Bone morphogenetic protein 6 Recombinant Protein | VGR6 recombinant protein

Recombinant Human Bone morphogenetic protein 6

Cat. Num. AAA1265252

• Gene Names: BMP6; VGR; VGR1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Bone morphogenetic protein 6; Recombinant Human Bone morphogenetic protein 6; VG-1-related protein; VG-1-R; VGR-1; VGR6 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 382-513aa; Partial
• Sequence: QQSRNRSTQSQDVARVSSASDYNSSELKTACRKHELYVSFQDLGWQDWIIAPKGYAANYCDGECSFPLNAHMNATNHAIVQTLVHLMNPEYVPKPCCAPTKLNAISVLYFDDNSNVILKKYRNMVVRACGCH
• Sequence Length: 513

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for VGR6 recombinant protein

Induces cartilage and bone formation.

Product Categories/Family for VGR6 recombinant protein

Developmental Biology

References

Identification of transforming growth factor beta family members present in bone-inductive protein purified from bovine bone.Celeste A.J., Iannazzi J.A., Taylor R.C., Hewick R.M., Rosen V., Wang E.A., Wozney J.M.Proc. Natl. Acad. Sci. U.S.A. 87:9843-9847(1990) The DNA sequence and analysis of human chromosome 6.Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.Nature 425:805-811(2003) The consensus coding sequences of human breast and colorectal cancers.Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.Science 314:268-274(2006) BMP-3 and BMP-6 structures illuminate the nature of binding specificity with receptors.Allendorph G.P., Isaacs M.J., Kawakami Y., Izpisua Belmonte J.C., Choe S.Biochemistry 46:12238-12247(2007)

NCBI and Uniprot Product Information

• NCBI GI #: 4502425
• NCBI GeneID: 654
• NCBI Accession #: NP_001709.1
• NCBI GenBank Nucleotide #: NM_001718.4
• UniProt Accession #: P22004; Q5TCP3
• Molecular Weight: 18.9 kDa
• NCBI Official Full Name: bone morphogenetic protein 6 preproprotein
• NCBI Official Synonym Full Names: bone morphogenetic protein 6
• NCBI Official Symbol: BMP6
• NCBI Official Synonym Symbols: VGR; VGR1
• NCBI Protein Information: bone morphogenetic protein 6
• UniProt Protein Name: Bone morphogenetic protein 6
• Protein Family: Bone morphogenetic protein
• UniProt Gene Name: BMP6
• UniProt Synonym Gene Names: VGR; BMP-6; VG-1-R; VGR-1
• UniProt Entry Name: BMP6_HUMAN

NCBI Description

The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity. [provided by RefSeq, Jul 2008]

Uniprot Description

BMP6: Induces cartilage and bone formation. Belongs to the TGF-beta family.

Protein type: Secreted, signal peptide; Secreted

Chromosomal Location of Human Ortholog: 6p24-p23

Cellular Component: cytoplasm; extracellular space

Molecular Function: cytokine activity; growth factor activity; protein heterodimerization activity; transforming growth factor beta receptor binding

Biological Process: BMP signaling pathway; cartilage development; cellular iron ion homeostasis; endochondral ossification; eye development; growth; immune response; inflammatory response; kidney development; male genitalia development; negative regulation of transcription from RNA polymerase II promoter; osteoblast differentiation; positive regulation of aldosterone biosynthetic process; positive regulation of bone mineralization; positive regulation of chondrocyte differentiation; positive regulation of endothelial cell differentiation; positive regulation of endothelial cell proliferation; positive regulation of epithelial cell proliferation; positive regulation of lipopolysaccharide-mediated signaling pathway; positive regulation of neuron differentiation; positive regulation of osteoblast differentiation; positive regulation of protein secretion; positive regulation of transcription from RNA polymerase II promoter; regulation of apoptosis; regulation of MAPKKK cascade; response to activity; response to glucocorticoid stimulus; response to magnesium ion; response to retinoic acid; skeletal development