Recombinant Human Activin AC Heterodimer Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. In a 100 µL reaction mixture containing rhActivin AC at 2 nM and rhActivin RIIB/Fc Chimera dilutions at 0.02-41 nM, the concentration of rhActivin RIIB/Fc Chimera (Catalog # 339-RBB) that produces 50% of the optimal binding response is found to be approximately 0.8-4 nM.
Source
Chinese Hamster Ovary cell line, CHO-derived human Activin AC protein
Human Activin beta A (Gly311 - Ser426) Accession # NP_002183
Human Activin beta C (Gly237 - Ser352) Accession # NP_005529
Gly311 ( beta A subunit) & Gly237 ( beta C subunit)
Structure / Form
Disulfide-linked heterodimer
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
Binding Activity
Theoretical MW
12.9 kDa ( beta A subunit), 12.5 kDa ( beta C subunit). 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
23 kDa, reducing conditions
Publications
Read Publications using 4879-AC/CF in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in HCl.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile 4 mM HCI.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Activin AC Heterodimer Protein, CF
Activin AC
Background
Activins and inhibins are TGF-beta superfamily proteins that regulate a wide range of processes including mesoderm induction, reproductive system development and function, liver growth and regeneration, wound healing, and inflammation. Activins and inhibins share a variety of beta subunits, while inhibins also possess a unique alpha subunit. There are four human inhibin beta subunits ( beta A beta B beta C and beta E ) and a single inhibin alpha subunit, each of which adopts a cysteine-knot structure (1 - 5). Activin AC is a 23 kDa heterodimer of beta A and beta C subunits (6). Human beta A consists of a 20 amino acid (aa) signal sequence, a 290 aa propeptide, and a 116 aa mature segment, while beta C consists of an 18 aa signal sequence, a 218 aa propeptide, and a 116 aa mature segment (8, 9). The subunit beta propeptides are required for subunit folding, dimerization, and secretion (10). Mature human beta A shares 64%, 51%, and 44% aa sequence identity with human beta B beta C and beta E respectively. Sequence identity between human, mouse, and rat is 100% for mature beta A and 91% - 93% for mature beta C . The beta A and beta C subunits are both expressed in the liver, pituitary, ovary, testis, and adrenal gland (1, 6, 11). The beta C subunit may dimerize with beta A beta B or the inhibin alpha subunit (6, 7). Overexpression of beta C results in increased production of Activin AC as well as a reduction in beta A expression and activin induced signaling (12, 13). The beta C subunit modulates activin induced effects in a variety of systems by forming intracellular dimers with the beta A subunit and impeding the release of Activins A, AB, and B (2, 12). Activins signal through heterodimeric receptor complexes composed of type I (Activin RIA or RIB) and type II (Activin RIIA or RIIB) transmembrane Ser/Thr kinases.
Thompson, T.B. et al. (2004) Mol. Cell. Endocrinol. 225:9.
Butler, C.M. et al. (2005) Cytokine Growth Factor Rev. 16:377.
Abe, Y. et al. (2004) Growth Factors 22:105.
Vitt, U.A. et al. (2001) Mol. Endocrinol. 15:681.
Werner, S. and C. Alzheimer (2006) Cytokine Growth Factor Rev. 17:157.
Mellor S.L. et al. (2000) J. Clin. Endocrinol. Metab. 85:4851.
Ushiro, Y. et. al. (2006) J. Reprod. Devel. 52:487.
Mason, A.J. et al. (1986) Biochem. Biophys. Res. Commun. 135:957.
Hötten, G. et al. (1995) Biochem. Biophys. Res. Commun. 206:608.
Gray, A.M. and A.J. Mason (1990) Science 247:1328.
Gold, E.J. et al. (2004) Mol. Cell. Endocrinol. 222:61.
Mellor, S.L. et al. (2003) Endocrinology 144:4410.
Wada, W. et al. (2004) Am. J. Physiol. Endocrinol. Metab. 287:E247.
Publications for Activin AC (4879-AC/CF)(3)
We have publications tested in 2 confirmed species: Human, Mouse.
We have publications tested in 2 applications: Cell Culture, Surface Plasmon Resonance.
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