BMPRIB/ALK-6 Protein, Human (HEK293, Fc)

BMPR1B/ALK-6 protein is a type I member of the bone morphogenetic protein (BMP) receptor family of transmembrane serine/threonine kinases^[1]. BMPR1B/ALK-6 is the receptor for BMP-7/OP-1 and GDF-5, positively regulates chondrocyte differentiation through GDF-5 interaction^[2][3]. BMPR1B/ALK-6 also involves in SCUBE3/BMP-2/BMP-4 signals regulation, controlling growth, morphogenesis, and bone and teeth development^[4]. ALK-6/GDF-9/BMP-15 signals is essential in prolificacy of goat^[5]. The human BMPR1B/ALK-6 protein contains 502 amino acids and a transmembrane domain (127-148 a.a.). BMPRIB/ALK-6 Protein, Human (HEK293, Fc) is produced by HEK293 cells (K14-R126) with a C-terminal hFc-tag.

BMPRIB/ALK-6, also known as CDw293 (cluster of differentiation w293), is a member of the bone morphogenetic protein (BMP) receptor family of transmembrane serine/threonine kinases. BMPs are involved in endochondral bone formation and embryogenesis, transducing signals through the formation of heteromeric complexes of 2 types BMP receptors: type I receptors (50-55 kD) and type II receptors (70-80 kD). Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators^[1]. ALK-6 is the receptor for BMP-7/OP-1 and GDF-5, positively regulates chondrocyte differentiation through GDF-5 interaction^[2][3]. ALK-6 signaling is also controlled by SCUBE3, a BMP-2/BMP-4 co-receptor, recruits the BMP receptor complexes into raft microdomains, and positively modulates signaling possibly by augmenting the specific interactions between BMPs and BMP type I receptors^[3]. ALK-6 involves in controlling growth, morphogenesis, and bone and teeth development through modulation of BMP signaling, is essential for chondrogenesis in vivo, while BMPR1A/ALK-3 and ALK-6 have overlapping functions during early chondrogenesis^[4]. ALK-6/GDF-9/BMP-15 signals play a key role in prolificacy. ALK-6 and GDF-9 are widely expressed in 20 tissues with highest in ovary, while BMP-15 gene was expressed exclusively in ovary and pituitary^[5]. The sequences of ALK-6 are highly conserved among different species, and the sequence of human shares a high similarity with rat (98.21%) and mouse (98.21%), respectively.

Human

HEK293

C-hFc

O00238 (K14-R126)

658  [NCBI]

Extracellular Domain

KKEDGESTAPTPRPKVLRCKCHHHCPEDSVNNICSTDGYCFTMIEEDDSGLPVVTSGCLGLEGSDFQCRDTPIPHQRRSIECCTERNECNKDLHPTLPPLKNRDFVDGPIHHR

≥ 90%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.

• [1]. /biology-dictionary/baf3-cell.html  [Content Brief]

  [2]. ten Dijke P, et al. Signaling via hetero-oligomeric complexes of type I and type II serine/threonine kinase receptors. Curr Opin Cell Biol. 1996 Apr;8(2):139-45.  [Content Brief]

  [3]. Xu H, et al. [BMP7 signaling via BMPR1A, BMPR1B inhibits the proliferation of lung large carcinoma NCI-H460 cell]. Zhongguo Fei Ai Za Zhi. 2010 Jul;13(7):659-64. Chinese.  [Content Brief]

  [4]. Demirhan O, et al. A homozygous BMPR1B mutation causes a new subtype of acromesomelic chondrodysplasia with genital anomalies. J Med Genet. 2005 Apr;42(4):314-7.  [Content Brief]

  [5]. Lin YC, et al. SCUBE3 loss-of-function causes a recognizable recessive developmental disorder due to defective bone morphogenetic protein signaling. Am J Hum Genet. 2021 Jan 7;108(1):115-133.  [Content Brief]

  [6]. Yang CX, et al. Cloning and mRNA expression levels of GDF9, BMP15, and BMPR1B genes in prolific and non-prolific goat breeds. Mol Reprod Dev. 2012 Jan;79(1):2.  [Content Brief]

  [7]. Yoon BS, et al. Bmpr1a and Bmpr1b have overlapping functions and are essential for chondrogenesis in vivo. Proc Natl Acad Sci U S A. 2005 Apr 5;102(14):5062-7.  [Content Brief]