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High quality food grade for cultivated meat, fish, fat and dairy

Recombinant bovine/porcine activin A PLUS™ protein (Qk109-FG)

Bovine/porcine high quality food grade recombinant activin A PLUS™ protein is an optimised biologically active truncation of the mature domain of human activin A protein.  The EC50 and activity in stem cell culture of activin A PLUS™ is equivalent to the full mature domain activin A.

High purity 24 kDa dimer comprising truncated mature domain of activin A protein, animal origin-free (AOF) and carrier-protein free (CF).  Recombinant activin A PLUS™ is designed to be manufactured at scale for cost-effective, large-scale stem cell culture applications for cultured meat and fat.

Orders are typically shipped same or next day (except Friday).
Easy world-wide ordering, direct or through our distributors.

1mg will be despatched as 2 x 500µg

Available on request.
For any questions, please email orders@qkine.com

Summary

  • High purity optimized mature domain of bovine/porcine activin A (Uniprot: P07995) – particularly suitable for bulk and scale-up stem cell culture applications

  • >98%, by SDS-PAGE quantitative densitometry

  • Cross-reactivity: bovine, porcine, human, mouse (murine), rat

  • 24 kDa (dimer)

  • Expressed in E. coli

  • Animal origin-free (AOF) and carrier protein-free

  • Manufactured in our Cambridge, UK laboratories

  • Lyophilized from acetonitrile, TFA

  • Resuspend in 10mM HCl at >100 µg/ml (provided with protein and free of charge), prepare single use aliquots, add carrier protein if desired and store frozen at -20°C or -80°C

Featured applications

  • Large scale stem cell expansion

ActA, Activin beta-A chain, Erythroid differentiation protein (EDP), Follicle-Stimulating Hormone (FSH) releasing protein (FRP), INHBA, Inhibin beta A, Inhibin beta 1

Bioactivity

Human Activin A PLUS Qk005 protein bioactivity lot #010

Activin A PLUS™ activity is determined using an activin-responsive firefly luciferase reporter in HEK293T cells. in triplicate) with a serial dilution of activin A for 6 hours.  Firefly luciferase activity is measured and normalized to the control Renilla luciferase activity. EC50 = 0.103 ng/ml (4.24 pM).  EC50 is within the expected range of 6 ± 2 pM.  Data from Qk005 lot #104344.

Purity

Human Activin A PLUS Qk005 protein purity SDS-PAGE lot #010

Activin A PLUS™ migrates as a single band at 24 kDa in non-reducing (NR) and 13 kDa as a single monomeric species upon reduction (R).  No contaminating protein bands are visible. Purified recombinant protein (7 µg) was resolved using 15% w/v SDS-PAGE in reduced (+β-mercaptothanol, R) and non-reduced conditions (NR) and stained with Coomassie Brilliant Blue R250.  Data from Qk005 lot #010.

Further quality assays

  • Mass spectrometry: single species with expected mass

  • Analytical reversed-phase: single sharp peak

  • Endotoxin: <0.005 EU/μg protein (below level of detection)

  • Recovery from stock vial:  >95%

We are a company founded and run by scientists to provide a service and support innovation in stem cell biology and regenerative medicine.  All our products are exceptionally high purity, with complete characterisation and bioactivity analysis on every lot.

Protein background

Activin A is a member of the TGFβ superfamily of growth factors used in stem cell differentiation and maintenance.  Activin A PLUS™, an engineered optimized form of activin A, incorporates an N-terminal truncation to remove a disulfide-linked extension. The resulting protein can be manufactured at extremely consistent high yield with no observed changes in bioactivity compared to the wild-type. This form is particularly suitable for large scale stem cell culture processes.

Activin A is involved in regulation of embryogenesis, development of the reproductive system, wound healing and regulation of immune responses in vivo. The activity of activin A is regulated by the high-affinity inhibitor, follistatin [1], and inhibins.  Activins are disulfide-linked homo- and heterodimers of four inhibin β chains. The best characterized 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, stabilization, transportation and signalling of the growth factors [2].

[1] Harrington, A. E. et al. Structural basis for the inhibition of activin signalling by follistatin. EMBO J. 25, 1035–1045 (2006). doi/10.1038/sj.emboj.7601000

[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). doi.org/10.1242/dev.091769

[4] D’Amour, K. A. et al. Efficient differentiation of human embryonic stem cells to definitive endoderm. Nat. Biotechnol. 23, 1534–1541 (2005). doi.org/10.1038/nbt1163

Qkine high quality food grade products are intended solely for use as food processing aids, ex vivo cell manufacturing and research use. Not for direct human consumption, therapeutic or diagnostic use.

The authorization of novel foods, including the use of growth factors as food processing aids, is regulated by regional government agencies. The use of our products as food processing aids in novel foods requires the end-user to obtain the necessary regulatory approvals.

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