H4666
Activin A human
recombinant, expressed in HEK 293 cells, HumanKine®, suitable for cell culture
Synonym(s):
Activin A Protein, Growth Factor, Human Activin A
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About This Item
biological source
human
Quality Level
recombinant
expressed in HEK 293 cells
Assay
≥95% (SDS-PAGE)
form
lyophilized powder
potency
≤5 ng/mL EC50
quality
endotoxin tested
mol wt
dimer 25 kDa (non-glycosylated)
packaging
pkg of 5x10 μg
pkg of 10 μg
technique(s)
cell culture | mammalian: suitable
impurities
≤1 EU/mg
storage temp.
−20°C
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Biochem/physiol Actions
Activin-A participates in a diverse array of functions that include; hypothalamic/pituitary/gonadal hormone secretion, insulin secretion; cell growth, differentiation and survival (apoptosis); embryonic patterning and development; wound healing; and inflammation/immune response. It was initially identified as a follicle stimulating hormone/FSH-releasing protein (gonadal hormone), Ling N, et al. (1986) and erythroid differentiation factor (EDF), Schwall R, et al. (1989). The FSH activity is linked to an increase in the population of pituitary gonadotrophs by Katayama T, et al. (1990). In addition to gonadotrophs, activin-A also modifies somatotrophs and lactotrophs, Kitaoka, et al. (1988).
Activin-A stimulates glycogenolysis in isolated rat hepatocytes, Mine T ET. al. (1989) and elevates insulin release from rat pancreatic islets, Verspohl EJ et al. (1993). Activin-A stimulates insulin secretion in rat pancreatic islets, Totsuka Y, et al. (1988).
Follistatin, an activin-binding protein, is a principle regulator of activin activity, de Winter JP, et al. (1996); however during embryogenesis, Cripto is an important noncompetitive activin antagonist that facilitates Nodal signaling, Kelber JA, et al. (2008).
A role for activin-A as a regulator of cell proliferation was recognized by Gonzalez-Manchon C and Vale W. (1989); wherein Act-A inhibited the growth of and induced morphological changes in CHO-KI cells in culture, in a way similar to but less potent than TGF-β.
Activin A is involved with the entire process of embryo development from germ cells thru embryonic development to adult tissues. It stimulates spermatogonial proliferation in germ-Sertoli cell cocultures, Mather JP, et al. (1990) and is a maturation factor for oocytes, Itoh M, et al. (1990). Activin A promotes proliferation of human luteinized preovulation granulose cells (ovarian granulose cells), Rabinovici J, et al. (1990).
Activin-A stimulates glycogenolysis in isolated rat hepatocytes, Mine T ET. al. (1989) and elevates insulin release from rat pancreatic islets, Verspohl EJ et al. (1993). Activin-A stimulates insulin secretion in rat pancreatic islets, Totsuka Y, et al. (1988).
Follistatin, an activin-binding protein, is a principle regulator of activin activity, de Winter JP, et al. (1996); however during embryogenesis, Cripto is an important noncompetitive activin antagonist that facilitates Nodal signaling, Kelber JA, et al. (2008).
A role for activin-A as a regulator of cell proliferation was recognized by Gonzalez-Manchon C and Vale W. (1989); wherein Act-A inhibited the growth of and induced morphological changes in CHO-KI cells in culture, in a way similar to but less potent than TGF-β.
Activin A is involved with the entire process of embryo development from germ cells thru embryonic development to adult tissues. It stimulates spermatogonial proliferation in germ-Sertoli cell cocultures, Mather JP, et al. (1990) and is a maturation factor for oocytes, Itoh M, et al. (1990). Activin A promotes proliferation of human luteinized preovulation granulose cells (ovarian granulose cells), Rabinovici J, et al. (1990).
Analysis Note
The specific activity was determined by the dose-dependent inhibition of proliferation of the MPC-11 cell line (mouse plasmocytoma cell line).
Legal Information
HumanKine is a registered trademark of Proteintech Group, Inc. and Humanzyme, Inc
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Sadegh Ghorbani-Dalini et al.
3 Biotech, 10(5), 215-215 (2020-05-02)
The first step in differentiation of pluripotent stem cell toward endoderm-derived cell/organ is differentiation to definitive endoderm (DE) which is the central issue in developmental biology. Based on several evidences, we hypothesized that activin-A optimization as well as replacement of
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
Melissa L Brown et al.
Islets, 6(5-6), e1017226-e1017226 (2015-04-04)
Emerging evidence suggests that activin with its associated receptors, second messengers, and antagonists would be excellent targets for therapeutic drug development in the treatment of diabetes. We undertook the current study to investigate the ability to extrapolate findings from rodent
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
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
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