Recombinant Human Activin AC Heterodimer Protein, CF

• Reactivity: Hu
• Applications: Binding Activity
• Format: Carrier-Free

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
  N-terminus	C-terminus

• Accession #: NP_002183 ( beta A) & NP_005529 ( beta C)
• N-terminal Sequence: 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

• 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

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 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.

1. Thompson, T.B. et al. (2004) Mol. Cell. Endocrinol. 225:9. 
2. Butler, C.M. et al. (2005) Cytokine Growth Factor Rev. 16:377. 
3. Abe, Y. et al. (2004) Growth Factors 22:105. 
4. Vitt, U.A. et al. (2001) Mol. Endocrinol. 15:681. 
5. Werner, S. and C. Alzheimer (2006) Cytokine Growth Factor Rev. 17:157. 
6. Mellor S.L. et al. (2000) J. Clin. Endocrinol. Metab. 85:4851.  
7. Ushiro, Y. et. al. (2006) J. Reprod. Devel. 52:487.
8. Mason, A.J. et al. (1986) Biochem. Biophys. Res. Commun. 135:957.
9. Hötten, G. et al. (1995) Biochem. Biophys. Res. Commun. 206:608.
10. Gray, A.M. and A.J. Mason (1990) Science 247:1328.
11. Gold, E.J. et al. (2004) Mol. Cell. Endocrinol. 222:61.
12. Mellor, S.L. et al. (2003) Endocrinology 144:4410.
13. Wada, W. et al. (2004) Am. J. Physiol. Endocrinol. Metab. 287:E247.

Publications for Activin AC (4879-AC/CF)(3)

Publications using 4879-AC/CF

• OE Olsen, H Hella, S Elsaadi, C Jacobi, E Martinez-H, T Holien Activins as Dual Specificity TGF-&amp;beta Family Molecules: SMAD-Activation via Activin- and BMP-Type 1 Receptors Biomolecules, 2020;10(4):. 2020 [PMID: 32235336] (Cell Culture, Human)
• E Latres, J Mastaitis, W Fury, L Miloscio, J Trejos, J Pangilinan, H Okamoto, K Cavino, E Na, A Papatheodo, T Willer, Y Bai, J Hae Kim, A Rafique, S Jaspers, T Stitt, AJ Murphy, GD Yancopoulo, J Gromada Activin A more prominently regulates muscle mass in primates than does GDF8 Nat Commun, 2017;8(0):15153. 2017 [PMID: 28452368] (Surface Plasmon Resonance, Human)
• Castonguay R, Werner ED, Matthews RG, Presman E, Mulivor AW, Solban N, Sako D, Pearsall RS, Underwood KW, Seehra J, Kumar R, Grinberg AV Soluble Endoglin Specifically Binds Bone Morphogenetic Proteins 9 and 10 via Its Orphan Domain, Inhibits Blood Vessel Formation, and Suppresses Tumor Growth. J. Biol. Chem., 2011;286(34):30034-46. 2011 [PMID: 21737454] (Surface Plasmon Resonance, Human)

Bioinformatics

• Uniprot:
  • NP_002183 ( beta A) & NP_005529 ( beta C)()