Cleaved TGF-β1 (Ala279)/ TGF-β3 (Ala301) (E5L1D) Rabbit mAb #70667

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Supporting Data

REACTIVITY	H
SENSITIVITY	Endogenous
MW (kDa)	12
Source/Isotype	Rabbit IgG

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, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

Protocol

Specificity / Sensitivity

Cleaved TGF-β1 (Ala279)/ TGF-β3 (Ala301) (E5L1D) Rabbit mAb recognizes endogenous levels of TGF-β1 and TGF-β3 proteins only when cleaved at Ala279 and Ala301, respectively. This antibody does not cross-react with full-length TGF-β1, TGF-β2, or TGF-β3, nor does it react with cleaved TGF-β2. Upper bands present in human platelet and K-562 lanes are non-specific.

Species Reactivity:

Human

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues adjacent to Ala279 and Ala301 of human TGF-β1 and TGF-β3 proteins, respectively.

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.

Database Links

UniProt ID: P61812 , P01137 , P10600

Entrez-Gene Id: 7042 , 7040 , 7043

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