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Insulin Receptor antibody (INSR)

Details for Product anti-INSR Antibody No. ABIN968448, Supplier: Login to see
Antigen
  • 18402
  • CG18402
  • DIHR
  • DILR
  • DIR
  • DIRH
  • DIRbeta
  • DInR
  • DInr
  • Dir-a
  • Dir-b
  • Dmel\\CG18402
  • INR
  • INS
  • IR
  • 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
  • INSR
  • NV14476
  • CD220
  • HHF5
  • 4932439J01Rik
  • D630014A15Rik
  • IR-A
  • IR-B
  • ir-A
  • ir
  • cd220
  • hhf5
  • CTK-1
Alternatives
anti-Human Insulin Receptor antibody for Enzyme Immunoassay
Reactivity
Human, Mouse (Murine), Rat (Rattus)
270
78
54
10
6
5
3
2
1
1
1
1
1
1
1
1
Host
Rabbit
218
82
3
Clonality
Polyclonal
Conjugate
This Insulin Receptor antibody is un-conjugated
21
16
9
9
7
7
1
1
1
1
1
1
1
1
1
1
1
1
Application
Immunofluorescence (IF), Western Blotting (WB)
166
122
53
44
32
18
18
11
10
10
10
8
8
7
2
2
1
1
1
Supplier
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Isotype Ig
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.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name CD220 (INSR Antibody Abstract)
Background 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.
Molecular Weight 95 kDa
Pathways NF-kappaB Signaling, RTK Signaling, AMPK Signaling
Comment

Related Products: ABIN968548, ABIN967390

Restrictions For Research Use only
Format Liquid
Concentration 250 µg/ml
Buffer Aqueous buffered solution containing BSA, glycerol.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
Western Blotting (WB) image for anti-Insulin Receptor antibody (INSR) (ABIN968448) Western blot analysis of CD220 (Insulin receptor beta) on a rat liver lysate. Lane 1:...
Immunofluorescence (IF) image for anti-Insulin Receptor antibody (INSR) (ABIN968448) Immunofluorescence staining of rat neurons.
Product cited in: 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).

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).

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).

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).

White, Kahn: "The insulin signaling system." in: The Journal of biological chemistry, Vol. 269, Issue 1, pp. 1-4, 1994 (PubMed).