Human Bone Morphogenetic protein-7 Recombinant

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Human Bone Morphogenetic protein-7 Recombinant

$70.00$3,500.00


accession P18075


Source Optimized DNA sequence encoding Human Bone Morphogenetic protein-7 mature chain was expressed in E.coli.
Molecular weight Native humanBMP-7 isgenerated by the proteolytic removal of the signal peptide and propeptide, the molecule has a calculated molecular mass of approximately17 kDa. Recombinant BMP-7 is a disulfide-linked monomerprotein consisting of amino acid residue subunits,and migrates as an approximately kDa protein under under reducing conditions in SDS-PAGE.
Purity >95%, as determined by SDS-PAGE and HPLC
Biological Activity Not Available
Protein Sequence MHVRSLRAAA PHSFVALWAP LFLLRSALAD FSLDNEVHSS FIHRRLRSQE RREMQREILS ILGLPHRPRP HLQGKHNSAP MFMLDLYNAM AVEEGGGPGG QGFSYPYKAV FSTQGPPLAS LQDSHFLTDA DMVMSFVNLV EHDKEFFHPR YHHREFRFDL SKIPEGEAVT AAEFRIYKDY IRERFDNETF RISVYQVLQE HLGRESDLFL LDSRTLWASE EGWLVFDITA TSNHWVVNPR HNLGLQLSVE TLDGQSINPK LAGLIGRHGP QNKQPFMVAF FKATEVHFRS IRSTGSKQRS QNRSKTPKNQ EALRMANVAE NSSSDQRQAC KKHELYVSFR DLGWQDWIIA PEGYAAYYCE GECAFPLNSY MNATNHAIVQ TLVHFINPET VPKPCCAPTQ LNAISVLYFD DSSNVILKKY RNMVVRACGC H
Endotoxin Endotoxin content was assayed using a LAL gel clot method. Endotoxin level was found to be less than.1 ng/µg(1EU/µg).
Presentation Recombinant BMP-7 was lyophilized from a.2 μm filtered PBS solution pH.4.
Reconstitution A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than.1 mg/mL. This solution can then be diluted into other buffers.
Storage The lyophilized protein is stable for at least years from date of receipt at -20° C. Upon reconstitution, this cytokine can be stored in working aliquots at° -° C for one month, or at -20° C for six months, with a carrier protein without detectable loss of activity. Avoid repeated freeze/thaw cycles.
Usage This cytokine product is for research purposes only.It may not be used for therapeutics or diagnostic purposes.


Biological Process Chondrogenesis
Biological Process Differentiation
Biological Process Osteogenesis
Molecular function Cytokine
Molecular function Developmental-protein
Molecular function Growth-factor

Methods

rBMP7 rescues Ngn2 mRNA expression in cultured E14.5 Bmp7-deficient cortical cells.

recombinant human BMP7
  • RT-PCR analysis of serial 4-fold cDNA dilutions (1, ¼, 1/16, 1/64, 1/256 cDNA input) for Ngn2 and Pax6 in isolated E14.5 wild-type (wt) or Bmp7

Cell culture and immunoblotting

  • Cranial fibroblasts were isolated from E14.5 C57BL/6 mouse embryos.
  • The mid-facial region was dissected from embryo heads and incubated in 0.05% trypsin-EDTA solution for 1 h at 37°C, after which the tissue was triturated by repeated aspiration.
  • Cells were centrifuged, resuspended in Dulbecco's Minimal Essential Medium (DMEM) containing 10% fetal calf serum (FCS), plated onto 10 cm cell culture dishes, and incubated at 37°C with 6% CO2.
  • At confluency, cranial fibroblasts were passaged by trypsinization.
  • Bmp7 stimulation experiments were performed in 24-well dishes with cells from the second passage.
  • Fibroblasts were first starved for 24 h in DMEM/0.3% FCS, before the medium was changed to DMEM/0.3% FCS containing human recombinant Bmp7 (, , 0, 10, 20, 50, and 100 ng/ml, respectively).
  • For positive controls, wells were incubated with DMEM/10% FCS.
  • Cell supernatant was collected from individual wells after 24 h, run on SDS-7.5% polyacrylamide gels under reducing conditions, and proteins were transferred to nitrocellulose.
  • Blots were briefly…
  • Cranial fibroblasts were isolated from E14.5 C57BL/6 mouse embryos.
  • The mid-facial region was dissected from embryo heads and incubated in 0.05% trypsin-EDTA solution for 1 h at 37°C, after which the tissue was triturated by repeated aspiration.
  • Cells were centrifuged, resuspended in Dulbecco's Minimal Essential Medium (DMEM) containing 10% fetal calf serum (FCS), plated onto 10 cm cell culture dishes, and incubated at 37°C with 6% CO2.
  • At confluency, cranial fibroblasts were passaged by trypsinization.
  • Bmp7 stimulation experiments were performed in 24-well dishes with cells from the second passage.
  • Fibroblasts were first starved for 24 h in DMEM/0.3% FCS, before the medium was changed to DMEM/0.3% FCS containing human recombinant Bmp7 (, , 0, 10, 20, 50, and 100 ng/ml, respectively).
  • For positive controls, wells were incubated with DMEM/10% FCS.
  • Cell supernatant was collected from individual wells after 24 h, run on SDS-7.5% polyacrylamide gels under reducing conditions, and proteins were transferred to nitrocellulose.
  • Blots were briefly stained with 0.1% Ponceauand then incubated with rabbit anti-mouse tenascin-W antiserum (see above) or rat anti-mouse tenascin-C monoclonal antibody mTn12 (obtained fromand

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Eggs and Embryo Manipulations

  • Fertilized White Leghorn chicken eggs were incubated at 38°C and the embryos staged according toand Hamilton (HH) in situ hybridization.

Specification of intermediate mesoderm (IM) from the hESC-derived PS cells.

50 ng/ml BMP7
  • (b) Comparison of OSR1 transcripts by combinatorial treatments with exogenous growth factors of retinoic acid , BMP7 (B7) and FGF2 (F2).