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Manufactured by BioVendor

Insulin Receptor Human HEK293

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:HEK293
  • Other names:INSR Protein, IR, short isoform (HIR-A, IR-A), CD220
  • Species:Human
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Cat. No. Size Price


RD172041050 0.05 mg
PubMed Product Details
Technical Data

Type

Recombinant protein

Description

Total 927 AA, UniProt P06213–2 (His28-Lys944 of HIR-A, whole subunit α and extracellular domain of subunit β). MW: 105.9 kDa (calculated), migrates at ~ 160 kDa on SDS PAGE. N-terminal linker (2 extra AA), C-terminal linker (2 extra AA) and C-terminal His-tag (6 extra AA). Protein identity confirmed by LC-MS/MS.

Amino Acid Sequence

ASHLYPGEVCPGMDIRNNLTRLHELENCSVIEGHLQILLMFKTRPEDFRDLSFPKLIMITDYLLLFRVYGLESLKDLFPNLTVIRGSRLFFNYALVIFEMVHLKELGLYNLMNITRGSVRIEKNNELCYLATIDWSRILDSVEDNYIVLNKDDNEECGDICPGTAKGKTNCPATVINGQFVERCWTHSHCQKVCPTICKSHGCTAEGLCCHSECLGNCSQPDDPTKCVACRNFYLDGRCVETCPPPYYHFQDWRCVNFSFCQDLHHKCKNSRRQGCHQYVIHNNKCIPECPSGYTMNSSNLLCTPCLGPCPKVCHLLEGEKTIDSVTSAQELRGCTVINGSLIINIRGGNNLAAELEANLGLIEEISGYLKIRRSYALVSLSFFRKLRLIRGETLEIGNYSFYALDNQNLRQLWDWSKHNLTITQGKLFFHYNPKLCLSEIHKMEEVSGTKGRQERNDIALKTNGDQASCENELLKFSYIRTSFDKILLRWEPYWPPDFRDLLGFMLFYKEAPYQNVTEFDGQDACGSNSWTVVDIDPPLRSNDPKSQNHPGWLMRGLKPWTQYAIFVKTLVTFSDERRTYGAKSDIIYVQTDATNPSVPLDPISVSNSSSQIILKWKPPSDPNGNITHYLVFWERQAEDSELFELDYCLKGLKLPSRTWSPPFESEDSQKHNQSEYEDSAGECCSCPKTDSQILKELEESSFRKTFEDYLHNVVFVPRPSRKRRSLGDVGNVTVAVPTVAAFPNTSSTSVPTSPEEHRPFEKVVNKESLVISGLRHFTGYRIELQACNQDTPEERCSVAAYVSARTMPEAKADDIVGPVTHEIFENNVVHLMWQEPKEPNGLIVLYEVSYRRYGDEELHLCVSRKHFALERGCRLRGLSPGNYSVRIRATSLAGNGSWTEPTYFYVTDYLDVPSNIAKKLHHHHHH

Source

HEK293

Purity

Purity as determined by densitometric image analysis: >95%

SDS-PAGE Gel

8% SDS-PAGE separation of Human INSR Protein: 1. M.W. marker – 45, 66, 97 kDa 2. reduced and heated sample, 2.5μg/lane 3. non-reduced and non-heated sample, 2.5μg/lane

Endotoxin

<0.1 EU/µg

Formulation

Filtered (0.4 μm) and lyophilized in 0.5 mg/mL in 0.05 M phosphate buffer, 0.075 M NaCl, pH 7.4

Reconstitution

Add 100ul of deionized water to prepare a working stock solution of 0.5 mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

Applications

Western blotting, ELISA, Cell culture and/or animal studies

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store the lyophilized protein at –80 °C. Lyophilized protein remains stable until the expiry date when stored at –80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.

Summary

Research topic

Diabetology - Other Relevant Products, Diabetology - Insulin, C-Peptide, Proinsulin, Energy metabolism and body weight regulation, Oncology

Summary

Insulin receptor (IR) is an α2β2-disulfide linked tetrameric tyrosin kinase receptor located in the plasma membrane of target cells. This glycoprotein is composed of two extracellular α-subunits (731 amino acids; 135 kDa) containing the insulin binding site and two transmembrane β-subunits (620 amino acids; 95kDa) that possess intrinsic tyrosine kinase activity in their intracellular domains and transduce the insulin signal into the cell interior. The human insulin receptor is involved in glucose homeostasis, cell growth and differentiation. Binding of insulin leads to a conformational change of the receptor, resulting in ATP binding, autophosphory­lation, and subsequent phosphorylation of insulin receptor substrate proteins that are linked to the action of two main signalling pathways. The PI3-K/Akt pathway is involved in the glucose transport to the cell, induction of proliferation or inhibition of apoptosis, while the Ras/MAPK pathway is involved mainly in the control of cell growth and differentiation. Two insulin receptor variants are produced in mammals by alternative splicing: IR-A lacking exon 11 and the full length IR-B. The IR-A and IR-B isoforms show different ligand binding affinity. IR-A is a high-affinity receptor not only for insulin but also for IGF-II, while IR-B may be considered a specific receptor for insulin. Both insulin receptor isoforms are coexpressed in cells, and the relative abundance of IR-A and IR-B is regulated by development stage- and tissue-specific factors. IR-A is predominantly expressed in fetal and cancer cells, whereas IR-B is predominantly expressed in well-differentiated tissues including liver, adipose tissue and skeletal muscle. Dysregulation of insulin receptor splicing, i.e., increased IR-A expression in adult life, may play an underestimated role in cancer progression. Insulin receptor is overexpressed in several tumors, including breast, colon, lung, ovary, and thyroid carcinomas. Moreover, human lymphocyte-derived malignant cells, such as the IM-9 cells, are abundantly endowed with high-affinity insulin receptors. Circulating forms of several classes of receptor molecules and their fragments have been identified in human plasma. The human insulin receptor was found to be secreted into the incubation medium by various cultured cell lines and Schaefer et al. reported that transgenic mice expressing and secreting the soluble ectodomain of human insulin receptor into the plasma showed chronic hyperglycemia. Another study has shown that injection of the purified His-tagged human insulin receptor α-subunit into veins of mice increased in the concentration of blood glucose. The soluble human insulin receptor ectodomain, which contains α-subunit and a extracellular part of β-subunit, has been observed in human plasma of healthy individuals and observed at significantly elevated levels in plasma of patients with elevated blood glucose. Furthermore, the urinary soluble insulin receptor levels in patients with diabetes were also significantly higher than those in healthy volunteers and were significantly correlated with both urinary resistin and insulin levels.

Summary References (10)

References to Insulin Receptor

  • Belfiore A, Frasca F, Pandini G, Sciacca L, Vigneri R. Insulin receptor isoforms and insulin receptor/insulin-like growth factor receptor hybrids in physiology and disease. Endocr Rev. 2009 Oct;30 (6):586-623
  • Giudice J, Jares-Erijman EA, Leskow FC. Insulin receptor membrane retention by a traceable chimeric mutant. Cell Commun Signal. 2013;11 (1):45
  • Kanezaki Y, Matsushima R, Obata T, Nakaya Y, Matsumoto T, Ebina Y. Injection of the insulin receptor alpha subunit increases blood glucose levels in mice. Biochem Biophys Res Commun. 2003 Sep 26;309 (3):572-7
  • Malaguarnera R, Belfiore A. The insulin receptor: a new target for cancer therapy. Front Endocrinol (Lausanne). 2011;2:93
  • Papa V, Russo P, Gliozzo B, Goldfine ID, Vigneri R, Pezzino V. An intact and functional soluble form of the insulin receptor is secreted by cultured cells. Endocrinology. 1993 Sep;133 (3):1369-76
  • Sacco A, Morcavallo A, Pandini G, Vigneri R, Belfiore A. Differential signaling activation by insulin and insulin-like growth factors I and II upon binding to insulin receptor isoform A. Endocrinology. 2009 Aug;150 (8):3594-602
  • Schaefer EM, Viard V, Morin J, Ferre P, Penicaud L, Ramos P, Maika SD, Ellis L, Hammer RE. A new transgenic mouse model of chronic hyperglycemia. Diabetes. 1994 Jan;43 (1):143-53
  • Taniguchi CM, Emanuelli B, Kahn CR. Critical nodes in signalling pathways: insights into insulin action. Nat Rev Mol Cell Biol. 2006 Feb;7 (2):85-96
  • The Soluble Insulin Receptor Study Group. Soluble insulin receptor ectodomain is elevated in the plasma of patients with diabetes. Diabetes. 2007 Aug;56 (8):2028-35
  • Umehara A, Nishioka M, Obata T, Ebina Y, Shiota H, Hashida S. A novel ultra-sensitive enzyme immunoassay for soluble human insulin receptor ectodomain and its measurement in urine from healthy subjects and patients with diabetes mellitus. Clin Biochem. 2009 Sep;42 (13-14):1468-75
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