Recombinant Mouse Activin RIIA Fc Chimera Protein, CF

• Reactivity: Mu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Mouse Activin RIIA Fc Chimera 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. The ED₅₀ for this effect is 6-36 ng/mL in the presence of 3 ng/mL of recombinant human Activin A (Catalog # 338-AC).
• Source: Mouse myeloma cell line, NS0-derived mouse Activin RIIA protein
  

  Mouse Activin RIIA (Met1 - Pro134) Accession # P27038	IEGRMDP	Mouse IgG2A (Glu98 - Lys330)
  N-terminus		C-terminus

• Accession #: P27038
• N-terminal Sequence: Ala20
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• 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

• Dilutions:
  • Bioactivity
• Theoretical MW: 40.5 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: 60-65 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 Mouse Activin RIIA Fc Chimera 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 mouse 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, mouse ActRIIA shares 98% and 100% aa sequence identity with human and rat ActRIIA, respectively. 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 proteins ARIP1 and ARIP2 (11, 12).

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. Mathews, L.S. and W.W. Vale (1991) Cell 65:973.
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. Shoji, H. et al. (2000) J. Biol. Chem. 275:5485.
12. Matsuzaki, T. et al. (2002) J. Biol. Chem. 277:19008.

Bioinformatics

• Uniprot:
  • P27038()