Recombinant Mouse Inhibin beta A Protein (His Tag)

Name: Recombinant Mouse Inhibin beta A Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-2966
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Mouse
Accession	NP_032406.1
Background	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 beta subunits, betaA betaA (activin A), betaB betaB (activin B), or betaA betaB (activin AB). Inhibin is composed of an alpha and one of two beta subunits, betaA (inhibin A) or betaB (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.
Description	A DNA sequence encoding the pro form of mouse INHBA (NP_032406.1) (Met 1-Ser 424) was expressed, with a C-terminal His tag.
Source	HEK293
Predicted N Terminal	Ser 21
AA Sequence	Met 1-Ser 424
Molecular Weight	The secreted recombinant mouse INHBA comprises 415 a.a. 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.
Purity	>88% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	1. Measured by its binding ability in a functional ELISA.2. Immobilized human ACVR2B at 10 ug/mL (100 ul/well) can bind biotinylated mouse INHBA-His, The EC50 of biotinylated mouse INHBA-His is 0.161 ug/mL.3. Immobilized mouse INHBA-his at 10 ug/mL (100 ul/well) can bind human Follistatin Protein, The EC50 of human Follistatin Protein is 0.39 ug/mL.
Formulation	Lyophilized from sterile PBS, pH 7.4.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.