Transforming growth factor bs (TGFbs) were originally discovered due to their ability to promote anchorage-independent growth of rat NRK fibroblasts in the presence of TGFa. It is now realized that TGFbs mediate many cell-cell interactions that occur during embryonic development. Three TGFbs have been identified in mammals. TGFb1, TGFb2 and TGFb3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecules. Biologically active TGFb requires dimerization of the monomers (usually homodimers) and release of the latent peptide portion. Overall, the mature region of the TGFb3 protein has approximately 80% identity to the mature region of both TGFb1 and TGFb2. However, the NH2 terminals or precursor regions of their molecules share only 27% sequence identity.
200ug/ml of Ab purified from Bioreactor Concentrate by Protein A/G. Prepared in 10mM PBS with 0.05% BSA & 0.05% azide. Also available WITHOUT BSA & azide at 1.0mg/ml.
SDS-PAGE Analysis of Purified TGF beta 2 Mouse Monoclonal Antibody (TGFB2/1679). Confirmation of Purity and Integrity of Antibody.
Formalin-fixed, paraffin-embedded human prostate carcinoma stained with TGF beta 2 Mouse Monoclonal Antibody (TGFB2/1679). Inset: PBS instead of primary antibody, secondary only negative control.
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