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Description:
Human complement component C3. Complement C3 contains two chains linked by a disulfide bond. Its activation by a C3 convertase releases the C3a anaphylatoxin from the amino end of the beta chain and generates C3b, which associates with the Bb fragment of complement factor B to form the alternative-complement-pathway C3/C5 convertase.C3a anaphylatoxin is a vasoactive peptide and a mediator of inflammation. C3b, with its highly reactive thiol group, binds to the surface of foreign particles and facilitates phagocytosis. It binds to complement C5 and renders it susceptible to proteolysis by the classical-complement-pathway C3/C5 convertase. The activity of C3b is regulated by proteolytic cleavage involving factors H and I. Its degradation products can also be biologically active.
Description:
Human CD14 antigen. CD14 is a surface protein preferentially expressed on monocytes/macrophages. It binds lipopolysaccharide binding protein and recently has been shown to bind apoptotic cells.
Description:
A family of protein kinases located upstream of the MAP kinases andresponsible for their activation has been identified. The prototype member ofthis family, designated MAP kinase kinase, or MEK-1, specifically phospho-rylates the MAP kinase regulatory threonine and tyrosine residues present inthe Thr-Glu-Tyr motif of ERK. A second MEK family member, MEK-2, resem-bles MEK-1 in its substrate specificity. MEK-3 (or MKK-3) functions to acti-vate p38 MAP kinase, and MEK-4 (also called SEK1 or MKK-4) activatesboth p38 and JNK MAP kinases. MEK-5 appears to specifically phosphory-late ERK5, whereas MEK-6 phosphorylates p38 and p38b. MEK-7 (or MKK-7)phosphorylates and activates the JNK signal transduction pathway.
Description:
Apolipoprotein B (Low density lipoprotein). Apolipoprotein B is a major protein constituent of chylomicrons, VLDL and LDL. It functions as a recognition signal for the cellular binding and internalization of LDL particles.
Description:
Insulin-like growth factor I (IGF1) belongs to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contains the N- and C-terminal propeptide regions. Mature human IGF-I consisting of 70 amino acids has 94% identity with mouse IGF-I and exhibits cross-species activity. IGF-1 binds IGF-IR, IGF-IIR, and the insulin receptor and plays a key role in cell cycle progression, cell proliferation and tumor progression. IGF-1 expression is regulated by growth hormone. R3 IGF-1 is an 83 amino acid analog of IGF-1 comprising the complete human IGF-1 sequence with the substitution of an Arg (R) for the Glu(E) at position three, hence R3, and a 13 amino acid extension peptide at the N terminus. R3 IGF-1 has been produced with the purpose of increasing biological activity. R3 IGF-1 is significantly more potent than human IGF-I in vitro.
Description:
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.
Description:
Interleukin-1 (IL-1) designates two proteins, IL-1 alpha and IL-1 beta , which are the products of distinct genes, but recognize the same cell surface receptors. IL-1 alpha and IL-1 beta are structurally related polypeptides that show approximately 25% homology at the amino acid level. Both proteins are produced by a wide variety of cells in response to stimuli such as those produced by inflammatory agents, infections, or microbial endotoxins. The proteins are synthesized as 31 kDa precursors that are subsequently cleaved into proteins with molecular weights of approximately 17.5 kDa. The specific protease responsible for the processing of IL-1 beta , designated interleukin 1 beta -converting enzyme (ICE), has been described. Mature human and mouse IL-1 beta share approximately 75% amino acid sequence identity and human IL-1 beta has been found to be active on murine cell lines.
Description:
Insulin-like growth factor I (IGF1) belongs to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGFs are generated by proteolytic processing of inactive precursor protein containing N-terminal and C-terminal propeptide regions. Mature human IGF-I consisting of 70 amino acids with 94% identity with mouse IGF1 and exhibits cross-species activity. IGF1 binds IGF-1R, IGF-2R, and the insulin receptor and plays a key role in cell cycle progression, cell proliferation and tumor progression. IGF1 expression is regulated by growth hormone.
Description:
The function remains unknown.The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is demonstrated to participate in the ubiquitination of p53, c-Fos, and the NF-kB precursor p105 in vitro. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
Description:
The preB cell receptor is found on the surface of proB and preB cells, where it is involved in transduction of signals for cellular proliferation, differentiation from the proB cell to the preB cell stage, allelic exclusion at the Ig heavy chain gene locus, and promotion of Ig light chain gene rearrangements. The preB cell receptor is composed of a membrane-bound Ig mu heavy chain in association with a heterodimeric surrogate light chain. IGLL1 is one of the surrogate light chain subunits and is a member of the immunoglobulin gene superfamily. Mutations in its gene can result in B cell deficiency and agammaglobulinemia, an autosomal recessive disease in which few or no gamma globulins or antibodies are made.The preB cell receptor is found on the surface of proB and preB cells, where it is involved in transduction of signals for cellular proliferation, differentiation from the proB cell to the preB cell stage, allelic exclusion at the Ig heavy chain gene locus, and promotion of Ig light chain gene rearrangements. The preB cell receptor is composed of a membrane-bound Ig mu heavy chain in association with a heterodimeric surrogate light chain. This gene encodes one of the surrogate light chain subunits and is a member of the immunoglobulin gene superfamily. This gene does not undergo rearrangement. Mutations in this gene can result in B cell deficiency and agammaglobulinemia, an autosomal recessive disease in which few or no gamma globulins or antibodies are made. Two transcript variants encoding different isoforms have been found for this gene.
Description:
EPS8L1 a protein that is related to epidermal growth factor receptor pathway substrate 8 (EPS8), a substrate for the epidermal growth factor receptor. The function of this protein is unknown.This gene encodes a protein that is related to epidermal growth factor receptor pathway substrate 8 (EPS8), a substrate for the epidermal growth factor receptor. The function of this protein is unknown. Several alternatively spliced transcript variants encoding different isoforms exist.
Description:
TPM2 is beta-tropomyosin, an isoform of tropomyosin that is mainly expressed in slow, type 1 muscle fibers.The TPM2 gene encodes beta-tropomyosin, an isoform of tropomyosin that is mainly expressed in slow, type 1 muscle fibers (Tajsharghi et al., 2007 [PubMed 17846275]). See also TPM1 (MIM 191010), TPM3 (MIM 191030), and TPM4 (MIM 600317).
Description:
Malate dehydrogenase catalyzes the reversible oxidation of malate to oxaloacetate, utilizing the NAD/NADH cofactor system in the citric acid cycle. MDH1 is localized to the cytoplasm and may play pivotal roles in the malate-aspartate shuttle that operates in the metabolic coordination between cytosol and mitochondria.Malate dehydrogenase catalyzes the reversible oxidation of malate to oxaloacetate, utilizing the NAD/NADH cofactor system in the citric acid cycle. The protein encoded by this gene is localized to the cytoplasm and may play pivotal roles in the malate-aspartate shuttle that operates in the metabolic coordination between cytosol and mitochondria. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.
UOM:
1 * 1 EA
Promotion
,PRSI30-390EA
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