BMPR1A/ALK-3 Protein, Human (HEK293, His)

BMPR1A/ALK-3 protein (ACVRLK3) is the receptor bone morphogenetic protein (BMP) type I receptors, widely expressed in tissues^[1]. BMPR1A/ALK-3 protein mediates iron metabolism factor hepcidin expression, interacts with GDF5/6 to regulate chondrocyte differentiation and adipogenesis^[2][3]. BMPR1A-ID2/ZEB1-TGFBR2 signaling axis could serve as a potentia target for pulmonary arterial hypertension (PAH) and other endothelial-mesenchymal transition (EndoMT)-related vascular disorders^[4]. Human BMPR1A/ALK-3 has a full length of 532 a.a., with a motif (107-109 a.a.) mediating specificity for BMP ligand. BMPR1A/ALK-3 Protein, Human (HEK293, His) is produced in HEK293 cells, with a C-terminal His-tags.

ALK-3 (BMPR1A; ACVRLK3) is the receptor bone morphogenetic protein (BMP) type I receptors, for BMP2, BMP4, GDF5 and GDF6. Among BMP type I receptors, ALK-2 and 3 are widely expressedin tissues, while ALK-1 is more selectively expressed in endothelial cells (ECs)^[1]. Hepcidin, the main regulator of iron metabolism, is synthesized and released by hepatocytes in response to increased body iron concentration and inflammation. BMP/ALK/SMAD pathway controls hepcidin expression, while BMP type I receptors ALK-2 and ALK-3 are responsible for iron-dependent hepcidin upregulation and basal hepcidin expression, respectively, to avoid low hepcidin which causes iron overload or high hepcidin levels which induce iron-restricted erythropoiesis^[2]. ALK-3 positively regulates chondrocyte differentiation through GDF5 interaction and mediates induction of adipogenesis by GDF6^[3]. ALK-3 protein shows function for the initiation of chondrogenesis, for regulating differentiation along the chondrogenic lineage, and for endochondral bone formation^[5]. Components of BMP signaling have been implicated in both pathogenesis of pulmonary arterial hypertension (PAH) and endothelial-mesenchymal transition (EndoMT), and BMPR1A is key to maintain endothelial identity and to prevent excessive EndoMT. BMPR1A-ID2/ZEB1-TGFBR2 signaling axis could serve as a potential novel target for PAH and other EndoMT-related vascular disorders^[4].

ALK3-Flag (2 ng/mL; 48 h) synergizes with HFE, results phospho-Smad1/5/8, HA increasing and stimulates hepcidin expression in transfected Hep3B cells^[6].

Human

HEK293

C-His

P36894 (Q24-R152)

657  [NCBI]

28-33 kDa

Greater than 85% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.

• [1]. Yang P, et al. The role of bone morphogenetic protein signaling in vascular calcification. Bone. 2020 Dec;141:115542.  [Content Brief]

  [2]. Traeger L, et al. HFE and ALK3 act in the same signaling pathway. Free Radic Biol Med. 2020 Nov 20;160:501-505.  [Content Brief]

  [3]. Miyazawa K, et al. Regulation of TGF-β Family Signaling by Inhibitory Smads. Cold Spring Harb Perspect Biol. 2017 Mar 1;9(3):a022095.  [Content Brief]

  [4]. Lee HW, et al. BMPR1A Promotes ID2-ZEB1 Interaction to Suppress Excessive Endothelial to Mesenchymal Transition. Cardiovasc Res. 2022 Sep 27:cvac159.  [Content Brief]

  [5]. Jing J, et al. Bmpr1a Signaling in Cartilage Development and Endochondral Bone Formation. Vitam Horm. 2015;99:273-91.  [Content Brief]

  [6]. Wu XG, et al. HFE interacts with the BMP type I receptor ALK3 to regulate hepcidin expression. Blood. 2014 Aug 21;124(8):1335-43.  [Content Brief]