Human Latent Activin A / INHBA Protein, His Tag | ACA-H424x-1mg

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SKU:
716-ACA-H424x-1mg
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IN STOCK
Size:
1 mg
€3,832.00
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Description

Human Latent Activin A / INHBA Protein, His Tag | ACA-H424x-1mg| Gentaur Distribution US, UK & Europe

Activin 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.

Source: Human Latent Activin A, His Tag (ACA-H424x) is expressed from human 293 cells (HEK293). It contains AA Ser 21 - Ser 426 (Accession # AAH07858.1).

Format: Powder.

Tag: N-6×His.

Expression System: HEK293.

Expression Region: Ser 21 - Ser 426.

Conjugate: Unconjugated.

Molecular Weight: 13.0 kDa (mature) and 32.0 kDa (pro).

Characteristics: This protein carries a polyhistidine tag at the N-terminus. The protein has a calculated MW of 13.0 kDa (mature) and 32.0 kDa (pro). As a result of glycosylation and Interchain disulfide bond, the protein migrates as 15 kDa (mature) and 43-48 kDa (pro) under reducing (R) condition, and 27 kDa (mature), 43-48 kDa (pro) and 60 kDa (pro & mature) under non-reducing (NR) condition (SDS-PAGE).

Purity: 95%.

Buffer: PBS, pH7.4.

Storage Conditions: -20℃.

Shipping Conditions: RT

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