Recombinant Human Activin RIIA Fc Chimera (CHO) Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human Activin RIIA Fc Chimera (CHO) Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit Activin A-induced hemoglobin expression in K562 human chronic myelogenous leukemia cells. Schwall, R.H. et al. (1991) Method Enzymol. 198:340.

Approximately 0.01-0.05 μg/mL of Recombinant Human (rh) Activin RIIA Fc Chimera will inhibit 50% of the biological response due to 3 ng/mL of rhActivin A.

Source
Chinese Hamster Ovary cell line, CHO-derived human Activin RIIA protein
Human Activin RIIA
(Met1 - Pro134)
Accession # P27037
IEGRMD Human IgG1
(Pro100 - Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Ala20
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
ACVR2A
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
40 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
60-67 kDa, 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 PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Activin RIIA Fc Chimera (CHO) Protein, CF

  • activin A receptor, type II
  • activin A receptor, type IIA
  • Activin receptor type IIA
  • activin receptor type-2A
  • Activin RIIA
  • ActivinRIIA
  • ACTRII
  • ACTRIIA
  • ACVR2A
  • ACVR2ACTR-IIA
  • AVR2A
  • EC 2.7.11
  • EC 2.7.11.30

Background

Activin proteins are involved in a wide range of biological processes including mesoderm induction, neural cell differentiation, bone remodeling, hematopoiesis, the regulation of reproductive physiology, inflammation, and carcinogenesis (1 ‑ 3). They function through heteromeric complexes of type I and type II serine/threonine kinase receptors (2, 4). Dimeric ligands bind to a type II receptor, such as Activin Receptor IIA (ActRIIA), which then associates with a type I receptor to initiate signal transduction (4). ActRIIA mediates the pleiotropic effects of Activins and Inhibins as well as several members of the BMP and GDF families of TGF-beta like proteins (4). Mature human ActRIIA is a 70 kDa glycoprotein that consists of a 116 amino acid (aa) extracellular domain (ECD), a 26 aa transmembrane segment, and a 352 aa cytoplasmic region that includes the kinase domain and a PDZ-binding motif (5). Within the ECD, human ActRIIA shares 98% aa sequence identity with mouse and rat ActRIIA. Signaling through ActRIIA is modulated by its interaction with RGM-B/DRAGON, Cripto, Endoglin/CD105, TGF‑ beta  RIII/Betaglycan, or BAMBI (6 - 10). These interactions can enhance ligand‑induced signaling or interfere with signaling by preventing ActRIIA association with type I receptors (6 - 9). Activin‑induced responses can also be limited by the enhanced internalization of ActRIIA following its association with the cytoplasmic protein ARIP2 (11).
  1. Welt, C. et al. (2002) Exp. Biol. Med. 227:724.
  2. Chen, Y.-G. et al. (2006) Exp. Biol. Med. 231:534.
  3. Werner, S. and C. Alzheimer (2006) Cytokine Growth Factor Rev. 17:157.
  4. de Caestecker, M. (2004) Cytokine Growth Factor Rev. 15:1.
  5. Matzuk, M.M. and A. Bradley (1992) Biochim. Biophys Acta 1130:105.
  6. Samad, T.A. et al. (2005) J. Biol. Chem. 280:14122.
  7. Gray, P.C. et al. (2003) Proc. Natl. Acad. Sci. 100:5193.
  8. Lewis, K.A. et al. (2000) Nature 404:411.
  9. Onichtchouk, D. et al. (1999) Nature 401:480.
  10. Barbara, N.P. et al. (1999) J. Biol. Chem. 274:584.
  11. Matsuzaki, T. et al. (2002) J. Biol. Chem. 277:19008.

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Bioinformatics

Gene Symbol ACVR2A
Entrez
Uniprot