Recombinant human activin E PLUS™ Avi-tag (biotinylated) protein (Qk136)

Product background

Activin E is a member of the TGF-beta superfamily, a group of proteins that play a key role in regulating cell growth, differentiation, and inflammation. Like other activins, activin E is a dimeric protein, consisting of two subunits connected by a disulfide bond. These subunits are produced from precursor molecules that undergo cleavage to form the active protein. Activin E has a characteristic cystine knot motif, common in the TGF-beta family and crucial for its function [1].

Activin E was initially identified for its role in reproductive biology but has since been implicated in broader biological processes, including metabolic regulation. It is primarily expressed in the liver and has been implicated in the regulation of glucose and lipid metabolism [2,3]. It has been detected in adipose tissue and the gastrointestinal tract.

Activin E signals through the ALK7 receptor in liver and adipose tissues, specifically using the ActRIIA and ActRIIB receptors, while resisting antagonists like follistatin [1]. Receptor binding activates the SMAD2/3 pathway in adipocytes, linking it to adipose tissue regulation and positioning it as a potential target for treating obesity and metabolic disorders by enhancing insulin sensitivity and thermogenesis. Blocking activin E may also serve as an anti-diabetic strategy by improving adipose energy metabolism [1].

Activin E shares functions with other activins, such as enhancing follicle-stimulating hormone (FSH) binding in the ovarian follicle, promoting spermatogenesis, and participating in androgen synthesis. These varied roles make it a protein of interest for drug discovery across multiple fields, including endocrinology, metabolism, and inflammation. Understanding the activin E signaling pathways and biological effects could open new avenues for therapeutic interventions in obesity, diabetes, and other metabolic diseases [2].

Avi-tag is a 15 amino acid peptide (GLNDIFEAQKIEWHE) which can be added to proteins to allow efficient bio biotinylation using BirA, an E. coli biotin ligase which catalyzes biotin attachment to the Avi-tag sequence [4]. Biotinylation is one of the most commonly used protein labeling methods for easy detection, immobilization, and purification of proteins for many experimental protocols.