Render Target: STATIC
Render Timestamp: 2024-12-06T12:20:44.935Z
Commit: 224419269841c11382c4555dbee545259bf6c379
XML generation date: 2024-11-18 21:16:11.173
Product last modified at: 2024-11-19T08:01:35.573Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Cleaved TGF-β1 (Ala279)/ TGF-β2 (Ala303)/ TGF-β3 (Ala301) Antibody #84912

Filter:
  • WB

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 12
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Cleaved TGF-β1 (Ala279)/ TGF-β2 (Ala303)/ TGF-β3 (Ala301) Antibody recognizes endogenous levels of TGF-β1,2,3 proteins only when cleaved at Ala279, Ala303, and Ala301, respectively. This antibody does not cross-react with full-length TGF-β1, TGF-β2, or TGF-β3.

    Species Reactivity:

    Human

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with synthetic peptides corresponding to residues adjacent to Ala279, Ala303, and Ala301 of human TGF-β1,2,3 proteins, respectively. Antibodies are purified by peptide affinity chromatography.

    Background

    Transforming growth factor-β (TGF-β) proteins belong to the TGF-β superfamily of cytokines that play a critical role in regulating cell proliferation and differentiation, developmental patterning and morphogenesis, and disease pathogenesis (1-3). TGF-β ligands elicit signaling through three cell surface receptors: type I (RI), type II (RII), and type III (RIII) TGF-β receptors. Type I and type II receptors are serine/threonine kinases that form a heteromeric complex following ligand binding to the type II receptor. In response to ligand binding, the type II receptors form a stable complex with the type I receptors, triggering phosphorylation and activation of the type I receptor (4). This results in the recruitment of receptor-mediated SMADs (SMAD2, SMAD3), which are phosphorylated by the type I kinase in an SSXS domain in the C-terminus. This leads to recruitment of the co-SMAD (SMAD4), and subsequent translocation of this heteromeric SMAD complex to the nucleus, where it regulates transcription of target genes (5-7). The type III receptor, also known as betaglycan, is a transmembrane proteoglycan with a large extracellular domain that binds TGF-β with high affinity but lacks a cytoplasmic signaling domain. Expression of the type III receptor can regulate TGF-β signaling through presentation of the ligand to the signaling complex (8).

    There are three TGF-β family members, designated TGF-β1, TGF-β2, and TGF-β3, which are encoded by distinct genes and are expressed in a tissue-specific manner (10). TGF-β proteins are synthesized as precursor proteins that are cleaved and reassembled in association with other proteins to form latent complexes. Activation occurs by proteolytic release of TGF-β monomers, which dimerize to form the mature TGF-β ligands.
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