Inhibin beta A chain Recombinant Protein | INHBA recombinant protein

Recombinant Human Inhibin beta A chain

Cat. Num. AAA113519

• Gene Names: INHBA; EDF; FRP
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Inhibin beta A chain; N/A; Recombinant Human Inhibin beta A chain; Activin beta-A chain; Erythroid differentiation protein; EDF; INHBA recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 311-426. Full Length of Mature Protein
• Sequence: GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for INHBA recombinant protein

Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.

Product Categories/Family for INHBA recombinant protein

Signal Transduction

References

Structure of two human ovarian inhibins.Mason A.J., Niall H.D., Seeburg P.H.Biochem. Biophys. Res. Commun. 135:957-964(1986) Erythroid differentiation factor is encoded by the same mRNA as that of the inhibin beta A chain.Murata M., Eto Y., Shibai H., Sakai M., Muramatsu M.Proc. Natl. Acad. Sci. U.S.A. 85:2434-2438(1988) Structure and sequence analysis of the human activin beta A subunit gene.Tanimoto K., Handa S.I., Ueno N., Murakami K., Fukamizu A.DNA Seq. 2:103-110(1991) The DNA sequence of human chromosome 7.Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.Nature 424:157-164(2003) Human inhibin genes. Genomic characterisation and sequencing.Stewart A.G., Milborrow H.M., Ring J.M., Crowther C.E., Forage R.G.FEBS Lett. 206:329-334(1986) Berg H., Walter M., Northemann W. Differential binding and neutralization of activins A and B by follistatin and follistatin like-3 (FSTL-3/FSRP/FLRG) .Schneyer A., Schoen A., Quigg A., Sidis Y.Endocrinology 144:1671-1674(2003) Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-beta ligand:receptor interactions.Thompson T.B., Woodruff T.K., Jardetzky T.S.EMBO J. 22:1555-1566(2003) The structure of FSTL3.activin A complex. Differential binding of N-terminal domains influences follistatin-type antagonist specificity.Stamler R., Keutmann H.T., Sidis Y., Kattamuri C., Schneyer A., Thompson T.B.J. Biol. Chem. 283:32831-32838(2008) Germline mutations of inhibins in early-onset ovarian epithelial tumors.Tournier I., Marlin R., Walton K., Charbonnier F., Coutant S., Thery J.C., Charbonnier C., Spurrell C., Vezain M., Ippolito L., Bougeard G., Roman H., Tinat J., Sabourin J.C., Stoppa-Lyonnet D., Caron O., Bressac-de Paillerets B., Vaur D., King M.C., Harrison C., Frebourg T.Hum. Mutat. 35:294-297(2014)

NCBI and Uniprot Product Information

• NCBI GI #: 4504699
• NCBI GeneID: 3624
• NCBI Accession #: NP_002183.1
• NCBI GenBank Nucleotide #: NM_002192.2
• UniProt Accession #: P08476; Q14599
• Molecular Weight: 29 kDa
• NCBI Official Full Name: inhibin beta A chain
• NCBI Official Synonym Full Names: inhibin beta A
• NCBI Official Symbol: INHBA
• NCBI Official Synonym Symbols: EDF; FRP
• NCBI Protein Information: inhibin beta A chain
• UniProt Protein Name: Inhibin beta A chain
• UniProt Gene Name: INHBA
• UniProt Synonym Gene Names: EDF
• UniProt Entry Name: INHBA_HUMAN