Human Activin B Precursor Antibody Summary
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
Detection of Activin B in A375 cells (positive) and U266 cells (negative). Activin B was detected in 10% Formalin fixed A375 human melanoma cell line (Positive) and absent in U266 human myeloma cell line (Negative) using Mouse Anti-Human Activin B Precursor Monoclonal Antibody (Catalog # MAB11450) at 8 µg/ml for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red; Catalog # NL007) and counterstained with DAPI (Blue). Specific staining was localized to cytoplasmic. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.
Detection of Activin B in PC-3 cells (positive) and U266 cells (negative). Activin B was detected in 10% Formalin fixed PC‑3 human prostate cancer cell line (Positive) and absent in U266 human myeloma cell line (Negative) using Mouse Anti-Human Activin B Precursor Monoclonal Antibody (Catalog # MAB11450) at 8 µg/ml for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red; Catalog # NL007) and counterstained with DAPI (Blue). Specific staining was localized to cytoplasmic. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Activin B
Activin and Inhibin are members of the TGF-beta superfamily of cytokines and are involved in a wide range of biological processes including tissue morphogenesis and repair, fibrosis, inflammation, neural development, hematopoiesis, reproductive system function, and carcinogenesis (1‑7). Activin and Inhibin are produced as precursor proteins. Their amino terminal propeptides are proteolytically cleaved and facilitate formation of disulfide-linked dimers of the bioactive proteins (8, 9). Activins are nonglycosylated homodimers or heterodimers of various beta subunits ( beta A, beta B, beta C, and beta E in mammals), while Inhibins are heterodimers of a unique alpha subunit and one of the beta subunits. Activin A is a widely expressed homodimer of two beta A chains. The beta A subunit can also heterodimerize with a beta B or beta C subunit to form Activin AB and Activin AC, respectively (10). The 14 kDa mature human beta A chain shares 100% amino acid sequence identity with bovine, feline, mouse, porcine, and rat beta A. Activin A exerts its biological activities by binding to the type 2 serine/threonine kinase Activin RIIA which then noncovalently associates with the type 1 serine/threonine kinase Activin RIB/ALK-4 (7, 11). Signaling through this receptor complex leads to Smad activation and regulation of activin-responsive gene transcription (7, 11). The bioactivity of Activin A is regulated by a variety of mechanisms (11). BAMBI, Betaglycan, and Cripto are cell-associated molecules that function as decoy receptors or limit the ability of Activin A to induce receptor complex assembly (12‑14). The intracellular formation of Activin A can be prevented by the incorporation of the beta A subunit into Activin AC or Inhibin A (3, 10). And the bioavailability of Activin A is restricted by its incorporation into inactive complexes with alpha 2-Macroglobulin, Follistatin, and FLRG (15, 16).
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- Maeshima, A. et al. (2008) Endocr. J. 55:1.
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- Werner, S. and C. Alzheimer (2006) Cytokine Growth Factor Rev. 17:157.
- Xu, P. and A.K. Hall (2006) Dev. Biol. 299:303.
- Shav-Tal, Y. and D. Zipori (2002) Stem Cells 20:493.
- Chen, Y.G. et al. (2006) Exp. Biol. Med. 231:534.
- Gray, A.M. and A.J. Mason (1990) Science 247:1328.
- Mason, A.J. et al. (1996) Mol. Endocrinol. 10:1055.
- Thompson, T.B. et al. (2004) Mol. Cell. Endocrinol. 225:9.
- Harrison, C.A. et al. (2005) Trends Endocrinol. Metab. 16:73.
- Onichtchouk, D. et al. (1999) Nature 401:480.
- Gray, P.C. et al. (2002) Mol. Cell. Endocrinol. 188:254.
- Kelber, J.A. et al. (2008) J. Biol. Chem. 283:4490.
- Phillips, D.J. et al. (1997) J. Endocrinol. 155:65.
- Schneyer, A. et al. (2003) Endocrinology 144:1671.
Product Datasheets
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