product summary
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company name :
MyBioSource
product type :
protein
product name :
Recombinant Human Inhibin beta A chain
catalog :
MBS955336
quantity :
0.05 mg (E-Coli)
price :
190 USD
more info or order :
product information
catalog number :
MBS955336
products type :
Recombinant Protein
products full name :
Recombinant Human Inhibin beta A chain
products short name :
Inhibin beta A chain
products name syn :
Activin beta-A chain; Erythroid differentiation protein; EDF
other names :
inhibin beta A chain; Inhibin beta A chain; inhibin beta A chain; inhibin beta A; Activin beta-A chain; Erythroid differentiation protein; EDF
products gene name :
INHBA
other gene names :
INHBA; INHBA; EDF; FRP; EDF
uniprot entry name :
INHBA_HUMAN
host :
E Coli or Yeast or Baculovirus or Mammalian Cell
sequence positions :
311-426
sequence length :
426
sequence :
GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANY
CEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLK
SCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS
purity :
Greater than 90% as determined by SDS-PAGE.
form :
Liquid containing glycerol; lyophilization may be available upon request.
storage stability :
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
products categories :
Signal Transduction
products description :
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.
products 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 gi num :
4504699
ncbi acc num :
NP_002183.1
ncbi gb acc num :
NM_002192.2
uniprot acc num :
P08476
ncbi mol weight :
28.97kD
ncbi pathways :
ALK1 Signaling Events Pathway (137968); Activin Signaling Pathway (1084757); Activin Signaling Pathway (1108220); Antagonism Of Activin By Follistatin Pathway (1269622); Cardiac Progenitor Differentiation Pathway (712094); Cytokine-cytokine Receptor Interaction Pathway (83051); Cytokine-cytokine Receptor Interaction Pathway (460); Glycoprotein Hormones Pathway (1268754); Integrated Pancreatic Cancer Pathway (711360); Metabolism Of Proteins Pathway (1268677)
ncbi summary :
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 summary :
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
size1 :
0.05 mg (E-Coli)
price1 :
190 USD
size2 :
0.2 mg (E-Coli)
price2 :
460
size3 :
0.5 mg (E-Coli)
price3 :
750
size4 :
0.05 mg (Baculovirus)
price4 :
850
size5 :
0.05 mg (Mammalian-Cell)
price5 :
1075
more info or order :
company information
MyBioSource
P.O. Box 153308
San Diego, CA 92195-3308
sales@mybiosource.com
https://www.mybiosource.com
1-888-627-0165
headquarters: USA
MyBioSource, LLC was orginally founded in Vancouver by three enthusiastic scientists who are passionate about providing the world with the best reagents available. Together, they form a company with a big vision known as MyBioSource. MyBioSource is now located in San Diego, California, USA.

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