ALK7 Extracellular Domain (human, recombinant)

Description

Activin receptor-like kinase 7 (ALK7) is a serine/threonine kinase and member of the type I TGF-β receptor superfamily that is encoded by ACVR1C in humans.1,2 It is composed of an extracellular ligand-binding domain, a single transmembrane domain, an intracellular serine/threonine kinase domain, and a cytoplasmic serine/threonine-rich region.3,4 Alternative splicing of the ACVR1C pre-mRNA produces a truncated isoform, tALK7, which lacks the first 50 amino acids of the full-length protein, and two soluble isoforms, sALK7a and sALK7b, which lack the transmembrane, kinase, and cytoplasmic domains.5 ALK7 is highly expressed in neuronal tissues, as well as intestinal tissues, pancreatic islets, and adipocytes.6,7,2 It heterodimerizes with activin receptor type 2A (ACTRIIA) or ACTRIIB, and upon ligand activation by activin A, activin B, activin AB, or Nodal, induces phosphorylation of SMAD2 and SMAD3 to regulate gene expression.6,3 ALK7-mediated signaling has roles in insulin secretion and apoptosis, as well as roles in the suppression of tumorigenesis and metastasis.8,9 ACVR1C SNPs are associated with increased risk of metabolic syndrome in women, and adipose tissue ACVR1C expression is decreased in obese individuals.2,7 Cayman’s ALK7 Extracellular Domain (human, recombinant) protein is a disulfide-linked homodimer. The reduced monomer, composed of ALK7 (22-113) fused to human IgG1 Fc at its C-terminus, consists of 330 amino acids, has a calculated molecular weight of 36.6 kDa, and a predicted N-terminus of Leu22 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is greater than 36.6 kDa due to glycosylation.WARNING This product is not for human or veterinary use.