Recombinant Human Soluble BMP Receptor Type-1A; Bone morphogenetic protein receptor type-1A; Activin receptor-like kinase 3; CD292

For Research Use Only. Not for use in diagnostic procedures.

Chromosome: 10; NC_000010.11 (86756639..86925188). Location: 10q22.3

Insect Cells

> 90% by SDS-PAGE & silver stain

Lyophilized

Lyophilized samples are stable for greater than six months at -20 degree C to -70 degree C. Reconstituted sBMPR-1A should be stored in working aliquots at -20 degree C.

Manufactured in an ISO 9001:2008 Certified Laboratory.

Small volumes of BMP receptor-1A recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

The extracellular domain of human BMPR-IA was fused with a carboxy-terminal 6X histidine-tag. The monomeric glycoprotein was expressed in baculovirus infected insect cells. Cellular responses to bone morphogenetic proteins (BMPs) have been shown to be mediated by the formation of hetero-oligomeric complexes of the type I and type II serine/threonine kinase receptors. BMP receptor 1A (BMPR-1A), also known as activin receptor-like kinase (ALK)-3, is a one of seven known type I serine/threonine kinases that are required for the signal transduction of TGF-b family cytokines. In contrast to the TGF-b receptor system in which the type I receptor does not bind TGF-b in the absence of the type II receptor, type I receptors involved in BMP signaling (including BMPR-IA, BMPR-IB/ALK-6, and ActR-I/ALK-2) can independently bind the various BMP family proteins in the absence of type II receptors. Recombinant soluble BMPR-IA binds BMP-2 and -4 with high-affinity in solution and is a potent BMP-2/4 antagonist in vitro. BMPR-IA is ubiquitously expressed during embryogenesis. In ***** tissues, BMPR-IA mRNA is also widely distributed; with the highest expression levels found in skeletal muscle. The extracellular domain of BMPR-IA shares little amino acid sequence identity with the other mammalian ALK type I receptor kinases, but the cysteine residues are conserved. Human and mouse BMPR-IA are highly conserved and share 98% sequence identity.

Soluble Receptors

BMP-2 BioLISA using recombinant human soluble BMPR-IA for capturing and recombinant human BMP-2 as standard. A rabbit anti-human BMP-2 antibody in combination with an goat anti-rabbit Biotin antibody was used for detection.

C2C12 cells were plated with 1500c/well in a 96well plate. Cells were stimulated with O.5).lg/ml BMP-2 and increasing amounts of recombinant human soluble BMPR-IA were added. The cells were incubated at 37 degree C, 5% C02 for 4 days.

23 kDa (Monomer)

bone morphogenetic protein receptor, type IA

bone morphogenetic protein receptor type-1A; ALK-3; BMPR-1A; BMP type-1A receptor; activin receptor-like kinase 3; activin A receptor, type II-like kinase 3; serine/threonine-protein kinase receptor R5

Bone morphogenetic protein receptor type-1A

ACVRLK3; ALK3; BMP type-1A receptor; BMPR-1A; ALK-3; SKR5??[Similar Products]

BMR1A_HUMAN

The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the activin receptors, ACVR1 and ACVR2. The ligands of these receptors are members of the TGF-beta superfamily. TGF-betas and activins transduce their signals through the formation of heteromeric complexes with 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding. [provided by RefSeq, Jul 2008]

Function: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP-2 and BMP-4.

Catalytic activity: ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.

Cofactor: Magnesium or manganese

By similarity.

Subcellular location: Membrane; Single-pass type I membrane protein.

Tissue specificity: Highly expressed in skeletal muscle.

Involvement in disease: Juvenile polyposis syndrome (JPS) [MIM:174900]: Autosomal dominant gastrointestinal hamartomatous polyposis syndrome in which patients are at risk for developing gastrointestinal cancers. The lesions are typified by a smooth histological appearance, predominant stroma, cystic spaces and lack of a smooth muscle core. Multiple juvenile polyps usually occur in a number of Mendelian disorders. Sometimes, these polyps occur without associated features as in JPS; here, polyps tend to occur in the large bowel and are associated with an increased risk of colon and other gastrointestinal cancers.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10Polyposis syndrome, mixed hereditary 2 (HMPS2) [MIM:610069]: A disease is characterized by atypical juvenile polyps, colonic adenomas, and colorectal carcinomas.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6A microdeletion of chromosome 10q23 involving BMPR1A and PTEN is a cause of chromosome 10q23 deletion syndrome, which shows overlapping features of the following three disorders: Bannayan-Zonana syndrome, Cowden disease and juvenile polyposis syndrome. Ref.6

Sequence similarities: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.Contains 1 GS domain.Contains 1 protein kinase domain.

1. Wu MY and CS Hill Dev Cell 16:329, 2009 2. Nickel J et al, Cytokine Growth Factor Rev 20:367, 2009 3. de Caestecker M, Cytokine Growth Factor Rev 15:1, 2004 4. Schmal H et al, Cytotherapy 14(7):868-76, 2012 5. Liu R etal, BMC Musculoskelet Disord 15;10:51, 2009

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