Bone Morphogenetic Proteins, BMPs

Expression system: E. coli
Length: 293-408 (mutation), Full Length of Mature Protein
Activity: Cell Activity

BMP-2 Protein, Human, Mouse, Rat, Rhesus, Canine, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 39.5 kDa and the accession number is C8C060.

BMP-2 Protein, Human, Mouse, Rat, Rhesus, Canine, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 13 kDa and the accession number is P12643.

Expression system: E. coli
Length: 283-396, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 382-513, Partial
Activity: Not Tested

BMP-4 Protein, Mouse, Recombinant (rFc) is expressed in HEK293 mammalian cells with rFc tag. The predicted molecular weight is 40.6 kDa and the accession number is P21275.

Bone Morphogenetic Protein 5 (BMP-5) is a member of the structurally and functionally related bone morphogenetic proteins (BMPs) which constitute a novel subfamily of the transforming growth factor β (TGF-β) superfamily. In agreement with a possible role in the control of cell death, BMP-5 exhibited a regulated pattern of expression in the interdigital tissue. Transcripts of BMP-5 and BMP-5 protein were abundant within the cytoplasm of the fragmenting apoptotic interdigital cells in a way suggesting that delivery of BMPs into the tissue is potentiated during apoptosis. Gain-of-function experiments demonstrated that BMP-5 has the same effect as other interdigital BMPs inducing apoptosis in the undifferentiated mesoderm and growth in the prechondrogenic mesenchyme. BMP-5 is a member of the 60A subgroup of BMPs, other members of which have been shown to stimulate dendritic growth in central and peripheral neurons. The signaling pathway that mediates the dendrite-promoting activity of BMP-5 may involve binding to BMPR-IA and activation of Smad-1, and relative levels of BMP antagonists such as noggin and follistatin may modulate BMP-5 signaling. Since BMP-5 is expressed at relatively high levels not only in the developing but also the adult nervous system, these findings suggest the possibility that BMP-5 regulates dendritic morphology not only in the developing but also the adult nervous system. BMP-5 may play important roles not only in myocardial differentiation but also in the formation and maintenance of endocardial cushion tissue. Additionally, a high expression level of BMP-5 has been detected in certain tumors of mesenchymal origin.

Expression system: HEK293 Cells
Length: 32-143, Partial
Activity: Not Tested

Expression system: E. coli
Length: 293-408, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 32-143, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 293-431, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 299-407, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli Length: 283-396, Full Length of Mature Protein Activity: Cell Activity

Expression system: E. coli
Length: 294-409, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 359-468, Full Length of Mature Protein
Activity: Not Tested

BMP-2 Protein, Danio rerio (zebrafish), Recombinant is expressed in E. coli expression system. The predicted molecular weight is 13.2 kDa and the accession number is B3DI86.

BMP-15 Protein, Sheep, Recombinant (His & Myc) is expressed in E. coli. The accession number is Q9MZE2.

Expression system: E. coli
Length: 268-392, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 293-431, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 293-431, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 32-143, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 316-431, Partial
Activity: Cell Activity

BMP-3b GDF-10 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Studies in mice suggest that the protein encoded by this gene plays a role in skeletal morphogenesis. In the bone morphogenetic cascade, cartilage differentiation, hypertrophy, and cell death are followed by bone formation. In this regard, all BMPs are cartilage morphogenetic proteins since cartilage is formed first. An overexpression or dysregulation of BMP pathways may lead to heterotopic bone formation or fibrodysplasia ossificans progressiva (FOP). BMPs have been implicated in FOP. The pioneering work of Sakou has implicated BMP-3b GDF-10 in ossification of the posterior longitudinal ligament of the spine in Japanese patients. The BMP-specific antagonists such as noggin or chordin might be used therapeutically in clinical conditions with pathologically excessive bone formation. The osteoinductive capacity of BMPs has been demonstrated in preclinical models, and the efficacy of BMPs for the treatment of orthopaedic patients is now being evaluated in clinical trials. It was suggested that further progress in the clinical application of the BMP-3b GDF-10 will depend upon the development of carriers with ideal release kinetics for the delivery of the BMPs.

Expression system: E. coli
Length: 363-472, Full Length of Mature Protein
Activity: Not Tested