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Recombinant Mouse Activin RIA/ALK-2 Fc Chimera Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse Activin RIA/ALK-2 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Mouse Activin RIA Fc Chimera is immobilized at 2 μg/mL (100 μL/well), the concentration of Recombinant Human BMP‑6 (Catalog # 507-BP) that produces 50% of the optimal binding response is found to be 6-60 ng/mL.
Source
Mouse myeloma cell line, NS0-derived mouse Activin RIA/ALK-2 protein
Mouse Activin RIA
(Met1-Glu123)
Accession # P37172		IEGRMDP Mouse IgG2A
(Glu98-Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
Asp23
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
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
  • Bioactivity
Theoretical MW
38.4 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
45-50 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 visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 250 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 RIA/ALK-2 Fc Chimera Protein, CF

  • activin A receptor, type I
  • Activin RIA
  • ActivinRIA
  • ACTRI
  • ACVR1
  • ACVR1A
  • ACVRLK2
  • ALK2
  • ALK-2
  • FOP
  • SKR1
  • TSRI

Background

Activin RIA, also known as ALK-2, TSK-7L, SKR1, TSR-I, and ACTR-I, is a glycosylated 65 kDa type I receptor in the TGF-beta serine/threonine kinase receptor family (1-3). Binding of TGF-beta superfamily ligands induces formation of a heterotetrameric complex that contains two chains each of a type I and a type II receptor in multiple combinations. The type II receptors phosphorylate the type I receptors which then phosphorylate and activate Smad signal transduction proteins (1, 2). Activin RIA functions in a wide variety of growth and differentiation processes including gastrulation, skeletal system development, and cardiac morphogenesis (1 4‑7). Mature mouse Activin RIA consists of a 103 aa extracellular domain (ECD), a 23 aa transmembrane segment, and a 363 aa cytoplasmic region that includes a Gly/Ser-rich GS box and the kinase domain (8). Within the ECD, mouse Activin RIA shares 99% and 93% aa sequence identity with human and rat Activin RIA, respectively. It shares 24%-26% aa sequence identity with other mouse type I receptors Activin RIB, BMPR-IA, BMPR-IB, and TGF-beta RI. BMP signaling through Activin RIA is enhanced by the direct interaction between Activin RIA and RGM-B/DRAGON, a BMP coreceptor that also associates with other type I and type II receptors (9). Activin RIA can additionally phosphorylate the co‑receptor Endoglin and blocks the inhibitory effect of Endoglin on prostate cancer cell motility (10).
  1. Wu, M.Y. and C.S. Hill (2009) Dev. Cell 16:329.
  2. Nickel, J. et al. (2009) Cytokine Growth Factor Rev. 20:367.
  3. de Caestecker, M. (2004) Cytokine Growth Factor Rev. 15:1.
  4. Chuva de Sousa Lopes, S.M. et al. (2004) Genes Dev. 18:1838.
  5. Zhang, D. et al. (2003) J. Bone Miner. Res. 18:1593.
  6. van Dinther, M. et al. (2010) J. Bone Miner. Res. 25:1208.
  7. Wang, J. et al. (2005) Dev. Biol. 286:299.
  8. Ebner, R. et al. (1993) Science 260:1344.
  9. Samad, T.A. et al. (2005) J. Biol. Chem. 280:14122.
  10. Romero, D. et al. (2010) Carcinogenesis 31:359.

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