Recombinant human activin A protein (Qk001-CTG) Price range: £3,035.00 through £4,785.00View product
Recombinant human activin A protein (Qk001-CTG)
Price range: £3,035.00 through £4,785.00
Activin A is a TGF-β family growth factor frequently used to maintain pluripotency in induced pluripotent and embryonic stem cell cultures. It is essential for many stem cell differentiation protocols, including endoderm lineage differentiation and further maturation into hepatocyte and pancreatic cells for regenerative cell therapy applications.
Cell therapy grade human activin A protein is a high-purity mature bioactive dimer of 26 kDa. It is animal origin-free (AOF), carrier protein-free, and tag-free to ensure its purity with exceptional lot-to-lot consistency.
Qkine cell therapy grade high purity animal origin-free proteins are manufactured as GMP grade equivalents in an ISO 9001:2015-certified facility, under ISO 20399:2022 standards with GMP compliance, defined quality criteria and documentation.Â
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Orders are typically shipped same or next day (except Friday).
Easy world-wide ordering, direct or through our distributors.
Price range: £3,035.00 through £4,785.00
1000µg will be despatched as 2 x 500µg
Buy online with secure credit card or purchase order. For any questions, please email orders@qkine.com
Summary:
- Bioactive mature domain of recombinant human activin A protein, residues 311-426 (Uniprot: P08476)
- 26 kDa (dimer)
Certified animal origin-free (AOF)
Cell and gene therapy grade
Manufactured in our ISO 9001:2015 facility in Cambridge, UK
Lot-to-lot consistency in bioactivity
Full traceability and documentation
Carrier protein-free, tag free
Expressed in E. coli
Lyophilized from acetonitrile, TFA
- Resuspend in 10 mM HCl (Reconstitution solution A) at >50 µg/ml, add carrier protein if desired, prepare single-use aliquots and store frozen at -20 °C (short-term) or -80 °C (long-term)
Featured applications:
Expansion of induced pluripotent, embryonic and mesenchymal stem cells
Regenerative stem cell therapy
Pluripotent stem cell therapy
Alternative proteins
Recombinant activin A activity was determined using a CAGA luciferase reporter assay in transiently transfected HEK293 cells. Transfected cells were treated in triplicate with a serial dilution of activin A for 6 hours. Firefly activity was measured and normalized to the control Renilla luciferase activity. Data from Qk001 #204564. EC50 = 0.27 ng/ml (10.4 pM)
The specific activity of recombinant human activin A GMP is >1.0 x 103 units/mg, which is calibrated against the human activin A standard (NIBSC code: 91/626).
Activin A 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 Qk001 lot #011.
Further quality assays
Mass spectrometry: single species with expected mass
Purity >98%, by SDS-PAGE quantitative densitometry
Recovery from stock vial:Â >95%
Sterility tested and mycoplasma negative
Endotoxin: <0.005 EU/μg protein (below level of detection)
Residual host cell protein <10 ng/µg
Residual host cell DNA <10 ng/μg
N-terminal sequence analysisÂ
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.
Qkine activin A was more active than the WHO (NIBSC) standard activin A. Activin A activity was determined using a CAGA luciferase reporter assay in transiently transfected HEK293 cells. Transfected cells were treated in triplicate with a serial dilution of activin A for 6 hours. Firefly activity was measured and normalized to the control Renilla luciferase activity. Qk001 #204564 EC50 = 0.27 ng/ml (10.4 pM). WHO (NIBSC) standard EC50 = 0.66 ng/ml.
Protein background
Activin A is a member of the belongs to the transforming growth factor beta (TGF-β) superfamily TGF-β family of growth factors [1]–[4]. It was first identified for its ability to stimulate the release of follicle-stimulating hormone (FSH) from the pituitary gland. It was later recognized as a multifunctional protein with diverse cellular effects [5], [6]. It plays crucial physiological roles in regulating embryonic development, cell proliferation, and differentiation [6], [7]. It promotes the patterning and differentiation of various organs, including the development of the mesoderm, neural, and reproductive systems. It is also involved in maintaining homeostasis, regulating immune responses, and wound healing [8]. Impaired activin A signaling has been associated with various pathological conditions, including cancer, inflammation, and fibrosis [9], [10]. As activin A can contribute to disease progression and severity, it is a growing area of research for promising therapeutic targets.
Activins are disulfide-linked homo- and heterodimers of four inhibin β chains [6]. The best-characterized are activin A and activin B, homodimers of inhibin βA and inhibin βB, respectively. Like all other members of the TGF-β family, activins are synthesized as significant 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 essential roles in the biosynthesis, stabilization, transportation and signaling of the growth factors in the body [11]. Activin A binds to activin type I (ALK4 or ALK7) and type II (ActRIIA or ActRIIB) receptors [6], [12]. The type II receptor phosphorylates the type I receptor upon ligand binding, initiating downstream signaling cascades, mainly through the SMAD family of proteins. Activated SMAD complexes translocate into the nucleus, regulating the transcription of target genes involved in various cellular processes. In vivo, the high-affinity inhibitor follistatin and inhibins tightly regulate activin A activity in a feedback loop [13], [14]. Follistatin is secreted into the media during stem cell culture. However, the impact on the efficiency of stem cell differentiation and cellular homogeneity has not been studied closely (see this discussion for more information).
Activin A is frequently used for the maintenance of pluripotency of human induced pluripotent stem cells and human embryonic stem cell lines along with fibroblast growth factor 2 (FGF-2) [2], [4]. Activin A is also used in various stem cell differentiation protocols. It directs the differentiation into definitive endoderm, precursor to different cell types such as pancreatic and liver cells [15]–[18]. Activin A also promotes neural precursor cells and drives astrocytic differentiation with Ciliary neurotrophic factor (CNTF) and Glial cell line-derived neurotrophic factor (GDNF) [19]. Moreover, activin A is also involved in mesodermal differentiation to derive muscle, bone, and blood cells. Finally, activin A is often used for the development and maintenance of organoids [18], [20], [21].
Additional resources
FAQ
What is the function of the activin A protein?
Activin A is a multifunctional protein. It is involved in regulating embryonic development, cell proliferation, and differentiation. It promotes the patterning and differentiation of various organs, including the development of the mesoderm, neural, and reproductive systems. It is also involved in maintaining homeostasis, regulating immune responses, and wound healing. Finally, it stimulates the release of follicle-stimulating hormone from the pituitary gland.Â
What does activin A bind to?
Activin A binds to activin type I (ALK4 or ALK7) and type II (ActRIIA or ActRIIB) receptors to activate downstream SMAD signalling.Â
What are activin A and inhibin A?
Activin A and inhibin A are closely related proteins in the TGF-β superfamily. They share structural similarities but have distinct functions and roles in regulating various physiological processes. Activin A has broader functions beyond reproduction, which include handling embryonic development, stem cell maintenance, and the immune system. Inhibin A, conversely, is more specifically associated with the feedback control of follicle-stimulating hormones in the context of reproductive physiology.Â
What does the activin gene do?
The activin gene family includes several genes that encode different activin subunits, forming various activin isoforms such as Inhibin Beta Subunits (INHBA / INHBB / INHBC / INHBD).Â
What inhibits activin A?
Follistatin and inhibins tightly regulate activin A activity in a feedback loop.Â
Does activin increase LH?
Yes, activin is involved in a feedback loop that regulates the secretion of follicle-stimulating hormone (FSH) and luteinising hormone (LH).Â
What does activin A do in cell culture?
Activin A is a critical factor in stem cell culture, commonly used to maintain the pluripotency of induced pluripotent stem cells (iPSCs) and embryonic stem cells (ESCs). It is integral to various stem cell differentiation protocols, guiding the differentiation of the definitive endoderm, neural and mesodermal lineages. Activin A is also commonly utilized in the development and maintenance of organoids.Â
Special guidance for reconstitution of TGF beta family including activins, BMPs and GDF-15
TGF beta family proteins and other growth factors can be very poorly soluble in physiological solutions. Please follow the handling guidance for lyophilized cytokines below to minimize loss of protein due to precipitation or adsorption to plastic. We advise storing the recombinant protein at very low pH before dilution in cell culture media or final working solutions. Low pH will also assist in maintaining the correct disulfide structure of the protein by minimizing disulfide bond exchange reactions.
- Resuspension in physiological buffers may cause precipitation of stock solutions, hence we recommend dissolving our lyophilized cytokines in 10 mM HCl (1:1000 dilution of concentrated HCl) while keeping the protein concentration at 50 µg/ml or above, in order to avoid loss by adsorption to plasticware.
- To ensure you recover all of the protein, let the sample sit for a few minutes with the solubilization buffer at room temperature and pipette gently up and down (avoid foaming).
- Rinse the tube with some more 10 mM HCl and pool with the rest.
- The protein is tolerant of some freeze and thaw cycles, but as always with proteins, it is better to aliquot and store frozen.
- Our proteins are supplied carrier-protein free. If compatible with your work, add carrier protein of your choice such as BSA, HSA or gelatin to further minimize loss by adsorption.
- Store in -80°C for long term storage. -20°C for short-term.
Every effort is made to ensure samples are sterile; however, we recommend sterile filtering after dilution in media or the final working solution.
Our products are for research use only and not for diagnostic or therapeutic use. Products are not for resale.
For use in manufacturing of cellular or gene therapy products. Not intended for in vivo applications.
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