Human TGFBR3 recombinant protein with polyhistidine tag at the C-terminus expressed in Escherichia coli.
Sequence:
MALDTNYCFRNLEENCCVRPLYIDFRQDLGWKWVHEPKGYYANFCSGPCPYLRSADTTHSTVLGLYNTLNPEASASPCCVPQDLEPLTILYYVGRTPKVEQLSNMVVKSCKCS with polyhistidine tag at the C-terminus.
Host:
Escherichia coli
Form:
Lyophilized
Preparation Method:
Escherichia coli expression system
Purification:
Ni-NTA chromatography
Purity:
> 98% as determined by SDS-PAGE.
Endotoxin Level:
< 0.1 EU/ ug of protein by the LAL method.
Activity:
ED50 < 50 pg/mL, measure by its ability to inhibit IL-4-induce proliferation in HT-2 cells. The specific activity of recombinant human TGF beta 3 is > 2 x 107 IU/mg.
Quality Control Testing:
SDS-PAGE Stained with Coomassie Blue.
SDS-PAGE analysis of TGFBR3 (Human) Recombinant Protein.
Recommend Usage:
Biological Activity SDS-PAGE The optimal working dilution should be determined by the end user.
Storage Buffer:
Lyophilized from a solution containing 20 mM sodium citrate, 0.2 M NaCl, pH 3.5. Reconstitute the lyophilized powder in ddH2O to 100 ug/mL. In some experiments, it recommends to add 10 mM HCl when reconstitute lyophilized protein.
Storage Instruction:
Lyophilized protein should be stored at -20°C. Protein aliquots should be stored at-20°C to -80°C. Avoid repeated freeze/thaw cycles.
Transforming growth factor (TGF)-beta is a multifunctional cytokine that modulates several tissue development and repair processes, including cell differentiation, cell cycle progression, cellular migration, adhesion, and extracellular matrix production. Three TGF-beta forms are encoded by separate genes: TGFB1 (MIM 190180), TGFB2 (MIM 190220), and TGFB3 (MIM 190230). The diverse effects of TGF-beta are mediated by the TGF-beta receptors and cell surface-binding proteins. Three TGF-beta receptors exist: type I (TGFBR1; MIM 190181), type II (TFGBR2; MIM 190182), and type III (TGFBR3). TGFBR3 is a glycoprotein that binds TGFB and exists in both a membrane-bound and a soluble form (Johnson et al., 1995 [PubMed 8530052]).[supplied by OMIM