Inhibin beta A chain Recombinant Protein | INHBA recombinant protein

Recombinant Human Inhibin beta A chain

Cat. Num. AAA955336

• Gene Names: INHBA; EDF; FRP
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Inhibin beta A chain; 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
• Protein Family: Inhibin
• UniProt Gene Name: INHBA
• UniProt Synonym Gene Names: EDF
• UniProt Entry Name: INHBA_HUMAN

NCBI Description

The inhibin beta A subunit joins the alpha subunit to form a pituitary FSH secretion inhibitor. Inhibin has been shown to regulate gonadal stromal cell proliferation negatively and to have tumor-suppressor activity. In addition, serum levels of inhibin have been shown to reflect the size of granulosa-cell tumors and can therefore be used as a marker for primary as well as recurrent disease. Because expression in gonadal and various extragonadal tissues may vary severalfold in a tissue-specific fashion, it is proposed that inhibin may be both a growth/differentiation factor and a hormone. Furthermore, the beta A subunit forms a homodimer, activin A, and also joins with a beta B subunit to form a heterodimer, activin AB, both of which stimulate FSH secretion. Finally, it has been shown that the beta A subunit mRNA is identical to the erythroid differentiation factor subunit mRNA and that only one gene for this mRNA exists in the human genome. [provided by RefSeq, Jul 2008]

Uniprot Description

INHBA: 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. Belongs to the TGF-beta family.

Protein type: Secreted, signal peptide; Secreted

Chromosomal Location of Human Ortholog: 7p15-p13

Cellular Component: extracellular region; perinuclear region of cytoplasm

Molecular Function: cytokine activity; growth factor activity; hormone activity; identical protein binding; peptide hormone binding; protein binding; protein heterodimerization activity; transforming growth factor beta receptor binding

Biological Process: activin receptor signaling pathway; cell cycle arrest; cell development; cell differentiation; cell surface receptor linked signal transduction; cell-cell signaling; defense response; erythrocyte differentiation; G1/S transition of mitotic cell cycle; growth; hair follicle development; hemoglobin biosynthetic process; hemopoietic progenitor cell differentiation; male gonad development; mesodermal cell differentiation; negative regulation of B cell differentiation; negative regulation of cell cycle; negative regulation of cell growth; negative regulation of cell proliferation; negative regulation of follicle-stimulating hormone secretion; negative regulation of interferon-gamma biosynthetic process; negative regulation of macrophage differentiation; negative regulation of phosphorylation; nervous system development; odontogenesis; ovarian follicle development; palate development; positive regulation of cellular protein metabolic process; positive regulation of erythrocyte differentiation; positive regulation of follicle-stimulating hormone secretion; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription, DNA-dependent; progesterone secretion; regulation of follicle-stimulating hormone secretion; regulation of MAPKKK cascade; regulation of transcription from RNA polymerase II promoter; response to drug; striatal medium spiny neuron differentiation