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Recombinant Human Activin RIIA Fc Chimera Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human Activin RIIA Fc Chimera Protein, CF Summary

Additional Information
A New Activin RIIA is Available! ~2-3x better activity; Lower endotoxin specification; CHO expressed!
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 0.03-0.1 µg/mL of rhActivin RIIA/Fc Chimera will inhibit 50% of the biological response due to 3 ng/mL of rhActivin A.
Source
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human Activin RIIA protein
Human Activin RIIA
(Ser25 - Pro134)
Accession # P27037		 IEGRMD Human IgG1
(Pro100 - Lys330)		 6-His tag
N-terminus C-terminus
Accession #
N-terminal Sequence
Ser25
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
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
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
50 kDa, reducing conditions
Publications
Read Publications using
340-R2/CF in the following applications:

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 sterile 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 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 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. 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. Shoji, H. et al. (2000) J. Biol. Chem. 275:5485.
  12. Matsuzaki, T. et al. (2002) J. Biol. Chem. 277:19008.

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    Publications for Activin RIIA (340-R2/CF)(5)

    We have publications tested in 2 confirmed species: Human, Bovine.

    We have publications tested in 3 applications: Bioassay, ELISA (detection), Surface Plasmon Resonance.


    Filter By Application
    Bioassay
    (4)
    ELISA (detection)
    (1)
    Surface Plasmon Resonance
    (1)
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    Filter By Species
    Human
    (3)
    Bovine
    (1)
    All Species
    Showing Publications 1 - 5 of 5.
    Publications using 340-R2/CF Applications Species
    K Sakamoto, Y Kanematsu-, Y Kamada, M Oka, T Ohnishi, M Miwa, T Asami, H Inooka Identification of ligand-selective peptidic ActRIIB-antagonists using phage display technology Biochem Biophys Rep, 2017-06-10;11(0):33-39. 2017-06-10 [PMID: 28955765] (Bioassay) Bioassay
    BR Yoon, YH Chung, SJ Yoo, K Kawara, J Kim, IS Yoo, CG Park, SW Kang, WW Lee Preferential Induction of the T Cell Auxiliary Signaling Molecule B7-H3 on Synovial Monocytes in Rheumatoid Arthritis J. Biol. Chem, 2015-12-23;291(8):4048-57. 2015-12-23 [PMID: 26702052] (Bioassay, Human) Bioassay Human
    Y Kienast, U Jucknischk, S Scheiblich, M Thier, M de Wouters, A Haas, C Lehmann, V Brand, D Bernicke, K Honold, S Lorenz Rapid Activation of Bone Morphogenic Protein 9 by Receptor-mediated Displacement of Pro-domains J. Biol. Chem, 2015-12-16;291(7):3395-410. 2015-12-16 [PMID: 26677222] (Bioassay, Human) Bioassay Human
    Sengle G, Ono RN, Lyons KM, Bachinger HP, Sakai LY A new model for growth factor activation: type II receptors compete with the prodomain for BMP-7. J. Mol. Biol., 2008-07-02;381(4):1025-39. 2008-07-02 [PMID: 18621057] (ELISA (detection), Surface Plasmon Resonance, Human) ELISA (detection), Surface Plasmon Resonance Human
    Fazzini M, Vallejo G, Colman-Lerner A, Trigo R, Campo S, Baranao JL, Saragueta PE Transforming growth factor beta1 regulates follistatin mRNA expression during in vitro bovine granulosa cell differentiation. J. Cell. Physiol., 2006-04-01;207(1):40-8. 2006-04-01 [PMID: 16245315] (Bioassay, Bovine) Bioassay Bovine

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    Bioinformatics

    Gene Symbol ACVR2A
    Uniprot