Insulin Receptor (ISR) Recombinant Protein | ISR recombinant protein

Recombinant Insulin Receptor (ISR)

Cat. Num. AAA2010333

• Applications: SDS-Page, Western Blot, ELISA, Immunoprecipitation
• Purity: > 95%
• Synonyms: Insulin Receptor (ISR); Recombinant Insulin Receptor (ISR); ISR recombinant protein

• Host: E Coli
• Purity/Purification: > 95%
• Form/Format: Supplied as lyophilized form in PBS,pH7.4, containing 5% sucrose, 0.01% sarcosyl.
• Sequence: The target protein is fused with N-terminal His-Tag, its sequence is listed below.; MGHHHHHHSGSEF-SHLRSLR PDAENNPGRP PPTLQEMIQM TAEIADGMAY LNAKKFVHRD LAARNCMVAH DFTVKIGDFG MTRDIYETDY YRKGGKGLLP VRWMSPESLK DGVFTASSDM WSFGVVLWEI TSLAEQPYQG LSNEQVLKFV MDGGYLDPPD NCPERLTDLM RMCWQFNPKM RPTFLEIVNL LKDDLHPSFP EVSFFYSEEN KAPESEELEM EFEDMENVPL DRSSHCQREE AGCREGGSSL SIKRTYDEHI PYTHMNGGKK NGRVLTLPRS NP
• Sequence Length: 1383

• Applicable Applications for ISR recombinant protein: SDS-PAGE, Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP)
• Organism: Rattus norvegicus (Rat)
• Expression System: Prokaryotic expression
• Residues: Ser1114~Pro1382 (Accession # P15127) with N-terminal His-Tag
• Subcellular Location: Cell membrane; Single-pass type I membrane protein
• Endotoxin Level: <1.0EU per 1ug (determined by the LAL method)
• Predicted Isoelectric Point: 5.5
• Reconstitution: Reconstitute in sterile PBS, pH7.2-pH7.4.
• Preparation and Storage: Avoid repeated freeze/thaw cycles. Store at 2-8 degree C for one month. Aliquot and store at -80 degree C for 12 months.; Stability Test: The thermal stability is described by the loss rate of the targetprotein. The loss rate was determined by accelerated thermal degradation test,that is, incubate the protein at 37 degree C for 48h, and no obvious degradation andprecipitation were observed. (Referring from China Biological Products Standard,which was calculated by the Arrhenius equation.) The loss of this protein is lessthan 5% within the expiration date under appropriate storage condition.

SDS-Page

NCBI and Uniprot Product Information

• NCBI GI #: 124531
• NCBI GeneID: 24954
• UniProt Accession #: P15127; P97681
• Molecular Weight: 32.3kDa
• NCBI Official Full Name: Insulin receptor
• NCBI Official Synonym Full Names: insulin receptor
• NCBI Official Symbol: Insr
• NCBI Protein Information: insulin receptor; IR; insulin receptor preproprotein
• UniProt Protein Name: Insulin receptor
• UniProt Gene Name: Insr
• UniProt Synonym Gene Names: IR
• UniProt Entry Name: INSR_RAT

NCBI Description

receptor for insulin; involved in intracellular signalling; mutations in gene are associated with type 2 diabetes mellitus [RGD, Feb 2006]

Uniprot Description

INSR: a receptor tyrosine kinase that mediates the pleiotropic actions of insulin. Binding of insulin leads to phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins serve as docking proteins for other signaling proteins that contain Src-homology-2 domains (SH2 domain) that specifically recognize different phosphotyrosines residues, including the p85 regulatory subunit of PI3K and SHP2. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT pathway, which is responsible for most of the metabolic actions of insulin, and the Ras-MAPK pathway, which regulates expression of some genes and cooperates with the PI3K pathway to control cell growth and differentiation. In addition to binding insulin, the insulin receptor can bind insulin-like growth factors (IGFI and IGFII). The holoenzyme is cleaved into two chains, the alpha and beta subunits. The active complex is a tetramer containing 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains constitute the ligand- binding domain, while the beta chains carry the kinase domain. Interacts with SORBS1 but dissociates from it following insulin stimulation. Familial mutations associated with insulin resistant diabetes, acanthosis nigricans, pineal hyperplasia, and polycystic ovary syndrome. SNP variants may be associated with polycystic ovary syndrome, atypical migraine and diabetic hyperlipidemia. Mutations also cause leprechaunism, a severe insulin resistance syndrome causing growth retardation and death in early infancy. Two isoforms of the human protein are produced by alternative splicing. The Short isoform has a higher affinity for insulin than the longer. Isoform Long and isoform Short are predominantly expressed in tissue targets of insulin metabolic effects: liver, adipose tissue and skeletal muscle but are also expressed in the peripheral nerve, kidney, pulmonary alveoli, pancreatic acini, placenta vascular endothelium, fibroblasts, monocytes, granulocytes, erythrocytes and skin. Isoform Short is preferentially expressed in fetal cells such as fetal fibroblasts, muscle, liver and kidney. Found as a hybrid receptor with IGF1R in muscle, heart, kidney, adipose tissue, skeletal muscle, hepatoma, fibroblasts, spleen and placenta. Overexpressed in several tumors, including breast, colon, lung, ovary, and thyroid carcinomas.

Protein type: Membrane protein, integral; Protein kinase, TK; Kinase, protein; EC 2.7.10.1; Protein kinase, tyrosine (receptor); TK group; InsR family

Cellular Component: membrane; intracellular membrane-bound organelle; integral to plasma membrane; integral to membrane; plasma membrane; synapse; caveola; nucleus; cytosol; receptor complex; endosome

Molecular Function: protein domain specific binding; GTP binding; PTB domain binding; receptor signaling protein tyrosine kinase activity; transmembrane receptor protein tyrosine kinase activity; protein kinase binding; protein phosphatase binding; insulin-like growth factor II binding; lipoic acid binding; protein kinase activity; insulin binding; insulin-like growth factor receptor binding; protein binding; insulin-like growth factor I binding; 3-phosphoinositide-dependent protein kinase binding; insulin receptor substrate binding; protein-tyrosine kinase activity; protein complex binding; phosphoinositide 3-kinase binding; ATP binding; insulin receptor activity

Biological Process: fat cell differentiation; heart morphogenesis; epidermis development; positive regulation of nitric oxide biosynthetic process; peptidyl-tyrosine phosphorylation; activation of MAPK activity; protein amino acid autophosphorylation; response to glucocorticoid stimulus; positive regulation of glycogen biosynthetic process; regulation of embryonic development; response to hormone stimulus; exocrine pancreas development; glucose homeostasis; protein amino acid phosphorylation; response to estradiol stimulus; response to insulin stimulus; positive regulation of glucose import; response to vitamin D; regulation of transcription, DNA-dependent; positive regulation of MAPKKK cascade; negative regulation of protein amino acid phosphorylation; male sex determination; positive regulation of cell proliferation; response to glucose stimulus; protein heterotetramerization; regulation of hydrogen peroxide metabolic process; response to nutrient levels; positive regulation of developmental growth; positive regulation of mitosis; activation of protein kinase B; response to testosterone stimulus; response to manganese ion; G-protein coupled receptor protein signaling pathway; positive regulation of protein kinase B signaling cascade; organ morphogenesis; response to ethanol; cellular response to insulin stimulus; positive regulation of glycolysis; activation of protein kinase activity; insulin receptor signaling pathway; positive regulation of protein amino acid phosphorylation; response to activity; negative regulation of transporter activity; transmembrane receptor protein tyrosine kinase signaling pathway; positive regulation of DNA replication; positive regulation of phosphorylation; positive regulation of cell migration; transformation of host cell by virus