|Tested applications||WB IHC FC|
|Recommended Dilution||WB 1:500 - 1:2000
IHC 1:50 - 1:200
FC 1:50 - 1:200|
|Observed MW||Refer to Figures|
|Immunogen||Recombinant protein of human TGFB1|
|Storage Buffer||Store at -20℃. Avoid freeze / thaw cycles.
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.|
Transforming growth factor-β (TGFB1) superfamily members are critical regulators of cell proliferation and differentiation, developmental patterning and morphogenesis, and disease pathogenesis (1-4). TGFB1 elicits signaling through three cell surface receptors: type I (RI), type II (RII) and type III (RIII). Type I and type II receptors are serine/threonine kinases that form a heteromeric complex. In response to ligand binding, the type II receptors form a stable complex with the type I receptors allowing phosphorylation and activation of type I receptor kinases (5). The type III receptor, also known as betaglycan, is a transmembrane proteoglycan with a large extracellular domain that binds TGFB1 with high affinity but lacks a cytoplasmic signaling domain (6,7). Expression of the type III receptor can regulate TGFB1 signaling through presentation of the ligand to the signaling complex. The only known direct TGFB1 signaling effectors are the Smad family proteins, which transduce signals from the cell surface directly to the nucleus to regulate target gene transcription (8,9).There are three isoforms of TGF-beta designated TGF-beta1, TGF-beta2, and TGF-beta3, which are encoded by distinct genes and are expressed in a tissue specific manner (10). Each of the isoforms are synthesized as larger precursor proteins containing a propeptide region which gets cleaved prior to secretion from the cell. Mature TGF-beta contains two polypeptides linked linked by disulfide bonds forming a protein of about 25 kDa.
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