Recombinant Human/Mouse/Rat Activin A, Animal-Free Protein Summary
| Details of Functionality |
Measured by its ability to induce hemoglobin expression in K562 human chronic myelogenous leukemia cells. Schwall, R.H. et al. (1991) Method Enzymol. 198:340. The ED50 for this effect is 0.200-1.20 ng/mL.
The specific activity of Recombinant Human/Mouse/Rat Activin A is >1000 units/mg, which is calibrated against the human Activin A WHO reference standard (NIBSC code: 91/626). |
| Source |
E. coli-derived Activin A protein
Gly311-Ser426
Produced using non-animal reagents in an animal-free laboratory. |
| Accession # |
|
| N-terminal Sequence |
Gly311 |
| Structure / Form |
Disulfide-linked homodimer |
| Protein/Peptide Type |
Animal-Free Recombinant Proteins |
| Gene |
INHBA |
| Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
| Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
| Dilutions |
|
| Theoretical MW |
13 kDa (monomer).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
| SDS-PAGE |
14 kDa, reducing conditions
24 kDa, non-reducing conditions |
Packaging, Storage & Formulations
| Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
| Buffer |
Lyophilized from a 0.2 μm filtered solution in HCl. |
| Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
| Reconstitution Instructions |
Reconstitute at 100-500 μg/mL in sterile 4 mM HCl. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human/Mouse/Rat Activin A, Animal-Free Protein
Background
Activin and Inhibin are
members of the TGF-beta superfamily of cytokines and are involved in a wide range
of biological processes including tissue morphogenesis and repair, fibrosis,
inflammation, neural development, hematopoiesis, reproductive system function,
and carcinogenesis (1‑7). Activin and Inhibin are produced as precursor
proteins. Their amino terminal propeptides are proteolytically cleaved and
facilitate formation of disulfide-linked dimers of the bioactive proteins (8,
9). Activins are nonglycosylated homodimers or heterodimers of various beta
subunits ( beta A, beta B, beta C, and beta E in mammals), while Inhibins are heterodimers of a
unique alpha subunit and one of the beta subunits. Activin A is a widely
expressed homodimer of two beta A chains. The beta A subunit can also heterodimerize
with a beta B or beta C subunit to form Activin AB and Activin AC,
respectively (10). The 14 kDa mature human beta A chain shares 100% amino acid
sequence identity with bovine, feline, mouse, porcine, and rat
beta A.
Activin A
exerts its biological activities by binding to the type 2 serine/threonine
kinase Activin RIIA which then noncovalently associates with the type
1 serine/threonine kinase Activin RIB/ALK-4 (7, 11). Signaling through this
receptor complex leads to Smad activation and regulation of activin-responsive
gene transcription (7, 11). The bioactivity of Activin A is regulated
by a variety of mechanisms (11). BAMBI, Betaglycan, and Cripto are cell‑associated
molecules that function as decoy receptors or limit the ability of
Activin A to induce receptor complex assembly (12‑14). The
intracellular formation of Activin A can be prevented by the
incorporation of the beta A subunit into Activin AC or Inhibin A (3, 10).
And the bioavailability of Activin A is restricted by its
incorporation into inactive complexes with alpha 2-Macroglobulin, Follistatin, and
FLRG (15, 16).
Activin A is involved
in the differentiation of various cell and tissue types. The induction of
definitive endoderm by Activin A is required in differentiation protocols of
induced pluripotent stem cells (iPSCs) (17, 18). In vitro models of human
gametogenesis use prolonged Activin A supplementation to human embryonic stem
cells for differentiation into human primordial germ cell-like cells (19).
Activin A can also be used to maintain cells in vitro, as is the case for
iPSC-derived nephron cells that can then be used in disease modeling, drug
screening and in regenerative medicine (20).
Activin
A is an important factor for tumor cells to evade the immune system as Activin
A can act on surrounding immune cells to decrease their antitumor activity
(21). Activin A also promotes migration and growth of tumors, making it a target
for cancer therapies (22). Specifically, research has shown that interfering
with Activin A activity can assist in overcoming CD8 T-cell exclusion and
immunotherapy resistance (23). In bone marrow-derived stem cell transplants for
treatment of diabetes, Activin A enhances migration and homing of stem cells
towards pancreatic lineage (24).
- Kumanov,
P. et al. (2005) Reprod. Biomed. Online
10:786.
- Maeshima, A. et
al. (2008) Endocr. J. 55:1.
- Rodgarkia-Dara,
C. et al. (2006) Mutat. Res.
613:123.
- Werner, S. and C. Alzheimer
(2006) Cytokine Growth Factor Rev.
17:157.
- Xu, P. and A.K. Hall (2006) Dev.
Biol. 299:303.
- Shav-Tal, Y. and D. Zipori
(2002) Stem Cells 20:493.
- Chen, Y.G. et al. (2006) Exp. Biol. Med.
231:534.
- Gray, A.M. and A.J. Mason
(1990) Science 247:1328.
- Mason, A.J. et al. (1996) Mol. Endocrinol.
10:1055.
- Thompson, T.B. et
al. (2004) Mol. Cell. Endocrinol.
225:9.
- Harrison, C.A. et
al. (2005) Trends Endocrinol. Metab.
16:73.
- Onichtchouk, D. et
al. (1999) Nature
401:480.
- Gray, P.C. et
al. (2002) Mol. Cell. Endocrinol.
188:254.
- Kelber, J.A. et
al. (2008) J. Biol. Chem.
283:4490.
- Phillips, D.J. et
al. (1997) J. Endocrinol.
155:65.
- Schneyer, A. et
al. (2003) Endocrinology
144:1671.
- Ghorbani-Dalini, S. et al. (2020) 3 Biotech.
10:215.
- Mennen, R. H. et
al. (2022) Reprod Toxicol. 107:44.
- Mishra,
S. et al. (2021) Stem Cells.
39:551.
- Tanigawa, S. et
al. (2019) Stem Cell Reports
13:322.
- Cangkrama, M. et
al. (2020) Trends Mol. Med.
26:1107.
- Ries, A. et
al. (2020) Expert Opin. Ther. Targets.
24:985.
- Pinjusic, K. et
al. (2022) J. Immunother. Cancer.
10:e004533.
- Dadheech, N. et
al. (2020) Stem Cell Res. Ther. 11:327.
Manufacturing Process
Animal-Free Manufacturing Conditions
Our dedicated controlled-access animal-free laboratories ensure that at no point in production are the products exposed to potential contamination by animal components or byproducts. Every stage of manufacturing is conducted in compliance with R&D Systems' stringent Standard Operating Procedures (SOPs). Production and purification procedures use equipment and media that are confirmed animal-free.
Production
- All molecular biology procedures use animal-free media and dedicated labware.
- Dedicated fermentors are utilized in committed animal-free areas.
Purification
- Protein purification columns are animal-free.
- Bulk proteins are filtered using animal-free filters.
- Purified proteins are stored in animal-free containers in a dedicated cold storage room.
Quality Assurance
- Low Endotoxin Level.
- No impairment of biological activity.
- High quality product obtained under stringent conditions.
- For ex vivo research or bioproduction, additional documentation can be provided.
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