INSR Human

Insulin Receptor Human Recombinant
Cat. No.
BT18945
Source
HEK 293.
Synonyms
Insulin receptor, IR, EC 2.7.10.1, CD220, INSR, HHF5.
Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock
Quick Inquiry

Description

Insulin Receptor Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (aa 28-944 of the short isoform- HIR-A, Uniprot accession # P06213-2 which includes the whole subunit alpha and extracellular domain of subunit beta) containing a total of 927 amino acids, having a molecular mass of 105.9kDa (calculated), though it migrates at approximately 160kDa on SDS PAGE, the INSR is fused to a 2 a.a N-terminal linker, a 2 a.a C-terminal linker and fused to a 6 a.a His tag at C-Terminus.
The Human INSR is purified by proprietary chromatographic techniques.

Product Specs

Introduction
The insulin receptor (INSR) is a receptor tyrosine kinase that plays a crucial role in mediating the diverse effects of insulin. Upon insulin binding to INSR, glucose uptake is stimulated. The INSR precursor undergoes post-translational cleavage into two chains, alpha and beta, which are covalently linked, following the removal of the precursor signal peptide. Insulin binding triggers the phosphorylation of various intracellular substrates, including insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL, and other signaling intermediaries. These phosphorylated proteins act as docking sites for signaling proteins containing Src-homology-2 domains (SH2 domain), which specifically recognize different phosphotyrosine residues. Notable examples include the p85 regulatory subunit of PI3K and SHP2.
Description
Recombinant Human Insulin Receptor, produced in HEK cells, is a single, glycosylated polypeptide chain encompassing amino acids 28-944 of the short isoform (HIR-A, Uniprot accession # P06213-2). This includes the complete alpha subunit and the extracellular domain of the beta subunit. It comprises a total of 927 amino acids, resulting in a calculated molecular mass of 105.9 kDa. However, it migrates at approximately 160 kDa on SDS-PAGE. The INSR is fused to a 2 amino acid N-terminal linker, a 2 amino acid C-terminal linker, and a 6 amino acid His tag at the C-terminus. The purification of Human INSR is achieved through proprietary chromatographic techniques.
Physical Appearance
White lyophilized powder that appears white after filtration.
Formulation
INSR underwent filtration at 0.4 µm and subsequent lyophilization from a solution of 0.5 mg/ml in 0.05 M phosphate buffer and 0.075 M NaCl, pH 7.4.
Solubility

To prepare a working solution, it is recommended to add deionized water to achieve a concentration of 0.5 mg/ml. Allow the lyophilized pellet to dissolve completely. Please note that INSR is not sterile. Before using it in cell culture, ensure to filter the product through an appropriate sterile filter.

Stability
The lyophilized protein should be stored at -20°C. After reconstitution, aliquot the product to prevent repeated freeze-thaw cycles. The reconstituted protein remains stable at 4°C for a limited period.
Purity
The purity of the protein is determined to be greater than 95.0% based on SDS-PAGE analysis.
Synonyms
Insulin receptor, IR, EC 2.7.10.1, CD220, INSR, HHF5.
Source
HEK 293.
Amino Acid Sequence
ASHLYPGEVC PGMDIRNNLT RLHELENCSV IEGHLQILLM FKTRPEDFRD LSFPKLIMIT DYLLLFRVYG LESLKDLFPN LTVIRGSRLF FNYALVIFEM VHLKELGLYN LMNITRGSVR IEKNNELCYL ATIDWSRILD SVEDNYIVLN KDDNEECGDI CPGTAKGKTN CPATVINGQF VERCWTHSHC QKVCPTICKS HGCTAEGLCC HSECLGNCSQ PDDPTKCVAC RNFYLDGRCV ETCPPPYYHF QDWRCVNFSF CQDLHHKCKN SRRQGCHQYV IHNNKCIPEC PSGYTMNSSN LLCTPCLGPC PKVCHLLEGE KTIDSVTSAQ ELRGCTVING SLIINIRGGN NLAAELEANL GLIEEISGYL KIRRSYALVS LSFFRKLRLI RGETLEIGNY SFYALDNQNL RQLWDWSKHN LTITQGKLFF HYNPKLCLSE IHKMEEVSGT KGRQERNDIA LKTNGDQASC ENELLKFSYI RTSFDKILLR WEPYWPPDFR DLLGFMLFYK EAPYQNVTEF DGQDACGSNS WTVVDIDPPL RSNDPKSQNH PGWLMRGLKP WTQYAIFVKT LVTFSDERRT YGAKSDIIYV QTDATNPSVP LDPISVSNSS SQIILKWKPP SDPNGNITHY LVFWERQAED SELFELDYCL KGLKLPSRTW SPPFESEDSQ KHNQSEYEDS AGECCSCPKT DSQILKELEE SSFRKTFEDY LHNVVFVPRP SRKRRSLGDV GNVTVAVPTV AAFPNTSSTS VPTSPEEHRP FEKVVNKESL VISGLRHFTG YRIELQACNQ DTPEERCSVA AYVSARTMPE AKADDIVGPV THEIFENNVV HLMWQEPKEP NGLIVLYEVS YRRYGDEELH LCVSRKHFAL ERGCRLRGLS PGNYSVRIRA TSLAGNGSWT EPTYFYVTDY LDVPSNIAKK LHHHHHH.

Product Science Overview

Structure and Function

The insulin receptor belongs to the protein kinase superfamily and exists as a tetramer consisting of two alpha subunits and two beta subunits linked by disulfide bonds . The alpha subunits are extracellular and contain the insulin-binding domain, while the beta subunits span the cell membrane and possess tyrosine kinase activity . Upon insulin binding, the receptor undergoes autophosphorylation, which triggers a cascade of downstream signaling pathways, including the activation of insulin receptor substrates (IRS) and phosphatidylinositol 3-kinase (PI3K) .

Recombinant Human Insulin Receptor

Recombinant DNA technology has enabled the production of human insulin receptor proteins in various host systems, such as HEK293 cells . The recombinant human insulin receptor is typically expressed as a fusion protein with a polyhistidine tag for easy purification . This technology allows for the production of high-purity, biologically active insulin receptor proteins that are used in research and therapeutic applications.

Applications

The recombinant human insulin receptor is widely used in biomedical research to study insulin signaling pathways and to develop new therapeutic strategies for diabetes and other metabolic disorders . It is also used in drug discovery to screen for potential insulin mimetics and other compounds that can modulate insulin receptor activity .

Stability and Storage

Recombinant human insulin receptor proteins are usually provided as lyophilized powders and are stable for up to twelve months when stored at -20°C to -80°C under sterile conditions . It is recommended to aliquot the protein to avoid repeated freeze-thaw cycles, which can degrade the protein .

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *

Category

Service

Related Products

Insulin Human, His
Insulin Human Recombinant, His Tag
Cat. No.
BT19124
Source
Escherichia Coli.
THE BIOTEK
THE BioTek is a global biotech company offering highly purified proteins for research in cancer, apoptosis, development, endocrinology, immunology, neuroscience, proteases, and stem cells.
  • Contact
  • Address: 1925 E Maple Ave, El Segundo, CA 90245 United States
  • Phone : +1 201-285-7826
  • Email : info@thebiotek.com
  • Hours : Mon.-Fri. 9:00 AM - 5:00 PM
© Copyright 2024 Thebiotek. All Rights Reserved.