|Datasheet||Specific References||Reviews||Related Products||Protocols|
|A DNA sequence encoding the pro form of mouse INHBA (NP_032406.1) (Met 1-Ser 424) was expressed, with a C-terminal polyhistidine tag.|
|In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.|
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
|> 88 % as determined by SDS-PAGE|
|1. Measured by its binding ability in a functional ELISA.|
2. Immobilized human ACVR2B (Cat:10229-H02H) at 10 μg/mL (100 μl/well) can bind biotinylated mouse INHBA-His (Cat:50659-M08H), The EC50 of biotinylated mouse INHBA-His (Cat:50659-M08H) is 0.161 μg/mL.
3. Immobilized mouse INHBA-his at 10 μg/mL (100 μl/well) can bind human Follistatin Protein, The EC50 of human Follistatin Protein is 0.39 μg/mL.
|< 1.0 EU per μg of the protein as determined by the LAL method|
|Samples are stable for up to twelve months from date of receipt at -70℃|
|The secreted recombinant mouse INHBA comprises 415 amino acids and has a calculated molecular mass of 46.5 kDa. As a result of glycosylation, the apparent molecular mass of rmINHBA is approximately 18 & 43 kDa corresponding to the mature inhibin beta A chain and the pro domain respectively in SDS-PAGE under reducing conditions.|
|Lyophilized from sterile PBS, pH 7.4|
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
|Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.|
|A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.|
Activin and inhibin are two closely related protein complexes that have almost directly opposite biological effects. The activin and inhibin protein complexes are both dimeric in structure, and, in each complex, the two monomers are linked to one another by a single disulfide bond. Activin is composed of two β subunits, βA βA (activin A), βB βB (activin B), or βA βB (activin AB). Inhibin is composed of an alpha and one of two β subunits, βA (inhibin A) or βB (inhibin B). Activins are produced in many cell types and organs, such as gonads, pituitary gland, and placenta. In the ovarian follicle, activin increases FSH binding and FSH-induced aromatization. It participates in androgen synthesis enhancing LH action in the ovary and testis. In the male, activin enhances spermatogenesis. In addition, Activin plays a role in wound repair and skin morphogenesis. Activin is strongly expressed in wounded skin, and overexpression of activin in epidermis of transgenic mice improves wound healing and enhances scar formation. Activin also regulates the morphogenesis of branching organs such as the prostate, lung, and kidney. There is also evidence showed that lack of activin during development results in neural developmental defects.