A4362
Activin A active human
Animal-component free, recombinant, expressed in Nicotiana, >97% (SDS-PAGE)
Synonym(s):
Erythroid differentiation protein, Inhibin beta A chain; Activin beta-A chain
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About This Item
UNSPSC Code:
12352202
NACRES:
NA.32
Recommended Products
biological source
human
Quality Level
recombinant
expressed in Nicotiana
assay
>97% (SDS-PAGE)
form
lyophilized
potency
≤5 ng/mL ED50
mol wt
27.4 kDa (disulfide-linked homodimers of two βA chains, each containing 116 amino residues)
packaging
pkg of 5 μg
storage condition
avoid repeated freeze/thaw cycles
impurities
Endotoxin, tested (LAL test, < 0.04 EU/ ug protein)
UniProt accession no.
storage temp.
−20°C
Gene Information
human ... INHBA(3624)
Amino Acid Sequence
HisHisHisHisHisHisGlyLeuGluCysAspGlyLysValAsnIleCysCysLysLysGlnPhePheValSerPheLysAspIleGlyTrpAsnAspTrpIleIleAlaProSerGlyTyrHisAlaAsnTyrCysGluGlyGluCysProSerHisIleAlaGlyThrSerGlySerSerLeuSerPheHisSerThrValIleAsnHisTyrArgMetArgGlyHisSerProPheAlaAsnLeuLysSerCysCysValProThrLysLeuArgProMetSerMetLeuTyrTyrAspAspGlyGlnAsnIleIleLysLysAspIleGlnAsnMetIleValGluGluCysGlyCysSer
General description
Activins are homodimers or heterodimers of the various β subunit isoforms, belonging to the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin exhibits a wide range of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins plays a key role in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells known to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
As with other members of the super-family, Activins interact with two types of cell surface trans-membrane receptors (Types I and II) which have intrinsic serine/threonine kinase activities in their cytoplasmic domains, Activin type 1 receptors, ACVR1, ACVR1B, ACVR1C and Activin type 2 receptors, ACVR2A, ACVR2B. The biological activity of Activin A can be neutralized by inhibins and by the diffusible TGF-B antagonist, Follistatin.
As with other members of the super-family, Activins interact with two types of cell surface trans-membrane receptors (Types I and II) which have intrinsic serine/threonine kinase activities in their cytoplasmic domains, Activin type 1 receptors, ACVR1, ACVR1B, ACVR1C and Activin type 2 receptors, ACVR2A, ACVR2B. The biological activity of Activin A can be neutralized by inhibins and by the diffusible TGF-B antagonist, Follistatin.
Physical form
Lyophilized from a Tris HCl 0.05 M buffer at pH 7.4
Reconstitution
Lyophilized protein should be reconstituted in water to a concentration of 50 ng /μl. Due to the protein nature, dimmers and multimers may be observed.
Analysis Note
The biological activity of Activin A is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation.
ED50: ≤ 5 ng/mL
ED50: ≤ 5 ng/mL
Other Notes
Extinction Coefficient: E0.1% = 1.27 (A 280 nm)
p.I: 7.27
p.I: 7.27
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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Yan Li et al.
The Journal of clinical endocrinology and metabolism, 100(11), E1415-E1427 (2015-08-26)
Activin A increases matrix metalloproteinase (MMP) 2 expression and cell invasion in human trophoblasts, but whether the expression of MMP2 is essential for the proinvasive effect of activin A has yet to be determined. Moreover, the identity of the activin
Hannah E J Yong et al.
Pregnancy hypertension, 5(4), 346-353 (2015-11-26)
Activin A, a TGFβ family member, circulates in the maternal blood at increasing concentrations throughout gestation during a healthy pregnancy. The circulating concentration of activin A is further increased in pre-eclampsia (PE), a hypertensive disorder of pregnancy that is marked
Xu Qian et al.
Biomaterials, 35(36), 9581-9590 (2014-09-06)
Well-defined culture conditions are essential for realizing the full potential of human embryonic stem cells (hESCs) in regenerative medicine where large numbers of cells are required. Synthetic polymers such as poly[2-(methacryloyloxy) ethyl dimethyl-(3-sulfopropyl) ammonium hydroxide] (PMEDSAH), offer multiple advantages over
Yutaka Ohsawa et al.
PloS one, 10(7), e0133713-e0133713 (2015-08-01)
Myostatin, a muscle-specific transforming growth factor-β (TGF-β), negatively regulates skeletal muscle mass. The N-terminal prodomain of myostatin noncovalently binds to and suppresses the C-terminal mature domain (ligand) as an inactive circulating complex. However, which region of the myostatin prodomain is
Yasuhide Ohinata et al.
PloS one, 9(9), e107308-e107308 (2014-09-10)
The inner cell mass (ICM) and trophoblast cell lineages duet early embryonic development in mammals. After implantation, the ICM forms the embryo proper as well as some extraembryonic tissues, whereas the trophoectoderm (TE) exclusively forms the fetal portion of the
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