Name: Human BMP-8a Recombinant Protein(His Tag)
Synonyms: BMP-8;OP-2;Osteogenic Protein-2
Expression host: E.coli
Sequence: Ala 264-His 402
Accesstion: Q7Z5Y6
Species: Human
Mol_Mass: 16.6 kDa
AP_Mol_Mass: 17 kDa
Tag: C-His
Purity: > 98 % as determined by reducing SDS-PAGE.
Endotoxin:
Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Formulation: Lyophilized from sterile 20 mM sodium citrate, 0.2 M NaCl, pH 3.5. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.Please refer to the specific buffer information in the printed manual.
Reconstitution: Please refer to the printed manual for detailed information.
Background: Induces cartilage and bone formation. May be the osteoinductive factor responsible for the phenomenon of epithelial osteogenesis. Plays a role in calcium regulation and bone homeostasis. Signaling protein involved in regulation of thermogenesis and energy balance. Proposed to increase the peripheral response of brown adipose tissue (BAT) to adrenergic stimulation while acting centrally in the hypothalamus to increase sympathetic output to BATBy Similarity1 PublicationGrowth factor of the TGF-beta superfamily that plays important role in various biological processes, including spermatogenesis, osteogenesis, steroidogenesis as well as regulation of energy balance. Initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2. Once all three components are bound together in a complex at the cell surface, BMPR2 phosphorylates and activates BMPR1A. In turn, BMPR1A propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes. In addition, activates the SMAD2/3 pathway.
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