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Rhesus ACVR1B / ALK-4 Protein (Fc Tag)

ACVR1B

Catalog Number P90066-C02H
Organism Species Rhesus
Host Human Cells
Synonyms ACVR1B
Molecular Weight The recombinant rhesus ACVR1B comprises 341 amino acids and has a calculated molecular mass of 38.2 KDa.
predicted N Arg 27
SDS-PAGE
Purity > 85 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the rhesus ACVR1B (NP_001252559.1) (Met1-Glu126) was expressed, fused with the Fc region of human IgG1 at the C-terminus.
Bio-activity
Research Area Cancer |Oncoprotein & suppressor & biomarker |Oncoprotein |Growth Factor & Receptor |Transforming Growth Factor Beta (TGF-beta) Superfamily |TGF-beta Superfamily Receptors |
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background ALK-4 (Activin Receptor-Like Kinase 4) or ACVR1B (Activin A Receptor, type 1B), belongs to the protein kinase superfamily, TKL Ser/Thr protein kinase family, and TGFB receptor subfamily. ALK-4/ACVR1B acts as a transducer of activin or activin like ligands signals. Activin binds to either ACVR2A or ACVR2B and then forms a complex with ACVR1B. The known type II activin receptors include ActRII and ActRIIB, while the main type I activin receptor in mammalian cells is ALK-4 (ActRIB). In the presence of activin, type II and type I receptors form complexes whereby the type II receptors activate ALK-4 through phosphorylation. The activated ALK-4, in turn, transduces signals downstream by phosphorylation of its effectors, such as Smads, to regulate gene expression and affect cellular phenotype. ALK-4/ACVR1B is an important regulator of vertebrate development, with roles in mesoderm induction, primitive streak formation, gastrulation, dorsoanterior patterning, and left-right axis determination.
Reference
  • Chen Y, et al. (2005) Developmental analysis of activin-like kinase receptor-4 (ALK4) expression in Xenopus laevis. 232(2): 393-8.
  • J. Massagu. (1998) TGF- SIGNAL TRANSDUCTION. Annual Review of Biochemistry. 67: 753-91.