Recombinant Human Activin A / INHBA,low endotoxin
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SynonymActivin A, INHBA
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SourceHuman Activin A,Tag Free, low endotoxin (ACA-H421b) is expressed from human 293 cells (HEK293). It contains AA Gly 311 - Ser 426 (Accession # AAH07858.1).Predicted N-terminus: Gly 311
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Molecular Characterization
This protein carries no "tag".
The protein has a calculated MW of 13 kDa. the protein migrates as 14 kDa under reducing (R) condition, and 27 kDa under non-reducing (NR) condition (SDS-PAGE).
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Endotoxin: Less than 0.1 EU per μg by the LAL method.
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Purity
>95% as determined by SDS-PAGE.
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Formulation
Lyophilized from 0.22 μm filtered solution in 0.056% TFA in 60% ACN. Normally trehalose is added as protectant before lyophilization.
Contact us for customized product form or formulation.
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Reconstitution
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
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Storage
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
No activity loss is observed after storage at:
- 4-8°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Human Activin A,Tag Free, low endotoxin on SDS-PAGE under reducing (R) and no-reducing (NR) conditions. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
Immobilized Human Activin A,Tag Free, low endotoxin at 10μg/mL (100 μL/well) can bind Human ACVR1B, Fc Tag
Immobilized Human Activin A,Tag Free, low endotoxin at 2 μg/mL (100 μL/well) can bind Human ACVR2A, Fc Tag with a linear range of 0.08-1.25 μg/mL (QC tested).
The bio-activity of Human Activin A,Tag Free, low endotoxin was determined by dose-dependent inhibition of the proliferation of MPC-11 cells. The EC50 for this effect is typically ≤ 9.5ng/ml (Routinely tested).
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Citations
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Invasion of ovarian cancer cells is induced by PITX2-mediated activation of TGF-β and Activin-A
Authors: Basu M, et al.
Journal: Mol Cancer 2015
Application: Cell Culture
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BackgroundActivin and inhibin are two closely related protein complexes that have almost directly opposite biological effects. Activin enhances FSH biosynthesis and secretion, and participates in the regulation of the menstrual cycle. Many other functions have been found to be exerted by activin, including roles in cell proliferation, differentiation, apoptosis, metabolism, homeostasis, immune response, wound repair, and endocrine function. Conversely inhibin down regulates FSH synthesis and inhibits FSH secretion.Activins are nonglycosylated homodimers or heterodimers of various β subunits (βA, βB, βC, and βE in mammals), while Inhibins are heterodimers of a unique α subunit and one of the β subunits. Activin A is a widely expressed homodimer of two βA chains. The βA subunit can also heterodimerize with a βB or βC subunit to form Activin AB and Activin AC, respectively. The 14 kDa mature human βA chain shares 100% amino acid sequence identity with bovine, feline, mouse, porcine, and rat βA.
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References
- (1) Chen YG., et al., 2006, Exp. Biol. Med. (Maywood) 231 (5): 534–44.
- (2) Sulyok S, et al., 2004, Mol. Cell. Endocrinol. 225 (1–2): 127–32.
- (3) van Zonneveld P, et al., 2003, Hum Reprod 18 (3): 495–501.
- (4) Harrison, C.A. et al., 2005, Trends Endocrinol. Metab. 16:73.
- (5) Thompson, T.B. et al., 2004, Mol. Cell. Endocrinol. 225:9.