Insulin Receptor (INSR) (Extracellular Domain), (AA 1-944) (Active) protein (His tag)

Details for Product No. ABIN2003949, Supplier: Log in to see
Protein Name
  • CD220
  • HHF5
  • 4932439J01Rik
  • D630014A15Rik
  • IR
  • IR-A
  • IR-B
  • 18402
  • CG18402
  • DIHR
  • DILR
  • DIR
  • DIRH
  • DIRbeta
  • DInR
  • DInr
  • Dir-a
  • Dir-b
  • Dmel\\CG18402
  • INR
  • INS
  • Inr
  • Inr-alpha
  • Inr-beta
  • InsR
  • dINR
  • dIR
  • dIRH
  • dInR
  • dInr
  • dInsR
  • dinr
  • dir
  • er10
  • inr
  • insulin/insulin-like growth factor receptor
  • l(3)05545
  • l(3)93Dj
  • l(3)er10
  • lnR
  • ir-A
  • CTK-1
  • ir
  • INSR
  • NV14476
  • cd220
  • hhf5
  • insulin receptor
  • Insulin-like receptor
  • insulin receptor L homeolog
  • INSR
  • Insr
  • InR
  • LOC100122567
  • LOC100451802
  • insr.L
Protein Characteristics
Extracellular Domain, AA 1-944
3
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Origin
Human
23
7
4
1
1
Source
Human Cells
13
9
3
3
2
1
1
Protein Type
Recombinant
Biological Activity
Active
Purification tag / Conjugate
This Insulin Receptor protein is labelled with His tag.
Application
Functional Studies (Func), SDS-PAGE (SDS)
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Characteristics The secreted recombinant human INSR isoform short consists of 928 amino acids and has a predicted molecular mass of 106 (83+23) kDa. As a result of glycosylation, the apparent molecular mass of rhINSR is approximately 125-135 kDa & 40-45 kDa, corresponding to the α subunit and the ECD of β subunit respectively in SDS-PAGE under reducing conditions.

Protein Structure: A DNA sequence encoding the human INSR isoform short (NP_001073285.1) extracellular domain (Met 1-Lys 944) was expressed, fused with a polyhistidine tag at the C-terminus.
Predicted N-Term: His 28 & Ser 751
Purity > 95 % as determined by SDS-PAGE
Endotoxin Level < 1.0 EU per μg of the protein as determined by the LAL method
Biological Activity Comment Measured by its ability to bind human Insulin in a functional ELISA.
Background Synonyms: CD220,HHF5,Insulin Receptor
Molecular Weight 125-135 kDa, 40-45 kDa
NCBI Accession NP_001073285
Pathways NF-kappaB Signaling, RTK Signaling, AMPK Signaling, Carbohydrate Homeostasis, Regulation of Cell Size, Regulation of Carbohydrate Metabolic Process, Growth Factor Binding, Negative Regulation of Transporter Activity
Application Notes Optimal working dilution should be determined by the investigator.
Restrictions For Research Use only
Format Lyophilized
Buffer Lyophilized from sterile PBS, pH 7.4
Normally 5 % - 8 % trehalose, mannitol and 0.01 % Tween80 are added as protectants before lyophilization.
Handling Advice Avoid repeated freeze-thaw cycles. It is recommended that the protein be aliquoted for optimal storage.
Storage -20 °C,-80 °C
Storage Comment Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Shipping: In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Expiry Date 12 months
Supplier Images
 image for Insulin Receptor (INSR) (Extracellular Domain), (AA 1-944) (Active) protein (His tag) (ABIN2003949) Insulin Receptor (INSR) (Extracellular Domain), (AA 1-944) (Active) protein (His tag)
Product cited in: Morcavallo, Buraschi, Xu, Belfiore, Schaefer, Iozzo, Morrione: "Decorin differentially modulates the activity of insulin receptor isoform A ligands." in: Matrix biology : journal of the International Society for Matrix Biology, Vol. 35, pp. 82-90, 2014 (PubMed).

Background publications Akhter, Struebing, Larsen, Gallagher, Ecklund, Henley, Mack-Shipman, Duckworth: "Determination of insulin requirements: excessive insulin dosages common in type 1 diabetes mellitus." in: Endocrine practice : official journal of the American College of Endocrinology and the American Association of Clinical Endocrinologists, Vol. 4, Issue 3, pp. 133-6, 2004 (PubMed).

Maddux, Goldfine: "Membrane glycoprotein PC-1 inhibition of insulin receptor function occurs via direct interaction with the receptor alpha-subunit." in: Diabetes, Vol. 49, Issue 1, pp. 13-9, 2000 (PubMed).

Kan, Kanai, Iida, Jinnouchi, Todaka, Imanaka, Ito, Nishioka, Ohnishi, Kamohara: "Frequency of mutations of insulin receptor gene in Japanese patients with NIDDM." in: Diabetes, Vol. 44, Issue 9, pp. 1081-6, 1995 (PubMed).

Kadowaki, Kadowaki, Accili, Taylor et al.: "Substitution of lysine for asparagine at position 15 in the alpha-subunit of the human insulin receptor. A mutation that impairs transport of receptors to the cell surface and decreases the affinity ..." in: The Journal of biological chemistry, Vol. 265, Issue 31, pp. 19143-50, 1990 (PubMed).

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