ActiveMax® Human Activin A / INHBA Protein, Tag Free, low endotoxin

Source : 

ActiveMax® Human 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).

 

Molecule : Activin A

 

Synonyms : Activin A,INHBA

 

Format : Powder

 

Category : ActiveMax® Cytokines

 

Accession : AAH07858.1

 

Storage : -20℃

 

Shipping condition : Powder,RT

 

Molecular Weight : 13.0 kDa

 

Characteristics :

This protein carries no "tag". The protein has a calculated MW of 13.0 kDa. the protein migrates as 14 kDa under reducing (R) condition, and 27 kDa under non-reducing (NR) condition (SDS-PAGE).

 

Endotoxin Level : Less than 0.1 EU per μg by the LAL method.

 

Buffer : 0.056% TFA in 60% ACN

 

Description :

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.

 

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.