Recombinant Human Activin A Hyperactive Protein, CF

R&D Systems, part of Bio-Techne | Catalog # BT-ACTAH

R&D Systems, part of Bio-Techne
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BT-ACTAH-010
BT-ACTAH-01M
BT-ACTAH-050
BT-ACTAH-100
BT-ACTAH-500
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Key Product Details

Source

CHO

Accession #

P08476.2

Structure / Form

Disulfide-linked homodimer

Conjugate

Unconjugated

Applications

Bioactivity

View all Activin A Proteins and Enzymes »

Product Specifications

Source

Chinese Hamster Ovary cell line, CHO-derived human Activin A protein
Gly311-Ser426, F368A

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Gly311

Predicted Molecular Mass

13 kDa

SDS-PAGE

12-14 kDa, under reducing conditions.

Activity

Measured by its ability to induce cytotoxicity using MPC-11 mouse B lymphocyte cells.
The ED50 for this effect is 1.00-15.0 ng/mL.

Scientific Data Images for Recombinant Human Activin A Hyperactive Protein, CF

Recombinant Human Activin A Hyperactive Protein Bioactivity.

Human Activin A Hyperactive Protein (Catalog # BT-ACTAH) induces cytotoxicity on MCP-11 cells. The ED50 for this effect is 1.00 15.0 ng/mL. The hyperactive Activin A protein has greater bioactivity than Wild Type Activin A.

Recombinant Human Activin A Hyperactive Protein Bioactivity.

Human Activin A Hyperactive Protein (Catalog # BT-ACTAH) induces SBE (SMAD-binding element) reporter activity in HEK293 human embryonic kidney cells. The hyperactive Activin A protein has greater bioactivity than Wild Type Activin A.

Recombinant Human Activin A Hyperactive Protein SDS-PAGE.

2 μg/lane of Recombinant Human Activin A Hyperactive Protein (Catalog # BT-ACTAH) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 12-14 kDa and 20-30 kDa, respectively.

Formulation, Preparation and Storage

BT-ACTAH
Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with Trehalose.
Reconstitution Reconstitute the 10 μg size at 100 μg/mL in sterile 4 mM HCl. Reconstitute all other sizes at 500 μg/mL in sterile 4 mM HCl.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

Background: Activin A

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 ( betaA, betaB, betaC, and betaE 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 betaA chains. The betaA subunit can also heterodimerize with a betaB or betaC subunit to form Activin AB and Activin AC, respectively (10). The 14 kDa mature human betaA chain shares 100% amino acid sequence identity with bovine, feline, mouse, porcine, and rat betaA. 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 betaA subunit into Activin AC or Inhibin A (3, 10). And the bioavailability of Activin A is restricted by its incorporation into inactive complexes with alpha2-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). With AI assisted designing, this engineered rhActivinA shows superior activity compared to the wild type. 

References

  1. Kumanov, P. et al. (2005) Reprod. Biomed. Online 10:786.
  2. Maeshima, A. et al. (2008) Endocr. J. 55:1.
  3. Rodgarkia-Dara, C. et al. (2006) Mutat. Res. 613:123.
  4. Werner, S. and C. Alzheimer (2006) Cytokine Growth Factor Rev. 17:157.
  5. Xu, P. and A.K. Hall (2006) Dev. Biol. 299:303.
  6. Shav-Tal, Y. and D. Zipori (2002) Stem Cells 20:493.
  7. Chen, Y.G. et al. (2006) Exp. Biol. Med. 231:534.
  8. Gray, A.M. and A.J. Mason (1990) Science 247:1328.
  9. Mason, A.J. et al. (1996) Mol. Endocrinol. 10:1055.
  10. Thompson, T.B. et al. (2004) Mol. Cell. Endocrinol. 225:9.
  11. Harrison, C.A. et al. (2005) Trends Endocrinol. Metab. 16:73.
  12. Onichtchouk, D. et al. (1999) Nature 401:480.
  13. Gray, P.C. et al. (2002) Mol. Cell. Endocrinol. 188:254.
  14. Kelber, J.A. et al. (2008) J. Biol. Chem. 283:4490.
  15. Phillips, D.J. et al. (1997) J. Endocrinol. 155:65.
  16. Schneyer, A. et al. (2003) Endocrinology 144:1671.
  17. Ghorbani-Dalini, S. et al. (2020) 3 Biotech. 10:215.
  18. Mennen, R.H. et al. (2022) Reprod Toxicol. 107:44.
  19. Mishra, S. et al. (2021) Stem Cells. 39:551.
  20. Tanigawa, S. et al. (2019) Stem Cell Reports 13:322.
  21. Cangkrama, M. et al. (2020) Trends Mol. Med. 26:1107.
  22. Ries, A. et al. (2020) Expert Opin. Ther. Targets. 24:985.
  23. Pinjusic, K. et al. (2022) J. Immunother. Cancer. 10:e004533.
  24. Dadheech, N. et al. (2020) Stem Cell Res. Ther. 11:327.

Alternate Names

activin AB alpha polypeptide, Activin beta-A chain, erythroid differentiation factor, Erythroid differentiation protein, follicle-stimulating hormone-releasing protein, FSH-releasing protein, inhibin beta A chain, inhibin beta A subunit, Inhibin, beta-1

Entrez Gene IDs

3624 (Human); 16323 (Mouse); 29200 (Rat)

Gene Symbol

INHBA

UniProt

P08476.2

Additional Activin A Products

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Product Specific Notices for Recombinant Human Activin A Hyperactive Protein, CF

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