Reconstitute with 20mM Tris and 150mM NaCl to 0.1-1.0mg/ml. Do not vortex. Lyophilized from 20mM Tris, 150mM NaCl, 1mM EDTA, 1mM DTT, 0.01% SKL, 5% Trehalose, ProClin 300.
Expression System:
E. coli
Form:
Lyophilized powder
Sequence:
N-terminal His-Tag, Ala331~Ser442 (NP_112393.1)
Application Notes:
Transforming growth factor-beta 2 (TGF-beta2) is a secreted protein known as a cytokine that performs many cellular functions and has a vital role during embryonic development (alternative names: Glioblastoma-derived T-cell suppressor factor, G-TSF, BSC-1 cell growth inhibitor, Polyergin, Cetermin). It is an extracellular glycosylated protein. It is known to suppress the effects of interleukin dependent T-cell tumors. Besides, Vitronectin (VTN) has been identified as an interactor of TGF-beta2, thus a binding ELISA assay was conducted to detect the interaction of recombinant rat TGF-beta2 and recombinant rat VTN. Briefly, TGF-beta2 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 µl were then transferred to VTN-coated microtiter wells and incubated for 2h at 37C. Wells were washed with PBST and incubated for 1h with anti-TGF-beta2 pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37C. Finally, add 50 µl stop solution to the wells and read at 450nm immediately. The binding activity of TGF-beta2 and VTN was in a dose dependent manner.
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