BMP-2 (human):Fc (human) (rec.) (non-lytic)
|Synonyms||BMP2; Bone Morphogenetic Protein 2|
The extracellular domain of human BMP-2 (aa 289-396) is fused to the N-terminus of the Fc region of a mutant human IgG1.
Shows the biological function of the BMP-2 moiety and exerts a prolonged circulating half-life caused by the modified Fc domain.
|Endotoxin Content||<0.06EU/μg protein (LAL test; Lonza).|
Reconstitute in 50µl sterile water.
Add 1X PBS to the desired protein concentration.
|Formulation||Lyophilized from 0.2μm-filtered solution in PBS.|
|Protein Negative Control|
|Other Product Data||
Non-lytic: Acts as a long lasting fusion protein which only binds to the receptor. Mutations to the complement (C1q) and FcgR I binding sites of the IgGs Fc fragment render the fusion proteins incapable of antibody directed cytotoxicity (ADCC) and complement directed cytotoxicity (CDC).
|Declaration||Manufactured by Chimerigen.|
|Shipping and Handling|
|Short Term Storage||+4°C|
|Long Term Storage||-20°C|
|Handling Advice||Avoid freeze/thaw cycles.|
Stable for at least 1 year after receipt when stored at -20°C.
Working aliquots are stable for up to 3 months when stored at -20°C.
|Product Specification Sheet|
Bone morphogenetic protein 2 (BMP-2) is a member of the BMP subgroup of the TGF-β superfamily. It plays a dominant role in embryonic dorsalventral patterning, organogenesis, limb bud formation and bone formation and regeneration. BMP-2 signals through heterodimeric complexes composed of a type I receptor (Activin RI, BMP-RIA or BMP-RIB) and a type II receptor (BMP-RII or Activin RIIB). BMP-2 induces chondrocyte proliferation, endochondral bone formation, longitudinal bone growth and bone and cartilage repair. It induces ectopic bone formation or calcification by promoting osteogenic and chondrogenic differentiation in mesenchymal cells, stem cells and vascular smooth muscle cells. It also promotes the maintenance and repair of colonic epithelium, suppresses neuronal dopamine synthesis and release, induces apoptosis in medulloblastoma cells and is required for cardiac contractility.