Activin A is a member of the TGFβ superfamily of growth factors involved in stem cell differentiation and maintenance, regulation of embryogenesis, development of the reproductive system, wound healing and regulation of immune responses. The activity of Activin A is regulated by the high-affinity inhibitor, follistatin (1), and inhibins.
Activins are disulphide-linked homo- and heterodimers of four inhibin β chains. The best characterised are Activin A and Activin B, homodimers of inhibin βA and inhibin βB respectively. Activins, like all other members in the TGF-β superfamily, are synthesized as larger precursors consisting of an N-terminal signal peptide, a pro-domain of 250–350 residues and a highly conserved mature domain. The pro-domain, which is cleaved off in the mature protein, has important roles in the biosynthesis, stabilisation, transportation and signalling of the growth factors (2).
Activin A is used for maintenance of pluripotency in many human induced-pluripotent stem cell and human embryonic stem cell lines (3), and to induce stem cell differentiation into endoderm (4) and other cell fates.
Product: recombinant human Activin A
Mature domain of human activin A (residues 311-426, Uniprot: P08476) expressed in E.coli, refolded and purified to homogeneity. The mature protein is a disulphide linked dimer with a molecular weight of ca. 25 kDa.
Protein is provided in lyophilised form without carrier protein.
GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC EGECPSHIAG
TSGSSLSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS MLYYDDGQNI
ActA, Activin beta-A chain, Erythroid differentiation protein (EDP), Follicle-Stimulating Hormone (FSH) releasing protein (FRP), INHBA, Inhibin beta A, Inhibin beta 1
1. Harrington, A. E. et al. Structural basis for the inhibition of activin signalling by follistatin. EMBO J. 25, 1035–1045 (2006).
2. Wang, X., Fischer, G. & Hyvönen, M. Structure and activation of pro-activin A. (2016). doi:10.1038/ncomms12052
3. Pauklin, S. & Vallier, L. Activin/Nodal signalling in stem cells. Development 142, 607–19 (2015).
4. D’Amour, K. A. et al. Efficient differentiation of human embryonic stem cells to definitive endoderm. Nat. Biotechnol. 23, 1534–1541 (2005).
We take the quality of our products very seriously. All our proteins are produced in-house by our scientists and we understand the potential impact on your work if your growth factors and cytokines are not consistent and of the highest quality. We provide quality control data for each individual batch, please contact us any time if you have any questions.