protein

Recombinant Human Activin INHBA protein, low endotoxin

INHBA-525H

Recombinant Human Activin INHBA protein, low endotoxin

Creative Biomart

INHBA

inhibin, beta A

EDF; FRP; INHBA

Recombinant Human Activin A/INHBA Protein, Native, ActiveMax (rhActivin A) Gly311-Ser426 (Accession #AAH07858.1 ) was expressed in human 293 cells (HEK293).

Recombinant Human Activin A/INHBA Protein, Native, ActiveMax (rhActivin A) Gly311-Ser426 (Accession #AAH07858.1 ) was expressed in human 293 cells (HEK293).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. Activin is produced in the gonads, pituitary gland, placenta, and other organs. The bioactivity of Activin A is regulated by a variety of mechanisms.[4] In the ovarian follicle, activin increases FSH binding and FSH-induced aromatization; 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 especially kidney. Activin A increased the expression level of type-I collagen suggesting that activin A acts as a potent activator of fibroblasts; Lack of activin during development results in neural developmental defects.

HEK293

Lyophilized from 0.22 μm filtered solution in 0.1M acetic acid, pH2.0. Normally Mannitol or Trehalose are added as protectants before lyophilization.

>95% as determined by SDS-PAGE of reduced (+) and non-reduced (-) rhActivin A.

Avoid repeated freeze-thaw cycles. No activity loss was observed after storage at: 4-8 centigrade for 1 year in lyophilized state, 4-8 centigrade for 1 month under sterile conditions after reconstitution, -20 centigrade to -70 centigrade for 3 months under sterile conditions after reconstitution.

P08476