Anti-Insulin Receptor β Rabbit Antibody [C9B17]

Catalog No.: F4144

    Application: Reactivity:

    Usage Information

    Dilution
    1:1000
    1:100
    1:50 - 1:200
    1:50 - 1:200
    1:50 - 1:200
    Application
    WB, IP, IHC, IF , FCM
    Reactivity
    Mouse, Rat, Human
    Source
    Rabbit
    Storage Buffer
    PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3
    Storage (from the date of receipt)
    -20°C (avoid freeze-thaw cycles), 2 years
    Predicted MW
    95 kDa, 220 kDa

    Datasheet & SDS

    Biological Description

    Specificity
    Anti-Insulin Receptor β Rabbit Antibody [C9B17] detects endogenous levels of total Insulin Receptor β protein.
    Clone
    C9B17
    Synonym(s)
    Insulin receptor, IR, Insulin receptor subunit alpha, Insulin receptor subunit beta, CD220, INSR
    Background
    Insulin receptor β (IR-β) is one of the two subunits forming the insulin receptor, a heterotetrameric protein complex consisting of two extracellular α-subunits and two transmembrane β-subunits. The β-subunit spans the cell membrane and includes an intracellular tyrosine kinase domain crucial for signal transduction. Upon insulin binding to the α-subunits, the receptor undergoes conformational changes that activate the β-subunit’s kinase domain through autophosphorylation of specific tyrosine residues. This phosphorylation event triggers downstream signaling pathways such as PI3K/Akt and MAPK, which regulate glucose transport, metabolism, cell growth, and gene expression. The β-subunit contains extracellular fibronectin type III domains (FnIII-2 and FnIII-3), a transmembrane region, and the intracellular kinase domain. The activation mechanism is a tightly controlled stepwise process involving structural changes that bring the intracellular kinase domains into proximity to facilitate trans-autophosphorylation. Regulation of IR-β involves not only tyrosine phosphorylation for activation but also serine/threonine phosphorylation, which can negatively regulate receptor activity and contribute to insulin resistance. Additionally, post-translational modifications like glycosylation affect its proper folding, trafficking, and surface expression. Abnormalities in IR-β function, such as impaired autophosphorylation or altered receptor expression, are linked to insulin resistance and the pathogenesis of type 2 diabetes and other metabolic disorders.
    References
    • https://pubmed.ncbi.nlm.nih.gov/2986534/
    • https://pubmed.ncbi.nlm.nih.gov/37779149/

    Tech Support

    Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

    Handling Instructions

    Tel: +1-832-582-8158 Ext:3
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