Insulin Receptor / INSR / CD220 Recombinant Protein | INSR recombinant protein

Recombinant Human Insulin Receptor / INSR / CD220 Protein (long isoform, His tag)

Cat. Num. AAA2545927

• Gene Names: INSR; HHF5; CD220
• Purity: > 95 % as determined by SDS-PAGE
• Synonyms: Insulin Receptor / INSR / CD220; Recombinant Human Insulin Receptor / INSR / CD220 Protein (long isoform; His tag); CD220; HHF5; INSR; INSR recombinant protein

• Host: Human Cells
• Purity/Purification: > 95 % as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH 7.4
• Sequence Length: 1382

• Application Notes: The secreted recombinant human INSR isoform long consists of 940 amino acids and has a predicted molecular mass of 107 (83+24) kDa. As a result of glycosylation, the apparent molecular mass of rhINSR is approximately 125-135 kDa & 40-45 kDa, corresponding to the alpha subunit and the ECD of beta subunit respectively in SDS-PAGE under reducing conditions.
• Predicted N Terminal: His 28 & Ser 763
• Endotoxin: < 1.0 EU per mug of the protein as determined by the LAL method
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

Related Product Information for INSR recombinant protein

Background: INSR (Insulin receptor), also known as CD220, is a transmembrane receptor that is activated by insulin. INSR belongs to theprotein kinase superfamily, and exists as a tetramer consisting of two alpha subunits and two beta subunits linked by disulfide bonds. The alpha and beta subunits are encoded by a single INSR gene, and the beta subunits pass through the cellular membrane. As the receptor for insulin with tyrosine-protein kinase activity, INSR associates with downstream mediators upon binding to insulin, including IRS1 (insulin receptor substrate 1) and phosphatidylinositol 3'-kinase (PI3K). IRS-1 binding and phosphorylation eventually leads to an increase in the high affinity glucose transporter (Glut4) molecules on the outer membrane of insulin-responsive tissues. INSR isoform long and isoform short are expressed in the peripheral nerve, kidney, liver, striated muscle, fibroblasts and skin, and is found as a hybrid receptor with IGF1R which also binds IGF1 in muscle, heart, kidney, adipose tissue, skeletal muscle, hepatoma, fibrobasts, spleen and placenta. Defects in Insulin Receptor/INSR are the cause of Rabson-Mendenhall syndrome (Mendenhall syndrome), insulin resistance (Ins resistance), leprechaunism (Donohue syndrome), and familial hyperinsulinemic hypoglycemia 5 (HHF5). It may also be associated with noninsulin-dependent diabetes mellitus (NIDDM).

Description: A DNA sequence encoding the human INSR isoform long (NP_000199.2) extracellular domain (Met 1-Lys 956) was expressed, fused with a polyhistidine tag at the C-terminus.

NCBI and Uniprot Product Information

• NCBI GI #: 119395736
• NCBI GeneID: 3643
• NCBI Accession #: NP_000199.2
• NCBI GenBank Nucleotide #: NM_000208.3
• UniProt Accession #: P06213; Q17RW0; Q59H98; Q9UCB7; Q9UCB8; Q9UCB9
• Molecular Weight: 155,146 Da
• NCBI Official Full Name: insulin receptor isoform Long preproprotein
• NCBI Official Synonym Full Names: insulin receptor
• NCBI Official Symbol: INSR
• NCBI Official Synonym Symbols: HHF5; CD220
• NCBI Protein Information: insulin receptor
• UniProt Protein Name: Insulin receptor
• Protein Family: Insulin receptor
• UniProt Gene Name: INSR
• UniProt Synonym Gene Names: IR

NCBI Description

This gene encodes a member of the receptor tyrosine kinase family of proteins. The encoded preproprotein is proteolytically processed to generate alpha and beta subunits that form a heterotetrameric receptor. Binding of insulin or other ligands to this receptor activates the insulin signaling pathway, which regulates glucose uptake and release, as well as the synthesis and storage of carbohydrates, lipids and protein. Mutations in this gene underlie the inherited severe insulin resistance syndromes including type A insulin resistance syndrome, Donohue syndrome and Rabson-Mendenhall syndrome. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Oct 2015]

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

Chromosomal Location of Human Ortholog: 19p13.2

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

Molecular Function: ATP binding; GTP binding; insulin binding; insulin receptor activity; insulin receptor substrate binding; insulin-like growth factor I binding; insulin-like growth factor II binding; insulin-like growth factor receptor binding; phosphoinositide 3-kinase binding; protein binding; protein-tyrosine kinase activity; PTB domain binding; receptor signaling protein tyrosine kinase activity

Biological Process: activation of MAPK activity; activation of protein kinase activity; activation of protein kinase B; cellular response to insulin stimulus; G-protein coupled receptor protein signaling pathway; glucose homeostasis; heart morphogenesis; insulin receptor signaling pathway; peptidyl-tyrosine phosphorylation; positive regulation of cell migration; positive regulation of cell proliferation; positive regulation of developmental growth; positive regulation of DNA replication; positive regulation of glucose import; positive regulation of glycogen biosynthetic process; positive regulation of glycolysis; positive regulation of MAPKKK cascade; positive regulation of mitosis; positive regulation of nitric oxide biosynthetic process; positive regulation of protein amino acid phosphorylation; positive regulation of protein kinase B signaling cascade; protein amino acid autophosphorylation; protein heterotetramerization; regulation of embryonic development; regulation of transcription, DNA-dependent; transformation of host cell by virus

Disease: Diabetes Mellitus, Insulin-resistant, With Acanthosis Nigricans; Donohue Syndrome; Hyperinsulinemic Hypoglycemia, Familial, 5; Pineal Hyperplasia, Insulin-resistant Diabetes Mellitus, And Somatic Abnormalities