Transforming Growth Factor beta2, Recombinant, Human (TGFb2, Polyergin, Cetermin, G-TSF, Glioblastoma-derived T-cell suppressor factor, BSC-1 cell growth inhibitor)

TGF-B is a multifunctional polypeptide growth factor. While specific receptors for this protein have been found on almost all mammalian cell types, the effect of the molecule varies depending on the cell type and growth conditions. Generally, TGF-B is stimulatory for cells of mesenchymal origin and inhibitory for cells of epithelial or neuroectodermal origin. It is a family of regulatory proteins consisting of a number of proteins distantly related. TGF-B1 has been found in the highest concentration in human platelets and mammalian bone, but is produced by many cell types in smaller amounts. TGF-B2 has been found in the highest concentration in porcine platelets and mammalian bone, but again is also produced by many types of cells. The heterodimer, TGF-B1.2, has so far been found only in small amounts in porcine platelets. TGF-B3 has been detected in human, porcine, and avian sources, mainly in cells of mesenchymal origin, suggesting a different role for this protein than for TGF-B1 or TGF-B2. TGF-B4 has been detected so far only in chick embryo chondrocytes, and its distribution in other types of cells has not yet been characterized. TGF-B5 has been detected only in Xenopus embryos. TGF-B1, TGF-B2, and TGF-B1.2 appear to be largely equivalent in biological activity, although there appear to be differences in binding to certain types of receptors, and there are a few reports of differential responses to TGF-B1 and TGF-B2.\n\nSource: \nRecombinant corresponding to 112aa from human Transforming Growth Factor beta2 expressed in E. coli.\n\nMolecular Weight: \n~25kD\n\nEndotoxin: ~0.1ng/ug\n\nBiological Activity: \nED50 (same/less than)0.2ng/ml ((same/more than)5x10e6units/mg), determined by its ability to inhibit the mouse IL-4 dependent proliferation of mouse HT-2 cells. TGF-b2 has growth inhibitory action and regulates the proliferation and differentiation of normal and transformed cells. Differential expression of TGF isoforms is observed in certain disease states. Human PC-3 prostatic carcinoma cell line and human glioblastoma cell lines predominantly secrete the TGF-b2 isoform over the other isoforms.\n\nStorage and Stability:\nLyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with sterile dH2O. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Reconstituted product is stable for 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

T8251-01

Size

5ug

Form

Supplied as a lyophilized powder from sodium citrate buffer, pH 3.5. Sterile filtered prior to lyophilization. Reconstitute with sterile ddH2O to a concentration of 0.1-1mg/ml. Do not vortex.

Purity

~98% (SDS-PAGE, HPLC). Purified by sequential chromatography.

References

[1] Madisen,L., Webb,N.R., Rose,T.M., Marquardt,H., Ikeda,T., Twardzik,D., Seyedin,S. and Purchio,A.F.\n Transforming growth factor-beta 2: cDNA cloning and sequence analysis\n[2] Webb,N.R., Madisen,L., Rose,T.M. and Purchio,A.F., et al.\n Structural and sequence analysis of TGF-beta 2 cDNA clones predicts two different precursor proteins produced by alternative mRNA splicing\n[3] , de Martin R., Haendler B., Hofer-Warbinek R., Gaugitsch H., Wrann M., Schluesener H., Seifert J.M., Bodmer S., Fontana A., Hofer E., et al.\n Complementary DNA for human glioblastoma-derived T cell suppressor factor, a novel member of the transforming growth factor-beta gene family.\n[4] , Madisen L., Webb N.R., Rose T.M., Marquardt H., Ikeda T., Twardzik D.R., Seyedin S., Purchio A.F.\n Transforming growth factor-beta 2: cDNA cloning and sequence analysis.\n[5] , Webb N.R., Madisen L., Rose T.M., Purchio A.F.\n Structural and sequence analysis of TGF-beta 2 cDNA clones predicts two different precursor proteins produced by alternative mRNA splicing.\n[6] , Rieder M.J., Livingston R.J., Daniels M.R., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., et al.\n NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).\n[7] , Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., Altschul S.F., et al.\n Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.\n[8] , Noma T., Glick A.B., Geiser A.G., O'Reilly M.A., Miller J., Roberts A.B., Sporn M.B.\n Molecular cloning and structure of the human transforming growth factor-beta 2 gene promoter.\n[9] , Marquardt H., Lioubin M.N., Ikeda T.\n Complete amino acid sequence of human transforming growth factor type beta 2.\n[10] , Daopin S., Piez K.A., Ogawa Y., Davies D.R.\n Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily.