domain. Recently, Fas has also been shown to promote tumor growth, since during tumor progression, it is frequently downregulated or cells are rendered apoptosis resistant. Cancer cells in general, regardless of their Fas apoptosis sensitivity, depend on constitutive activity of Fas. This is stimulated by cancer-produced Fas ligand for optimal growth.
Description:
Receptor tyrosine-protein kinase erbB-4 (ErbB4) is also known as Her4, is a single-pass type I transmembrane glycoprotein that is a member of the ErbB family of tyrosine kinase receptors. ErbB family members serve as receptors for the epidermal growth factor (EGF) family of growth factors. ErbB4 is expressed in normal skeletal muscle, heart, pituitary, brain and several breast carcinomas. ERBB4 contains multiple furin-like cysteine rich domains, a tyrosine kinase domain, a phosphotidylinositol-3 kinase binding site and a PDZ domain binding motif. The protein binds to and is activated by neuregulins-2 and -3, heparin-binding EGF-like growth factor and betacellulin. Ligand binding induces a variety of cellular responses including mitogenesis and differentiation. Multiple proteolytic events allow for the release of a cytoplasmic fragment and an extracellular fragment. ErbB4 appears to play important roles in neuronal development, development of the heart and cancer. ERBB4 has been shown to interact with: DLG4, NRG1, STAT5A and YAP1. Mutations in this gene have been associated with cancer. Other single-nucleotide polymorphisms and a risk haplotype have been linked to schizophrenia.
Description:
Oncostatin M is a cytokine that is produced by macrophages, dendritic cells, and T lymphocytes during inflammatory events. The Type-I and Type-II Oncostatin M receptors are located on the cell surface of endothelial and tumor cells, contain the glycoprotein 130 (gp130) subunit, and activate the JAK/STAT signaling pathway. Oncostatin M functions to inhibit tumor cell proliferation, induce liver stem cell maturation, regulate cytokine production during hematopoiesis and inflammation, stimulate bone formation, and promote nervous system development.
Description:
Interleukin 17F (IL-17F), a member of the IL-17 cytokine family, is secreted by activated CD4+ T cells and monocytes. IL-17F binds the IL-17 receptor related molecule, IL17RC, to promote the production of the interleukin 6 (IL-6), interleukin 8 (IL-8), and granulocyte macrophage colony-stimulating factor (GM-CSF) cytokines. IL-17F also functions to regulate matrix turnover rates, inhibit endothelial cell angiogenesis, and induce the endothelial cell expression of interleukin 2 (IL-2), monocyte chemoattractant protein-1 (MCP-1), and transforming growth factor beta 1 (TGF-b1).
Description:
The cytokine thymic stromal lymphopoietin receptor (TSLPR) is consisting of a common gamma receptor–like chain (TSLPR- gamma ) and a common interleukin 7 (IL-7) R alpha chain that belongs to the type 1 cytokine receptor family. Transfection of TSLPR cDNA result in only low affinity binding, while cotransfection of the IL-7R alpha chain cDNA shows high affinity binding. TSLP and TSLPR play a critical role in the initiation of allergic diseases in mice. The TSLP R cDNA encodes a transmembrane receptor containing 370 amino acids (aa) with two potential N-linked glycosylation sites and a cytoplasmic domain of 104 aa including a single tyrosine residue. TSLPR can mediate signalling of the signal transducer and activator of transcription 5 (Stat5) by TSLP. TSLP R is broadly expressed in the immune and hematopoietic cells, particularly in hematopoietic progenitors and myeloid cells.
Description:
Transforming growth factor beta 2 (TGF- beta 2) is a member of TGF-beta superfamily that shares a characteristic cysteine knot structure. Mice with TGF- beta 2 gene deletion show defects in development of cardiac, lung, craniofacial, limb, spinal column, eye, inner ear and urogenital systems. All TGF- beta isoforms signal via the same heteromeric receptor complex, consisting of a ligand binding TGF- beta receptor type II (T beta R-II), and a TGF- beta receptor type I (T beta R-I). Signal transduction from the receptor to the nucleus is mediated via SMADs. TGF- beta expression is found in cartilage, bone, teeth, muscle, heart, blood vessels, haematopoitic cells, lung, kidney, gut, liver, eye, ear, skin, and the nervous system.
Description:
The tetrameric receptor complex for IFN gamma consists of two subunits, IFNGR1 (IFN gamma R alpha) and IFNGR2 (IFN gamma R beta ), through which the dimeric IFN- gamma exerts its biological functions, including antiviral, antiproliferation and immune-modulatory activity in mammals. Both IFNGR1 and IFNGR2 are single transmembrane proteins belonging to the class II cytokine family. FNGR1, widely expressed in most host cells, is essential for IFN gamma binding, receptor trafficking, and signal transduction. IFNGR1 possesses an intracellular Janus tyrosine kinase (JAK) 1 binding site, a signal transducer and activator of transcription 1 (STAT1) binding site. The resulting STAT1 homodimers translocate from the cytoplasm to the nucleus and bind to the interferon-gamma activated sequence (GAS) promoter to induce expression of downstream interferon stimulated genes (ISGs).
Description:
Lymphocyte-activation gene 3 (LAG3), also known as CD223, is a type I transmembrane protein with four extracellular Ig-like domains, designated D1 to D4 and belongs to the immunoglobulin superfamily. The gene for LAG3 lies adjacent to the gene for CD4 on human chromosome 12p13.32 and shares approximately 20% identical to the CD4 gene. LAG3 is expressed on activated T cells, natural killer cells, B cells and plasmacytoid dendritic cells. LAG3 binds with high affinity to MHC class II molecules, and it interferes competitively with the binding of CD4 to MHC class II and thereby blocks the transduction of stimulatory signals mediated by this interaction. LAG3 negatively regulates cellular proliferation, activation, and homeostasis of T cells, and plays an important role in Treg suppressive function. LAG3 is the target of various drug development programs to develop new treatments for cancer and autoimmune disorders. The soluble form, sLAG-3, is being developed as a cancer drug.
Description:
Ribonucleoside-Diphosphate Reductase Subunit M2 (RRM2) belongs to the ribonucleoside diphosphate reductase small chain family. The reductase of RRM2 catalyzes the formation of deoxyribonucleotides from ribonucleotides. Synthesis of the encoded protein (M2) is regulated in a cell-cycle dependent fashion. RRM2 supplies the precursors essential for DNA synthesis. RRM2 catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Phosphorylation on Ser-20 relieves the inhibitory effect on Wnt signaling.
Description:
Tissue Factor (TF) is a single-pass type I membrane glycoprotein member of the tissue factor family. TF expression is highly dependent upon cell type. This factor enables cells to initiate the blood coagulation cascades, and it functions as the high-affinity receptor for the coagulation factor VII. TF initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The complex activates factors IX or X by specific limited protolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade.
Description:
Lysosome-Associated Membrane Glycoprotein 1 (LAMP1) is a single-pass type I membrane protein belonging to the LAMP family. LAMP1 is expressed largely in the endosome-lysosome membranes of cells.It shuttles between lysosomes, endosomes, and the plasma membrane. LAMP1 functions to present carbohydrate ligands to selectins and it has also been implicated in tumor cell metastasis. It has been proposed LAMP1 can be used as a therapeutic agent for certain cancers, as well as a marker for lysosomal storage disorders and degranulation on lymphocytes such as CD8+ and NK cells. Cell surface LAMP1 and LAMP2 have been shown to promote adhesion of human peripheral blood mononuclear cells(PBMC) to vascular endothelium, therefore they are possibly involved in the adhesion of PBMCs to the site of inflammation.
Description:
BAG Family Molecular Chaperone Regulator 2 (BAG2) is a member of the Bag family whose members compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. BAG2 contains 1 BAG domain and is a important component of the HSC 70/CHIP chaperone-dependent ubiquitin ligase complex. In mammalian cells BAG1, BAG2, and BAG3 bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner.
UOM:
1 * 50 µG
Promotion
,PRSI92-006EA
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