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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:
The TIM (T cell/transmembrane, immunoglobulin and mucin) family plays a critical role in regulating immune responses, including allergy, asthma, transplant tolerance, autoimmunity and the response to viral infections. The unique structure of TIM immunoglobulin variable region domains allows highly specific recognition of phosphatidylserine (PtdSer), exposed on the surface of apoptotic cells. TIM-4 (T cell; immunoglobulin; Mucin-4), also known as SMUCKLER, is a 60 kDa member of the TIM family of immune regulating proteins. TIM-4 is exclusively expressed on antigen-presenting cells, where it mediates phagocytosis of apoptotic cells and plays an important role in maintaining tolerance. TIM-4 binds specifically to TIM-1 which is also the cellular receptor for the hepatitis A virus, and has been implicated in the development of asthma. Among hematopoietic cells, TIM-1 is expressed on activated B and T cells, preferentially in the Th2 subset of CD4+ T cells. The interaction of TIM-4 with TIM-1 induces costimulatory and hyperproliferative signals in T cells.
Description:
Interleukin 11 (IL-11) is a thrombopoietic growth factor that directly stimulates the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells and induces megakaryocyte maturation resulting in increased platelet production. IL-11 is a member of a family of human growth factors that includes human growth hormone, granulocyte colony-stimulating factor, and other growth factors.
Description:
Cytokines of the IL6/GCSF/MGF family are glycoproteins of about 170 to 180 amino acid residues that contain four conserved cysteine residues involved in two disulfide bonds. They have a compact, globular fold (similar to other interleukins), stabilized by the 2 disulfide bonds. One half of the structure is dominated by a 4 alpha-helix bundle with a left-handed twist; the helices are anti-parallel, with 2 overhand connections, which fall into a 2-stranded anti-parallel beta-sheet. The fourth alpha helix is important to the biological activity of the molecule. Interleukin-6 (IL-6) is an important proinflammatory and immunoregulatory cytokine expressed by various cells. Interleukin-6 has been shown to inhibit the growth of early stage and to promote the proliferation of advanced stage melanoma cells in vitro.
Description:
TNFRSF11B is a secreted protein, containing 2 death domains and 4 TNFR-Cys repeats. TNFRSF11B is a decoy receptor for the receptor activator of nuclear factor kappa B ligand (RANKL). By binding RANKL, TNFRSF11B inhibits nuclear kappa B (NF-κB) which is a central and rapid acting transcription factor for immune-related genes, and a key regulator of inflammation, innate immunity, and cell survival and differentiation. TNFRSF11B levels are influenced by voltage-dependent calcium channelsCav1.2. TNFRSF11B can reduce the production of osteoclasts by inhibiting the differentiation of osteoclast precursors (osteoclasts are related to monocytes/macrophages and are derived from granulocyte/macrophage-forming colony units (CFU-GM)) into osteoclasts and also regulates the resorption of osteoclasts in vitroand in vivo. TNFRSF11B binding to RANKL on osteoblast/stromal cells, blocks the RANKL-RANK ligand interaction between osteoblast/stromal cells and osteoclast precursors. This has the effect of inhibiting the differentiation of the osteoclast precursor into a mature osteoclast.
Description:
TNFRSF10B is a member of the TNF-receptor superfamily, and contains an intracellular death domain. This receptor can be activated by tumor necrosis factor-related apoptosis inducing ligand (TNFSF10/TRAIL/APO-2L), and transduces apoptosis signal. The adapter molecule FADD recruits caspase-8 to the activated receptor and is required for the apoptosis mediated by TNFRSF10B. TNFRSF10B is expressed in a number of cell types, and to particularly high levels in lymphocytes and spleen. This single-pass transmembrane protein contains two cysteine-rich repeat units in its extracellular region, followed by a transmembrane segment and a cytoplasmic tail containing a typical “death domain”. TNFRSF10B expression is regulated by the tumor suppressor p53. It is also indicated that the activation of NF-kappa-B can be promoted by TNFRSF10B.
Description:
Mouse CD275 (B7-H2) is a member of the growing B7 family of immune costimulatory proteins. CD275 has been identified as the ligand for ICOS, a member of the CD28 family of co-stimulatory receptors. Mouse CD275 is expressed on resting B cells and at low levels on monocytes. The CD275/ICOS interaction appears to play roles in T cell dependent B cell activation and Th differentiation.
Description:
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.
Description:
CST7 is a secreted protein and primarily expressed in peripheral blood cells and spleen.It is belongs to the cystatin family. The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. This gene encodes a glycosylated cysteine protease inhibitor with a putative role in immune regulation through inhibition of a unique target in the hematopoietic system.
Description:
Legumain is a lysosomal cysteine protease which is a member of the peptidase C13 family. Though it is found in many tissues, it is highly expressed in the kidney, heart, and placenta. Legumain has a strict specificity for hydrolysis of asparaginyl bonds and can also cleave aspartyl bonds slowly, especially under acidic conditions. Over-expression Legumain in tumors is significant for invasion and metastasis. In addition, Legumain may be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system and negative regulation of neuron apoptosis.
Description:
Matrix Metalloproteinase-1 (MMP-1) is expressed by fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. MMP1 contains several distinct domains: a prodomain that is cleaved upon activation, a catalytic domain containing the zinc binding site, a short hinge region, and a carboxyl terminal (hemopexin like) domain. MMP-1 can degrade a broad range of substrates including types I, II, III, VII, VIII, and X collagens as well as casein, gelatin, alpha1 antitrypsin, myelin basic protein, L-Selectin, pro-TNF, IL1, IGFBP3, IGFBP5, pro-MMP2, and pro-MMP9. A significant role of MMP1 is the degradation of fibrillar collagens in extracellular matrix remodeling, characterized by the cleavage of the interstitial collagen triple helix into 3/4, 1/4 fragments. MMP1 may also be involved in enzyme cascades, cytokine regulation and cell surface molecule modulation.
Description:
Nuclear NMNAT isoform. Catalyses the formation of NAD+ from nicotinamide mononucleotide (NMN) and ATP. It can also use the deamidated form of nicotinic acid mononucleotide (NAMN) as substrate with the same efficiency. Interacts with PARP-1/ARTD1. Protects against axonal degeneration following mechanical or toxic insults. Widely expressed.
Description:
MMP3 is a member of the matrix metalloproteinase (MMP) family whose members are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, tissue remodeling, and disease processes including arthritis and metastasis. The MMP-3 enzyme degrades collagen types II, III, IV, IX, and X, proteoglycans, fibronectin, laminin, and elastin. In addition, MMP-3 can also activate other MMPs such as MMP-1, MMP-7, and MMP-9, rendering MMP-3 crucial in connective tissue remodeling.[3] The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation.
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:
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.
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