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| Product Name | Active Recombinant Human Activin A protein |
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| Description | Human recombinant protein expressed in Nicotiana benthamiana. It is produced by transient expression in non-transgenic plants. This product contains no animal-derived components or impurities. Animal Free product. Activins are homodimers or heterodimers of the various beta subunit isoforms, belonging to the TGFbeta family. Mature Activin A has two 116 amino acids residues betaA subunits (betaA-betaA). 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. Recombinant human Activin A is a polypeptide chain containing 116 amino acids (311- 426 P08476 INHBA_HUMAN) and a His-tag at the N-terminal end. Several forms are observed with different predicted molecular masses such as monomer (13.7 kDa), dimmer ( 27.4 kDa) and multimeric forms. Purity >97% by SDS-PAGE gel |
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| Size | 1 µg, 5 µg, 10 µg, 50 µg, 100 µg |
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| Concentration | n/a |
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| Applications | Functional studies, Cell culture, Western Blot, Dermocosmetic (rh Activin A increases the expression of E-cadherin and improves the distribution of e-cadherin in cell-cell contact areas). |
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| Other Names | Inhibin beta A chain; Activin beta-A chain; Erythroid differentiation protein |
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| Gene, Accession, CAS # | UniProt: P08476 |
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| Catalog # | RF0062 |
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| Order / More Info | Active Recombinant Human Activin A protein from AGRENVEC |
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| Product Specific References | 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., Scharer A., Antsiferova M., Tychsen B., Pankow S., Muller M., Rulicke 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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