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Index / Agren / rHuman Activin A Active, Human cytokinesand growth factors /Product Detail : RF0010-10 rHuman Activin A Active, Human cytokinesand growth factors
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rHuman Activin A Active, Human cytokinesand growth factors

 Price: 190   EUR
216   USD
147   GBP

Product name : rHuman Activin A Active, Human cytokinesand growth factors

Catalog number : RF0010-10

Quantity: 10

Availability: Yes

Supplier name : Agren

Data sheet Data sheet : Ask more or other datasheet now !

About this Product :

rHuman Activin A Active, Human cytokinesand growth factors Human samples 80 % of the research is conducted on human samples. Gentaur suppliers human normal cells, cell lines, RNA extracts and lots of antibodies and elisa kit to Human proteins as well as rHuman Activin A Active, Human cytokinesand growth factors.

More Details about

Human recombinant protein expressed in Nicotiana benthamiana. 

Molecular formula:

Molecular weight:
27.4  kDa disulfide-linked homodimers of two βA chains, each containing 116 amino residues


Extinction coefficient :
E0.1% = 1,27 (A 280 nm)

Purity assay:
> 97% by SDS-PAGE gel

Endotoxin level:
< 0.04 EU/ µg protein (LAL method)

Animal-free product*


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.

Lyophilized from a Tris HCl 0.05M buffer at pH 7,4

Produced by transient expression of Activin A in non-transgenic plants. Recombinant human Activin A contains a 6-His-tag at the N-terminal end and is purified by sequential chromatography (FPLC). Contains no animal–derived components or impurities.

Reconstitution recommendation: 
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.

Storage and Stability:
This lyophilized preparation is stable at 2-8º C. For long storage should be kept at  -20º C and it is recommended to add a carrier protein (0.1% HSA or BSA). Repeated freezing and thawing is not recommended.  

Purity and Serological Identification:
The protein was resolved by SDS polyacrylamide gel electrophoresis and the gel was stained with Coomassie blue.

Serological Identification:
Serological Identification:  The protein was  electrophoresed under reducing condition on a 15% SDS- polyacrylamide gel, transferred by electroblotting to a NC membrane and visualized by  immune-detection with specific antibody Activin A.

Biological Activity: 
Biological Activity:  The biological activity of Activin A  is measured  by its ability to inhibit  mouse plasmacytoma cell line  (MPC-11)  cells proliferation ( [3H]thymidine incorporation).

ED50 ≤5ng/ml


-Vale W., Hseuh A., Rivier C.  and Yu J. (1990).  The inhibin/Activin family of hormones and growth factors. In Peptide Growth Factors and their Receptors: Handbook of Experimental Physiology,  95:  211–248. Eds M Sporn & A Roberts. Berlin: Springer-Verlag.

-Schwall  R. H., and  Lai, C. (1991).  Erythroid differentiation bioassys for activin. Methods Enzymol, 198: 340-346.

-Sulyok S., Wankell M., Alzheimer C. and Werner S. (2004). Activin: an important regulator of wound repair,  fibrosis, and neuroprotection. Mol. Cell. Endocrinology, 225 (1-2): 127–32. 

-Bamberger C., Schärer  A.,  Antsiferova M., Tychsen B., Pankow S.,  Müller M., Rülicke T., Paus R. and Werner S. (2005). Activin controls skin morphogenesis and wound repair predominantly via stromal cells and in a concentration- dependent manner via keratinocytes. Am. J. Pathol., 167 (3): 733–47.

 -Chen Y. G., Wang Q., Lin S. L., Chang C. D., Chuang J., Chung J. and  Ying S. Y. (2006). Activin signalling and its role in regulation of cell proliferation, apoptosis, and carcinogenesis. Exp. Biol. Med. (Maywood), 231 (5): 534–44. 

-Phillips D. J., Brauman J. N., Mason A. J., Kretser D.M and Hedger M. P.(1999). A sensitive and specific in vitro bioassay for activin using a mouse plasmacytoma cell line, MPC-11. J. of Endocrinology, 162: 111-116.

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