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CDK2AP2, also known as DOC1R, is short for cyclin-dependent kinase 2-associated protein 2. The gene CDK2AP2 encodes this protein that interacts with cyclin-dependent kinase 2 associated protein 1. Pseudogenes associated with this gene are located on chromosomes 7 and 9. Alternatively spliced transcript variants have been observed for this gene. It belongs to the CDK2AP family. CDK2AP1 (cyclin-dependent kinase 2-associated protein 1), corresponding to the gene doc-1 (deleted in oral cancer 1), is a tumor suppressor protein. The doc-1 gene is absent or down-regulated in hamster oral cancer cells and in many other cancer cell types. The ubiquitously expressed CDK2AP1 protein is the only known specific inhibitor of CDK2, making it an important component of cell cycle regulation during G(1)-to-S phase transition.

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Dtk, also called Tyro3, belongs to the TAM receptor family of receptor protein tyrosine kinases (RPTKs) composed of three receptors Tyro3, Axl, and Mer. These receptors share a characteristic molecular structure of two immunoglobulin-like and two fibronectin type III repeats and have been best Characterised for their roles in immune regulation, fertility, thrombosis and phagocytosis. Gas6 and protein S have been identified as ligands for these receptors. Gas6 binding induces tyrosine phosphorylation and downstream signallling pathways that can lead to cell proliferation, migration, or the prevention of apoptosis. Tyro3 and Axl play important regulatory roles in a variety of tissues, including the central nervous, reproductive, immune, and vascular systems. Tyro3 is widely expressed during embryonic development and preferentially expressed during neurogenesis in the central nervous system.

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Junctional Adhesion Molecule B (JAM-B) is a single-pass type I membrane protein that belongs to the juctional adhesion molecules family. JAM-B includes a signal sequence (aa 1-28), an extracellular region (aa 29-238) with one Ig-like C2-type domain and one Ig-like V-type domain, a transmembrane segment (aa 239-259), and a cytoplasmic domain (aa 260 - 298). JAMB is localized to the tight junctions between endothelial cells or epithelial cells. JAM-B is prominently expressed in the heart, placenta, lung, foreskin and lymph node. It is also present on the endothelia of other vessels. JAM-B acts as an adhesive ligand for interacting with a variety of immune cell types and may play a role in lymphocyte homing to secondary lymphoid organs.

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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.

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Human IL-2RB, also known asinterleukin-2 receptor subunit beta,is the receptor for interleukin-2. IL2 receptor complex is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2. IL2 receptor complex has three forms with respect to ability to bind IL2. IL-2RB is belonged to a type I membrane protein,and has a 26 residue signal peptide, a 214 residue extracellular region, a 25 residue transmembrane region and a 286 residue cytoplasmic domain. IL-2RB is the subunit critical for receptor-mediated signalling via physically or functionally coupling to other signalling molecules, such as the Jak-STAT and Src-family protein tyrosine kinase although it lacks apparent catalytic motifs.

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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.

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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.

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CD40 is a Type I Transmembrane Glycoprotein that belongs to the TNF Receptor Superfamily. CD40 is expressed in B cells, follicular dendritic cells, dendritic cells, activated monocytes, macrophages, endothelial cells, vascular smooth muscle cells, and several tumor cell lines. The extracellular domain of CD40 is characterised by Cysteine rich repeat regions. Interaction of CD40 with its ligand (CD40L) leads to aggregation of CD40 molecules, which in turn interact with cytoplasmic components to initiate signalling pathways. Several different TRAF proteins (adaptor proteins) have been identified to serves as mediators of the signal transduction. CD40 plays an essential role in mediating a broad variety of immune and inflammatory responses including T cell-dependent immunoglobulin class switching, memory B cell development, and germinal center formation.

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Interleukin-18 is a secreted protein and it belongs to the IL-1 family. IL-18 is a proinflammatory cytokine and produced by macrophages and other cells. This cytokine can induce the IFN-gamma production of T cells. The combination of this cytokine and IL12 has been shown to inhibit IL-4 dependent IgE and IgG1 production, and enhance IgG2a production of B cells. IL-18 binding protein (IL18BP) can specifically interact with this cytokine, and thus negatively regulate its biological activity. After stimulation with IL-18, natural killer (NK) cells and certain T cells release another important cytokine called interferon- gamma (IFN- gamma ) or type II interferon that plays an important role in activating the macrophages or other cells.

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Mouse Ifng is a secreted protein which belongs to the type I I (or gamma) interferon family. IFNG is produced by lymphocytes and activated by specific antigens or mitogens. In addition to having antiviral activity, IFNG also has important immunoregulatory functions. It is a potent activator of macrophages and has antiproliferative effects on transformed cells. It can potentiate the antiviral and antitumor effects of the type I interferons. Genetic variation in IFNG is associated with the risk of aplastic anemia (AA) which is a rare disease in which the reduction of the circulating blood cells results from damage to the stem cell pool in bone marrow. In most patients, the stem cell lesion is caused by an autoimmune attack. T-lymphocytes, activated by an endogenous or exogenous, and most often unknown antigenic stimulus, secrete cytokines, including IFN-gamma, which would in turn be able to suppress hematopoiesis.

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B- and T-Lymphocyte Attenuator (BTLA) is a single-pass type I membrane protein containing 1 Ig-like V-type (immunoglobulin-like) domain. BTLA expression is induced during activation of T cells, and BTLA remains expressed on Th1 cells but not Th2 cells. Like PD1 and CTLA4, BTLA interacts with a B7 homolog, B7H4. However, unlike PD-1 and CTLA-4, BTLA displays T-Cell inhibition via interaction with tumor necrosis family receptors (TNF-R), not just the B7 family of cell surface receptors. BTLA is a lymphocyte inhibitory receptor that inhibits lymphocytes during immune response. BTLA also is a ligand for tumor necrosis factor (receptor) superfamily, member 14 (TNFRSF14), also known as herpes virus entry mediator (HVEM). BTLA-HVEM complexes negatively regulate T-cell immune responses.

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T-Cell Surface Glycoprotein CD8 beta Chain (CD8 Antigen) is a cell surface glycoprotein found on most cytotoxic T lymphocytes that mediates efficient cell-cell interactions within the immune system. CD8 Antigen, acting as a coreceptor, and the T-cell receptor on the T lymphocyte recognize antigens displayed by an antigen presenting cell (APC) in the context of class I MHC molecules. The functional coreceptor is either a homodimer composed of two alpha chains, or a heterodimer composed of one alpha and one beta chain. Both alpha and beta chains share significant homology to immunoglobulin variable light chains. Multiple alternatively spliced transcript variants encoding distinct membrane associated or secreted isoforms have been described. A pseudogene, also located on chromosome 2, has been identified.

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Interleukin-1 Receptor Antagonist (IL-1RN) is a member of the IL-1 family. Endogenous IL-1RN is produced in numerous animal disease models as well as in human autoimmune and chronic inflammatory diseases. It binds to IL-1 receptors in competition with IL-1, but does not elicit intracellular response from this binding. Its role in counteracting the proinflammatory effects of IL-1 is being studied by numerous research groups. IL-4 and IL-13 have been shown to amplify the stimulatory effect of IL1-beta on the production of soluble and intracellular forms of IL-1RN. The regulated expression of IL-1RN in various cell types has been shown to be influenced by cytokines. In synovial fibroblasts, IL-1, TNF-alpha, or PDGF markedly enhances the synthesis of IL-1RN.

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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- gamma , 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 unidentified in immune tissues such as the spleen, but also in nonimmune cells including keratinocytes.

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The Galectin family of proteins, with specificity for Nacetyllactosamine containing glycoproteins, consists of beta-galactoside binding lectins containing homologous carbohydrate recognition domains (CRDs).They also possess hemagglutination activity, which is attributable to their bivalent carbohydrate binding properties. Galectins are active both intracellularly and extracellularly. Although they are localized primarily in the cytoplasm and lack a classical signal peptide; they can be secreted by one or more as yet unidentified non-classical secretory pathways. They have diverse effects on many cellular functions including adhesion, migration, polarity, chemotaxis, proliferation, apoptosis, and differentiation. Galectins may play a key role in many pathological states, including autoimmune diseases, allergic reactions, inflammation, tumor cell metastasis, atherosclerosis, and diabetic complications.

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T-Cell Surface Glycoprotein CD3 epsilon Chain (CD3 epsilon ) is a single-pass type I membrane protein. CD3 epsilon contains 1 Ig-like (immunoglobulin-like) domain and 1 ITAM domain. CD3 epsilon is a polypeptide encoded by the CD3E gene on chromosome 11 in humans. The T cell receptor-CD3 complex (TCR/CD3 complex) is involved in T-cell development and several intracellular signal-transduction pathways. This complex is critical for T-cell development and function, and represents one of the most complex transmembrane receptors. The T cell receptor-CD3 complex is unique in having ten cytoplasmic immunoreceptor tyrosine-based activation motifs (ITAMs). TCR/CD3 complex plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways.

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Mesothelin is a cell surface glycoprotein whose expression is limited to mesothelial cells of the serosa (pleura, pericardium, and peritoneum) and epithelial cells of the trachea, tonsils, fallopian tube, and kidneys. Mesothelin plays an important role in cell survival, proliferation, migration, invasion, tumour progression, and resistance to chemotherapy. The overexpression of mesothelin can activate NF-κB and signal transducer and activator of transcription 3 (Stat3), inhibit apoptotic signalling and TNF- alpha-induced apoptosis, and accelerate the G1–S transition. Mesothelin is also found overexpressed in various cancers, including malignant mesothelioma, pancreatic or ovarian carcinoma, sarcomas and in some gastrointestinal or pulmonary carcinomas. As a result of its limited expression in normal tissues, mesothelin has been reported as an ideal tumour-associated marker for the development of targeted therapy.

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High efficiency competent cells in convenient packaging designed to satisfy higher throughput requirements.

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The S100 family of proteins are found in vertebrates and are characterised by two calcium-binding sites that have a helix-loop-helix conformation. The family of 24 is divided into three subgroups based on function: those with intracellular, intracellular plus extracellular, and extracellular regulatory effects. The calcium-binding protein S100A8, also called MRP8 or Myeloid-related protein 8, and Calgranulin A, forms a heterodimer with S100A9, called Calprotectin. The heterodimer is expressed by granulocytes, monocytes, and early differentiation states of macrophages, and is known to be an important pro-inflammatory mediator in acute and chronic inflammation. S100A8 and 9 are DAMPs, or Damage-associated molecular pattern molecules, and are able to activate receptors of the innate immune system, one being TLR4.

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Members of the immunoglobulin-like transcript (ILT) family are activating and inhibitory immunoreceptors whose genes are located same locus that encodes killer cell Ig-like receptors (KIR). Leukocyte Immunoglobulin-Like Receptor Subfamily B Member 2 (LIR-2) is a type I transmembrane protein. LIR-2 is expressed primarily on monocytes and dendritic cells (DC). Human LIR-2 is produced as a 598 amino acino acid precursor including a 21 aa signal sequence, a 440 aa extracellular domain (ECD), a 21 aa transmenbrane segment, and a 116 aa cytoplasmic domain. LIR-2 binds to Classical MHCI proteins. Ligation of LIR-2 incluces Tyr phosphorylation within its cytoplasmic ITIMs, a requirement for association with SHP-1. LIR-2 mediates tolerogenic DC-induced CD4+ T cell energy in vitro and in vivo.

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Human Chemokine (C-X-C motif) Ligand 7 (CXCL7), also known as neutrophil activating peptide 2 (NAP-2), is a member of the CXC chemokines containing an ELR domain (Glu-Leu-Arg tripeptide motif). Similar to other ELR domain containing CXC chemokines, such as IL-8 and the GRO proteins, CXCL7 binds CXCR2, chemoattracts and activates neutrophils. CXCL7, Connective Tissue Activating Protein III (CTAPIII) and beta thrombogulin ( beta TG), are proteolytically processed carboxylterminal fragments of platelet basic protein (PBP) which is found in the alphagranules of human platelets. Although CTAPIII, beta TG, and PBP represent amino-terminal extended variants of NAP2 and possess the same CXC chemokine domains, these proteins do not exhibit CXCL7/NAP2 activity. CXCL7 induces cell migration through the G-protein-linked receptor CXCR-2.

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Complement Factor H-Related 1 (CFHR1) is a 43 kDa secreted member of the factor H family of glycoproteins. The human Complement Factor H protein family consists of the complement and immune regulators factor H, the factor H-like protein 1 (FHL-1) and five factor H-related proteins (CFHR-1 to -5). Members of the H-related protein family are exclusively composed of individually folded protein domains, termed short consensus repeats (SCRs) or complement control modules. FHR1 is produced by hepatocytes and circulates as two differentially glycosylated isoforms (37 kDa and 43 kDa). Mature human FHR1 is 312 amino acids in length. It contains five, approximately 60 aa SCRs that basically constitute the entire molecule. FHR1 may play a role in complement regulation, lipid metabolism and lipoprotein complexes that bind PMNs to LPS.

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Tumour necrosis factor receptor superfamily member 9(TNFRSF9), also known as CD137 and 4-1BB, is an inducible T cell surface protein belonging to the tumour necrosis factor receptor superfamily. It is a single-pass type I membrane protein which contains 4 TNFR-Cys repeats. The human and mouse proteins share 60% amino acid sequence identity. CD137 is expressed by mesenchymal cells, including endothelial cells, chondrocytes, and cells of the central nervous system. CD137 is also broadly expressed by cells of the human immune system, is broadly expressed by cells of the human immune system, including activated CD8+ and CD4+ T cells, activated natural killer (NK) cells, follicular dendritic cells (FDCs) and monocytes. CD137 has diverse roles in the immune response, the one key function is to promote the survival of both T cells and dendritic cells by binding the cognate ligand CD137L (4-1BBL).

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CD274, also known as B7-H1 or programmed death ligand 1 (PD-L1), is a 40 kD type I transmembrane protein and a member of the B7 family within the immunoglobulin receptor superfamily. Programmed death-1 ligand-1 (PD-L1, CD274, B7-H1) has been identified as the ligand for the immunoinhibitory receptor programmed death-1(PD1/PDCD1) and has been demonstrated to play a role in the regulation of immune responses and peripheral tolerance. By binding to PD1 on activated T-cells and B-cells, PD-L1 may inhibit ongoing T-cell responses by inducing apoptosis and arresting cell-cycle progression. Accordingly, it leads to growth of immunogenic tumor growth by increasing apoptosis of antigen specific T cells and may contribute to immune evasion by cancers. PD-L1 thus is regarded as promising therapeutic target for human autoimmune disease and malignant cancers.

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It is a single-pass type I membrane protein and contains 4 TNFR-Cys repeats. The protein is a member of the tumor necrosis factor (TNF) family of receptors. It is expressed on the surface of most cell types, including cells of epithelial and myeloid lineages, but not on T and B lymphocytes. The protein is the receptor for the heterotrimeric lymphotoxin containing LTA and LTB, and for TNFS14/LIGHT. It promotes apoptosis via TRAF3 and TRAF5 and may play a role in the development of lymphoid organs. The encoded protein and its ligand play a role in the development and organization of lymphoid tissue and transformed cells. Activation of the encoded protein can trigger apoptosis. Not only does the TNFRSF3 help trigger apoptosis, it can lead to the release of the cytokine interleukin 8. Overexpression of TNFRSF3 in Human Cells cells increases IL-8 promoter activity and leads to IL-8 release. TNFRSF3 is also essential for development and organization of the secondary lymphoid organs and chemokine release.

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Zinc Finger and BTB Domain-Containing Protein 17 (ZBTB17) belongs to the Kruppel C2H2-type zinc finger protein family. ZBTB17 may function as a housekeeping DNA-binding protein that regulates the expression of specific genes, it has been shown to bind to the promoters of adenovirus major late protein and cyclin D1 and activate transcription. ZBTB17 may has growth arrest activity, probably through inhibition of cell cycle progression. ZBTB17 required for early embryonic development during gastrulation. ZBTB17 induces cell arrest at G1, an effect mediated by its activation of the gene coding for P15INK4b. This effect is blocked by Myc, which displaces transcriptional coactivators bound to ZBTB17. Although the downregulation of ZBTB17 may contribute to Myc-induced cell transformation, the de-activation of ZBTB17 is absolutely essential for Myc-induced apoptosis.

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Human beta -Nerve Growth Factor ( beta -NGF) was initially isolated in the mouse submandibular gland. It is composed of three non-covalently linked subunits alpha, beta , and gamma ; it exhibits all the biological activities ascribed to NGF. It is structurally related to BDNF, NT-3 and NT-4 and belongs to the cysteine-knot family of growth factors that assume stable dimeric structures. beta -NGF is a neurotrophic factor that signals through its receptor beta -NGF, and plays a crucial role in the development and preservation of the sensory and sympathetic nervous systems. beta -NGF also acts as a growth and differentiation factor for B lymphocytes and enhances B-cell survival. These results suggest that beta -NGF is a pleiotropic cytokine, which in addition to its neurotropic activities may have an important role in the regulation of the immune system. Human beta -NGF shares 90% sequence similarity with mouse protein and shows cross-species reactivity.

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Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. In Saccharomyces cerevisiae, ubiquitin-like proteins include Rub1, Ula1, Uba3, Smt3, Ubc2, Ubc12 and Ubc9. Rub1 shares 53% homology with ubiquitin and requires activation via the E2 proteins, including Ula1, Uba3 and Ubc12 in order to conjugate to substrates directed to different proteolytic systems. Ubc4 catalyzes ubiquitination of IkBa in a phosphorylation and SCFB-TRCP dependent manner. In this particular reaction, E1 first transfers ubiquitin to the E2 component Ubc4, and Ubc4 then associates with E3 ligase, which conjugates the poly-ubiquitin chain on a target protein. In this fashion, the chain tags the IkBa for degradation by a proteasome thus lifting the inhibitory effect of IkBa on NFkB and allowing NFkB to enter the nucleus.

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Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. In Saccharomyces cerevisiae, ubiquitin-like proteins include Rub1, Ula1, Uba3, Smt3, Ubc2, Ubc12 and Ubc9. Rub1 shares 53% homology with ubiquitin and requires activation via the E2 proteins, including Ula1, Uba3 and Ubc12 in order to conjugate to substrates directed to different proteolytic systems. Ubc4 catalyzes ubiquitination of IkBa in a phosphorylation and SCFB-TRCP dependent manner. In this particular reaction, E1 first transfers ubiquitin to the E2 component Ubc4, and Ubc4 then associates with E3 ligase, which conjugates the poly-ubiquitin chain on a target protein. In this fashion, the chain tags the IkBa for degradation by a proteasome thus lifting the inhibitory effect of IkBa on NFkB and allowing NFkB to enter the nucleus.

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Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. In Saccharomyces cerevisiae, ubiquitin-like proteins include Rub1, Ula1, Uba3, Smt3, Ubc2, Ubc12 and Ubc9. Rub1 shares 53% homology with ubiquitin and requires activation via the E2 proteins, including Ula1, Uba3 and Ubc12 in order to conjugate to substrates directed to different proteolytic systems. Ubc4 catalyzes ubiquitination of IkBa in a phosphorylation and SCFB-TRCP dependent manner. In this particular reaction, E1 first transfers ubiquitin to the E2 component Ubc4, and Ubc4 then associates with E3 ligase, which conjugates the poly-ubiquitin chain on a target protein. In this fashion, the chain tags the IkBa for degradation by a proteasome thus lifting the inhibitory effect of IkBa on NFkB and allowing NFkB to enter the nucleus.