Comparison

Recombinant Human Activin A protein European Partner

Item no. RF009-5
Manufacturer Agrenvec
Amount 5ug
Category
Type Proteins Recombinant
Specific against other
ECLASS 10.1 32160409
ECLASS 11.0 32160409
UNSPSC 12352202
Alias Inhibin beta A chain, Activin beta-A chain, Erythroid differentiation protein
Available
Molecular Weight:
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.
Molecular Formula:
C600H911N173O174S13
p.I:
7.27
Ext. Coeff. Abs (280nm) 0.1% (=1g/l) =
1.27
UniProtKB:
P08476
Endotoxin level:
Endotoxin Level : < 0.04 EU / ug protein (LAL method)
Source:
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.
Description:
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.
Sequence:
HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWI IAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVIN HYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQN IIKKDIQNMIVEECGCS
Formulation:
Recombinant human Activin is lyophilized from a Tris HCl 0.05M buffer at pH 7.4
Purity
Purity >97% by SDS-PAGE gel
Applications:
Western Blot, ELISA
Bioassay 1 - Result assay 1:
-
Bioassay 2 - Result assay 2:
-
Bioassay 3 - Result assay 3:
-
Bioassay 4 - Result assay 4:
-
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., 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.
RESCONSTITUTION RECOMENDATION QC SHEET
Centrifuge vial before opening. Lyophilized protein should be reconstituted in water to a concentration of 50 ng/ul. Due to the protein nature, dimmers and multimers may be observed. At higher concentration the solubility may be reduced and multimers generated. Optimal concentration should be determined for specific application.
Storage and Stability:
This lyophilized preparation is stable at 2-8C C for short term, long storage it should be kept at -20C. Reconstituted protein should be stored in working aliquots at –20C. Repeated freezing and thawing is not recommended.
Shipping
Room temperature
Available sizes (ug) :
1 ug, 5 ug, 10 ug, 100 ug, 200 ug

Note: The presented information and documents (Manual, Product Datasheet, Safety Datasheet and Certificate of Analysis) correspond to our latest update and should serve for orientational purpose only. We do not guarantee the topicality. We would kindly ask you to make a request for specific requirements, if necessary.

All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.

Amount: 5ug
Available: In stock
available

Compare

Add to wishlist

Get an offer

Request delivery time

Ask a technical question

Submit a bulk request

Questions about this Product?
 
Close