Comparison

Active Recombinant Human Activin AB protein European Partner

Item no. RF0037-50
Manufacturer Agrenvec
Amount 50ug
Category
Type Proteins Recombinant
Specific against other
ECLASS 10.1 32160409
ECLASS 11.0 32160409
UNSPSC 12352202
Alias Activin beta A beta B heterodimer
Available
Molecular Weight:
Recombinant Activin AB is a disulphide linked heterodimer of subunits betaA / betaB . betaA Single chain, containing 116 aa (13.7 kDa) and betaB single chain, 123 amino residues (14kDa). Recombinant human Activin AB contains a His-tag at the N-terminal end.
Molecular Formula:
betaA C600H911N173O174S13/ betaB - C615H910N178O177S12
p.I:
6.8
Ext. Coeff. Abs (280nm) 0.1% (=1g/l) =
1.56
UniProtKB:
P08476 P09529
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 AB has two chains of 116 and 123 amino acids residues (betaA-betaB). 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. Inhibins /Activins are proteins that are formed by the dimerization of two subunits, i. e. an alpha with either betaA –inhibin A- or betaB - inhibin B. The subunits betaA and betaB can also form homodimers or heterodimers calleds activins: Activin A (betaAbetaA), Activin B (betaBbetaB) and Activin AB (betaAbetaB). The activin gene family comprises the additional, but poorly characterized members activin betaC, betaD, and betaE. - 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 development of assays distinguishing between different forms of activins and inhibins, along with knock-in and knock-out models, have provided evidence that the betaA- and betaB-subunits have independent and separate roles physiologically. Additionally, evaluation of ligand-receptor interactions indicates significant differences in receptor affinity between activin isoforms, as well as between inhibin isoforms.
Sequence:
betaA:GLECDGKVNICCKKQFFVSFKDIGWNDWI IAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVIN HYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQN IIKKDIQNMIVEECGCS betaB:GLECDGRTNLC CRQQFFIDFRLIGWNDWIIAPTGYYGNYCEGSCPA YLAGVPGSASSFHTAVVNQYRMRGLNPGTVNSCCI PTKLSTMSMLYFDDEYNIVKRDVPNMIVEECGCA
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:
Functional studies, Cell culture, Western Blot
Bioassay 1 - Result assay 1:
The biological activity of Activin AB is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. - EC50 <5ng/mL are required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.
Bioassay 2 - Result assay 2:
-
Bioassay 3 - Result assay 3:
-
Bioassay 4 - Result assay 4:
-
References:
-Chen, Y. G. et al., 2006. Activin signalling and its role in regulation of cell proliferation, apoptosis, and carcinogenesis. Exp. Biol. Med. (Maywood), 231 (5): 534-44. -Bamberger, C. et al., 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. -Phillips, D. J. et al., 1999. A sensitive and specific in vitro bioassay for activin using a mouse plasmacytoma cell line, MPC-11. J. of Endocrinology, 162: 111-116. -Vale, W. et al., 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. ?
RESCONSTITUTION RECOMENDATION QC SHEET
Centrifuge vial before opening. Lyophilized protein should be reconstituted in water to a concentration of 50 ng/ul. Optimal concentration should be determined for specific application and cell lines.
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) :
1ug, 10ug, 50 ug of active protein

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: 50ug
Available: In stock
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