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Inhibin beta A chain (Activin beta-A chain) (Erythroid differentiation protein) (EDF)

 INHBA_HUMAN             Reviewed;         426 AA.
P08476; Q14599;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 2.
25-OCT-2017, entry version 197.
RecName: Full=Inhibin beta A chain;
AltName: Full=Activin beta-A chain;
AltName: Full=Erythroid differentiation protein;
Short=EDF;
Flags: Precursor;
Name=INHBA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3754442; DOI=10.1016/0006-291X(86)91021-1;
Mason A.J., Niall H.D., Seeburg P.H.;
"Structure of two human ovarian inhibins.";
Biochem. Biophys. Res. Commun. 135:957-964(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3267209; DOI=10.1073/pnas.85.8.2434;
Murata M., Eto Y., Shibai H., Sakai M., Muramatsu M.;
"Erythroid differentiation factor is encoded by the same mRNA as that
of the inhibin beta A chain.";
Proc. Natl. Acad. Sci. U.S.A. 85:2434-2438(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1777673; DOI=10.3109/10425179109039678;
Tanimoto K., Handa S.I., Ueno N., Murakami K., Fukamizu A.;
"Structure and sequence analysis of the human activin beta A subunit
gene.";
DNA Seq. 2:103-110(1991).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
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.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 311-426.
PubMed=3758355; DOI=10.1016/0014-5793(86)81006-7;
Stewart A.G., Milborrow H.M., Ring J.M., Crowther C.E., Forage R.G.;
"Human inhibin genes. Genomic characterisation and sequencing.";
FEBS Lett. 206:329-334(1986).
[7]
NUCLEOTIDE SEQUENCE OF 311-426.
TISSUE=Testis;
Berg H., Walter M., Northemann W.;
Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
[8]
INTERACTION WITH FST AND FSTL3.
PubMed=12697670; DOI=10.1210/en.2002-0203;
Schneyer A., Schoen A., Quigg A., Sidis Y.;
"Differential binding and neutralization of activins A and B by
follistatin and follistatin like-3 (FSTL-3/FSRP/FLRG).";
Endocrinology 144:1671-1674(2003).
[9]
X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) IN COMPLEX WITH RAT ACTRIIB
EXTRACELLULAR DOMAIN.
PubMed=12660162; DOI=10.1093/emboj/cdg156;
Thompson T.B., Woodruff T.K., Jardetzky T.S.;
"Structures of an ActRIIB:activin A complex reveal a novel binding
mode for TGF-beta ligand:receptor interactions.";
EMBO J. 22:1555-1566(2003).
[10]
X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 311-426 IN COMPLEX WITH
FSTL3, AND DISULFIDE BONDS.
PubMed=18768470; DOI=10.1074/jbc.M801266200;
Stamler R., Keutmann H.T., Sidis Y., Kattamuri C., Schneyer A.,
Thompson T.B.;
"The structure of FSTL3.activin A complex. Differential binding of N-
terminal domains influences follistatin-type antagonist specificity.";
J. Biol. Chem. 283:32831-32838(2008).
[11]
VARIANTS GLU-280 AND SER-386, AND CHARACTERIZATION OF VARIANT SER-386.
PubMed=24302632; DOI=10.1002/humu.22489;
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.;
"Germline mutations of inhibins in early-onset ovarian epithelial
tumors.";
Hum. Mutat. 35:294-297(2014).
-!- FUNCTION: 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.
-!- SUBUNIT: Dimeric, linked by one or more disulfide bonds. Inhibin A
is a dimer of alpha and beta-A. Inhibin B is a dimer of alpha and
beta-B. Activin A is a homodimer of beta-A. Activin B is a
homodimer of beta-B. Activin AB is a dimer of beta-A and beta-B.
Interacts with FST and FSTL3. {ECO:0000269|PubMed:12660162,
ECO:0000269|PubMed:12697670, ECO:0000269|PubMed:18768470}.
-!- INTERACTION:
P21674:Fst (xeno); NbExp=2; IntAct=EBI-8077140, EBI-5746973;
-!- SUBCELLULAR LOCATION: Secreted.
-!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Activin entry;
URL="https://en.wikipedia.org/wiki/Activin";
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EMBL; M13436; AAA59168.1; -; mRNA.
EMBL; X04447; CAA28041.1; -; Genomic_DNA.
EMBL; X57578; CAA40805.1; -; Genomic_DNA.
EMBL; X57579; CAA40805.1; JOINED; Genomic_DNA.
EMBL; X57579; CAA40806.1; -; Genomic_DNA.
EMBL; AC005027; AAQ96861.1; -; Genomic_DNA.
EMBL; BC007858; AAH07858.1; -; mRNA.
EMBL; J03634; AAA35787.1; -; mRNA.
EMBL; X72498; CAA51163.1; -; mRNA.
CCDS; CCDS5464.1; -.
PIR; S30488; B24248.
RefSeq; NP_002183.1; NM_002192.3.
RefSeq; XP_016867665.1; XM_017012176.1.
UniGene; Hs.28792; -.
UniGene; Hs.583348; -.
PDB; 1NYS; X-ray; 3.05 A; B/D=311-426.
PDB; 1NYU; X-ray; 3.10 A; B/D=311-426.
PDB; 1S4Y; X-ray; 2.30 A; B/D=311-426.
PDB; 2ARP; X-ray; 2.00 A; A=311-426.
PDB; 2ARV; X-ray; 2.00 A; A/B=311-426.
PDB; 2B0U; X-ray; 2.80 A; A/B=311-426.
PDB; 2P6A; X-ray; 3.40 A; A/B=311-426.
PDB; 3B4V; X-ray; 2.48 A; A/B/E/F=311-426.
PDB; 4MID; X-ray; 2.14 A; A=334-426.
PDB; 5HLY; X-ray; 2.30 A; A=30-426.
PDB; 5HLZ; X-ray; 2.85 A; A/C/E/G=30-305, B/D/F/H=311-426.
PDBsum; 1NYS; -.
PDBsum; 1NYU; -.
PDBsum; 1S4Y; -.
PDBsum; 2ARP; -.
PDBsum; 2ARV; -.
PDBsum; 2B0U; -.
PDBsum; 2P6A; -.
PDBsum; 3B4V; -.
PDBsum; 4MID; -.
PDBsum; 5HLY; -.
PDBsum; 5HLZ; -.
ProteinModelPortal; P08476; -.
SMR; P08476; -.
BioGrid; 109836; 9.
DIP; DIP-5824N; -.
IntAct; P08476; 1.
MINT; MINT-1786936; -.
STRING; 9606.ENSP00000242208; -.
ChEMBL; CHEMBL3588735; -.
iPTMnet; P08476; -.
PhosphoSitePlus; P08476; -.
BioMuta; INHBA; -.
DMDM; 124279; -.
MaxQB; P08476; -.
PaxDb; P08476; -.
PeptideAtlas; P08476; -.
PRIDE; P08476; -.
DNASU; 3624; -.
Ensembl; ENST00000242208; ENSP00000242208; ENSG00000122641.
Ensembl; ENST00000442711; ENSP00000397197; ENSG00000122641.
Ensembl; ENST00000638023; ENSP00000490646; ENSG00000122641.
GeneID; 3624; -.
KEGG; hsa:3624; -.
UCSC; uc003thq.4; human.
CTD; 3624; -.
DisGeNET; 3624; -.
EuPathDB; HostDB:ENSG00000122641.9; -.
GeneCards; INHBA; -.
HGNC; HGNC:6066; INHBA.
HPA; HPA020031; -.
MalaCards; INHBA; -.
MIM; 147290; gene.
neXtProt; NX_P08476; -.
OpenTargets; ENSG00000122641; -.
Orphanet; 213504; Adenocarcinoma of ovary.
PharmGKB; PA29877; -.
eggNOG; KOG3900; Eukaryota.
eggNOG; ENOG410XT8Z; LUCA.
GeneTree; ENSGT00760000119112; -.
HOGENOM; HOG000220890; -.
HOVERGEN; HBG105613; -.
InParanoid; P08476; -.
KO; K04667; -.
OMA; LRPHPKH; -.
OrthoDB; EOG091G09LW; -.
PhylomeDB; P08476; -.
TreeFam; TF351791; -.
Reactome; R-HSA-1502540; Signaling by Activin.
Reactome; R-HSA-209822; Glycoprotein hormones.
Reactome; R-HSA-2473224; Antagonism of Activin by Follistatin.
SignaLink; P08476; -.
SIGNOR; P08476; -.
EvolutionaryTrace; P08476; -.
GenomeRNAi; 3624; -.
PRO; PR:P08476; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000122641; -.
CleanEx; HS_INHBA; -.
ExpressionAtlas; P08476; baseline and differential.
Genevisible; P08476; HS.
GO; GO:0043509; C:activin A complex; IDA:HGNC.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0043512; C:inhibin A complex; IDA:HGNC.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005125; F:cytokine activity; IDA:HGNC.
GO; GO:0008083; F:growth factor activity; TAS:UniProtKB.
GO; GO:0005179; F:hormone activity; TAS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
GO; GO:0034711; F:inhibin binding; IEA:Ensembl.
GO; GO:0017046; F:peptide hormone binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0005160; F:transforming growth factor beta receptor binding; IBA:GO_Central.
GO; GO:0070699; F:type II activin receptor binding; IPI:BHF-UCL.
GO; GO:0032924; P:activin receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0007050; P:cell cycle arrest; IDA:HGNC.
GO; GO:0048468; P:cell development; IBA:GO_Central.
GO; GO:0030154; P:cell differentiation; TAS:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; TAS:UniProtKB.
GO; GO:0071397; P:cellular response to cholesterol; IEA:Ensembl.
GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEA:Ensembl.
GO; GO:0006952; P:defense response; TAS:UniProtKB.
GO; GO:0035987; P:endodermal cell differentiation; IDA:BHF-UCL.
GO; GO:0030218; P:erythrocyte differentiation; NAS:UniProtKB.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:0061029; P:eyelid development in camera-type eye; ISS:UniProtKB.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:HGNC.
GO; GO:0097154; P:GABAergic neuron differentiation; IDA:ParkinsonsUK-UCL.
GO; GO:0001942; P:hair follicle development; IGI:UniProtKB.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IDA:UniProtKB.
GO; GO:0042541; P:hemoglobin biosynthetic process; IDA:UniProtKB.
GO; GO:0008584; P:male gonad development; IGI:UniProtKB.
GO; GO:0048333; P:mesodermal cell differentiation; IEA:Ensembl.
GO; GO:0045578; P:negative regulation of B cell differentiation; TAS:UniProtKB.
GO; GO:0045786; P:negative regulation of cell cycle; IDA:HGNC.
GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0046882; P:negative regulation of follicle-stimulating hormone secretion; NAS:UniProtKB.
GO; GO:0045077; P:negative regulation of interferon-gamma biosynthetic process; TAS:UniProtKB.
GO; GO:0045650; P:negative regulation of macrophage differentiation; TAS:UniProtKB.
GO; GO:0042326; P:negative regulation of phosphorylation; TAS:UniProtKB.
GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
GO; GO:0042476; P:odontogenesis; IGI:UniProtKB.
GO; GO:0001541; P:ovarian follicle development; IGI:UniProtKB.
GO; GO:0060021; P:palate development; IGI:UniProtKB.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; IDA:BHF-UCL.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IDA:HGNC.
GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:UniProtKB.
GO; GO:0046881; P:positive regulation of follicle-stimulating hormone secretion; TAS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
GO; GO:0060279; P:positive regulation of ovulation; ISS:UniProtKB.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0042701; P:progesterone secretion; IGI:UniProtKB.
GO; GO:0046880; P:regulation of follicle-stimulating hormone secretion; IGI:UniProtKB.
GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0042493; P:response to drug; IDA:UniProtKB.
GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
GO; GO:0021773; P:striatal medium spiny neuron differentiation; IDA:ParkinsonsUK-UCL.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR000491; Inhibin_betaA.
InterPro; IPR001839; TGF-b_C.
InterPro; IPR001111; TGF-b_propeptide.
InterPro; IPR015615; TGF-beta-rel.
InterPro; IPR017948; TGFb_CS.
PANTHER; PTHR11848; PTHR11848; 1.
Pfam; PF00019; TGF_beta; 1.
Pfam; PF00688; TGFb_propeptide; 1.
PRINTS; PR00670; INHIBINBA.
SMART; SM00204; TGFB; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS00250; TGF_BETA_1; 1.
PROSITE; PS51362; TGF_BETA_2; 1.
1: Evidence at protein level;
3D-structure; Cleavage on pair of basic residues; Complete proteome;
Disulfide bond; Glycoprotein; Growth factor; Hormone; Polymorphism;
Reference proteome; Secreted; Signal.
SIGNAL 1 20 {ECO:0000250}.
PROPEP 21 310
/FTId=PRO_0000033708.
CHAIN 311 426 Inhibin beta A chain.
/FTId=PRO_0000033709.
CARBOHYD 165 165 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 314 322 {ECO:0000269|PubMed:18768470}.
DISULFID 321 391 {ECO:0000269|PubMed:18768470}.
DISULFID 350 423 {ECO:0000269|PubMed:18768470}.
DISULFID 354 425 {ECO:0000269|PubMed:18768470}.
DISULFID 390 390 Interchain.
{ECO:0000269|PubMed:18768470}.
VARIANT 280 280 G -> E (found in a patient with early-
onset epithelial ovarian tumor; uncertain
pathological significance).
{ECO:0000269|PubMed:24302632}.
/FTId=VAR_072640.
VARIANT 299 299 Q -> P (in dbSNP:rs41294833).
/FTId=VAR_052566.
VARIANT 386 386 N -> S (found in a patient with early-
onset epithelial ovarian tumor; alters
the ratio of secreted activins and
ihibins; uncertain pathological
significance).
{ECO:0000269|PubMed:24302632}.
/FTId=VAR_072641.
CONFLICT 377 379 RMR -> AC (in Ref. 7; CAA51163).
{ECO:0000305}.
HELIX 52 65 {ECO:0000244|PDB:5HLY}.
HELIX 80 89 {ECO:0000244|PDB:5HLY}.
STRAND 92 95 {ECO:0000244|PDB:5HLY}.
HELIX 97 99 {ECO:0000244|PDB:5HLY}.
STRAND 101 103 {ECO:0000244|PDB:5HLY}.
HELIX 107 118 {ECO:0000244|PDB:5HLY}.
STRAND 120 126 {ECO:0000244|PDB:5HLY}.
STRAND 135 139 {ECO:0000244|PDB:5HLY}.
HELIX 143 146 {ECO:0000244|PDB:5HLY}.
STRAND 149 160 {ECO:0000244|PDB:5HLY}.
STRAND 170 180 {ECO:0000244|PDB:5HLY}.
STRAND 201 212 {ECO:0000244|PDB:5HLY}.
STRAND 217 222 {ECO:0000244|PDB:5HLY}.
HELIX 224 232 {ECO:0000244|PDB:5HLY}.
STRAND 237 243 {ECO:0000244|PDB:5HLY}.
TURN 245 251 {ECO:0000244|PDB:5HLY}.
STRAND 253 255 {ECO:0000244|PDB:5HLY}.
HELIX 284 289 {ECO:0000244|PDB:5HLY}.
STRAND 292 298 {ECO:0000244|PDB:5HLY}.
STRAND 318 320 {ECO:0000244|PDB:5HLY}.
STRAND 321 324 {ECO:0000244|PDB:2ARP}.
STRAND 327 329 {ECO:0000244|PDB:2ARP}.
HELIX 330 333 {ECO:0000244|PDB:2ARP}.
TURN 336 338 {ECO:0000244|PDB:2ARP}.
STRAND 339 341 {ECO:0000244|PDB:2ARP}.
STRAND 343 346 {ECO:0000244|PDB:2ARP}.
STRAND 349 352 {ECO:0000244|PDB:2ARP}.
HELIX 356 358 {ECO:0000244|PDB:2ARV}.
STRAND 362 364 {ECO:0000244|PDB:2P6A}.
HELIX 368 375 {ECO:0000244|PDB:2ARP}.
TURN 378 380 {ECO:0000244|PDB:2B0U}.
TURN 382 386 {ECO:0000244|PDB:2ARV}.
STRAND 391 404 {ECO:0000244|PDB:2ARP}.
TURN 406 408 {ECO:0000244|PDB:2ARV}.
STRAND 410 425 {ECO:0000244|PDB:2ARP}.
SEQUENCE 426 AA; 47442 MW; 201CDEDF99CB6919 CRC64;
MPLLWLRGFL LASCWIIVRS SPTPGSEGHS AAPDCPSCAL AALPKDVPNS QPEMVEAVKK
HILNMLHLKK RPDVTQPVPK AALLNAIRKL HVGKVGENGY VEIEDDIGRR AEMNELMEQT
SEIITFAESG TARKTLHFEI SKEGSDLSVV ERAEVWLFLK VPKANRTRTK VTIRLFQQQK
HPQGSLDTGE EAEEVGLKGE RSELLLSEKV VDARKSTWHV FPVSSSIQRL LDQGKSSLDV
RIACEQCQES GASLVLLGKK KKKEEEGEGK KKGGGEGGAG ADEEKEQSHR PFLMLQARQS
EDHPHRRRRR GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC EGECPSHIAG
TSGSSLSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS MLYYDDGQNI IKKDIQNMIV
EECGCS


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E0838h ELISA kit Activin beta-A chain,EDF,Erythroid differentiation protein,Homo sapiens,Human,INHBA,Inhibin beta A chain 96T
U0838h CLIA Activin beta-A chain,EDF,Erythroid differentiation protein,Homo sapiens,Human,INHBA,Inhibin beta A chain 96T
PNb-014-I Activin-B (inactive) Human Host: Nicotiana benthamiana INHBBActivin beta-B chain, Inhibin beta B chain precursor; Inhibin, beta-2 10
RF0029-25 rHuman Activin B Active; Activin beta-B chain, Inhibin beta B chain precursor; Inhibin, beta-2 25ug
RF0029-100 rHuman Activin B Active; Activin beta-B chain, Inhibin beta B chain precursor; Inhibin, beta-2 100ug
RF0029-100 Activin beta-B chain, Inhibin beta B chain precursor; Inhibin, beta-2, rHuman Activin B Active 100ug
RF0029-10 rHuman Activin B Active; Activin beta-B chain, Inhibin beta B chain precursor; Inhibin, beta-2 10ug
RF0029-5 rHuman Activin B Active; Activin beta-B chain, Inhibin beta B chain precursor; Inhibin, beta-2 5ug


 

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