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Human/Mouse/Rat Activin A Biotinylated MAb (Clone 69403) (100 UG)

货号: BAM3381 基本售价: 5512.4 元 规格: 100 ug

产品信息

概述
货号BAM3381
描述For ELISA the Antibody Pairs information:Capture antibody:MAB3381-500;Detection antibody:BAM3381; and protein: 338-AC-005
别名INHBA
反应种属Human/Mouse/Rat
应用ELISA Capture (Matched Antibody Pair)(2-8 µg/mL )
ELISA Detection (Matched Antibody Pair)(0.5-2.0 µg/mL )
目标/特异性Detects human Activin A in direct ELISAs. Recognizes proteins containing the precursor or mature beta A subunits. The amino acid sequences of mature beta A subunits from human, mouse, and rat are identical. Therefore, this antibody will also detect the mature beta A subunits from mouse and rat.
使用方法ELISA Capture (Matched Antibody Pair): 2-8 µg/mL 
ELISA Detection (Matched Antibody Pair): 0.5-2.0 µg/mL 
来源Reconstitute at 0.5 mg/mL in sterile PBS.
产品组分
性能
供应商R&D Systems
Entrez Gene IDs3624 (Human); 16323 (Mouse)
应用文献
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

Fibroblast growth factor 2 modulates transforming growth factor beta signaling in mouse embryonic fibroblasts and human ESCs (hESCs) to support hESC self-renewal.
Authors: Greber B, Lehrach H, Adjaye J
Stem Cells, 2006;25(2):455-64.
Species: Mouse
Sample Type: Cell Culture Supernates
Application: ELISA Development

纯化方式Protein A or G purified from ascites
免疫原Chinese hamster ovary cell line CHO-derived recombinant human Activin A and recombinant human Pro-Activin A
生物活性Human, Mouse, Rat
标记Biotin
溶解方法Reconstitute at 0.5 mg/mL in sterile PBS.
背景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).
运输条件Blue Ice
存放说明-20℃
参考文献
  1. Kumanov, P. et al. (2005) Reprod. Biomed. Online 10:786.
  2. Maeshima, A. et al. (2008) Endocr. J. 55:1.
  3. Rodgarkia-Dara, C. et al. (2006) Mutat. Res. 613:123.
  4. Werner, S. and C. Alzheimer (2006) Cytokine Growth Factor Rev. 17:157.
  5. Xu, P. and A.K. Hall (2006) Dev. Biol. 299:303.
  6. Shav-Tal, Y. and D. Zipori (2002) Stem Cells 20:493.
  7. Chen, Y.G. et al. (2006) Exp. Biol. Med. 231:534.
  8. Gray, A.M. and A.J. Mason (1990) Science 247:1328.
  9. Mason, A.J. et al. (1996) Mol. Endocrinol. 10:1055.
  10. Thompson, T.B. et al. (2004) Mol. Cell. Endocrinol. 225:9.
  11. Harrison, C.A. et al. (2005) Trends Endocrinol. Metab. 16:73.
  12. Onichtchouk, D. et al. (1999) Nature 401:480.
  13. Gray, P.C. et al. (2002) Mol. Cell. Endocrinol. 188:254.
  14. Kelber, J.A. et al. (2008) J. Biol. Chem. 283:4490.
  15. Phillips, D.J. et al. (1997) J. Endocrinol. 155:65.
  16. Schneyer, A. et al. (2003) Endocrinology 144:1671.