Insulin Receptor (INSR) antibody
| Antigen | Insulin Receptor (INSR) |
| Synonyms |
HHF5, CD220, IR, 4932439J01Rik, D630014A15Rik, DIHR, DILR, DIR, DIRH, DIRbeta, DInR, Dir-a, Dir-b, INR, Inr-alpha, Inr-beta, InsR, dInsR, er10, insulin/insulin-like growth factor receptor, l(3)05545, ...
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| Clonality | Polyclonal |
| Host |
Alternatives Rabbit |
| Reactivity |
Alternatives Rat (Rattus), Mouse (Murine), Human |
| Conjugate |
Alternatives Un-conjugated |
| Application |
Alternatives Western Blotting (WB), Immunofluorescence (IF) |
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5 references available |
| Catalog no. | ABIN968448 |
| Quantity | 50 µg (250 µg/ml) (Variants) |
| Price | Product not available in this region. |
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Additional Information
| Alternative name | CD220 |
| Format | Liquid |
| Isotype | Ig |
| Description |
The Insulin Receptor (IR), also known as CD220, is a transmembrane receptor tyrosine kinase which, upon insulin binding, initiates a cascade of events, including autophosphorylation, phosphorylation of cellular protein substrates, glucose transport, and glycogen synthesis. IR is synthesized as a large glycosylated precursor that is cleaved upon maturation into a 130 kDa alpha-subunit with kinase activity and a 95 kDa beta-chain. The active Insulin Receptor is a heterotetramer of homologous alpha and beta subunits joined by disulfide bonds. Among the major cytosolic substrates of the Insulin Receptor are IRS-1 and -2, beta-Adrenergic receptor, and pp15 (adipocyte lipid-binding protein, ALBP). Autophosphorylation of the IR recruits IRS-1 and -2 act as docking sites for other signaling proteins like PI3-Kinase, Shc, PTP1D, Nck, etc. In addition, the phosphatase LAR is tightly associated with the IR and LAR becomes activated after insulin stimulation dephosphorylating the IR and its substrates. Therefore, LAR provides a turn-off mechanism in insulin signaling. This antibody was generated using the human insulin pro-receptor beta-subunit aa. 1212-1381. |
| Characteristics |
1. Since applications vary, each investigator should titrate the reagent to obtain optimal results. 2. Source of all serum proteins is from USDA inspected abattoirs located in the United States. 3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing. 4. Please refer to us for technical protocols. |
| Molecular Weight | 95 kDa |
| Comments |
Related Products: ABIN968548, ABIN967390 |
| Synonyms | HHF5, CD220, IR, 4932439J01Rik, D630014A15Rik, DIHR, DILR, DIR, DIRH, DIRbeta, DInR, Dir-a, Dir-b, INR, Inr-alpha, Inr-beta, InsR, dInsR, er10, insulin/insulin-like growth factor receptor, l(3)05545, l(3)93Dj, l(3)er10, DmelCG18402, CG18402, INSR, ir-A, CTK-1, ir, NV14476 |
Application Details
| Concentration | 250 µg/ml |
| Purity | Purified |
| Purification | Purified from tissue culture supernatant or ascites by affinity chromatography. |
| Buffer | Aqueous buffered solution containing BSA, glycerol. |
| Preservative | 0.09% Sodium azide. |
| Storage | Store undiluted at -20° C. |
| Restrictions | For Research Use only |
Images
Publications
| Product |
White, Kahn: "The insulin signaling system." in: The Journal of biological chemistry, Vol. 269, Issue 1, pp. 1-4, 1994 (PubMed).
Lu, Guidotti: "Identification of the cysteine residues involved in the class I disulfide bonds of the human insulin receptor: properties of insulin receptor monomers." in: Molecular biology of the cell, Vol. 7, Issue 5, pp. 679-91, 1997 (PubMed). Kasus-Jacobi, Béréziat, Perdereau et al.: "Evidence for an interaction between the insulin receptor and Grb7. A role for two of its binding domains, PIR and SH2." in: Oncogene, Vol. 19, Issue 16, pp. 2052-9, 2000 (PubMed). Parpal, Karlsson, Thorn et al.: "Cholesterol depletion disrupts caveolae and insulin receptor signaling for metabolic control via insulin receptor substrate-1, but not for mitogen-activated protein kinase control." in: The Journal of biological chemistry, Vol. 276, Issue 13, pp. 9670-8, 2001 (PubMed). Swindle, Tran, Johnson et al.: "Epidermal growth factor (EGF)-like repeats of human tenascin-C as ligands for EGF receptor." in: The Journal of cell biology, Vol. 154, Issue 2, pp. 459-68, 2001 (PubMed). |
Alternatives
Alternatives for antigen "Insulin Receptor (INSR)", type "Antibodies"




Alternatives