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Recombinant Human, Mouse, Rat, Rhesus, Canine BMP-2 Protein

Cat # Size Price Quantity
63350120 μg$275
633502100 μg$650

  Bulk/Custom

Product Details

ApplicationBioassay
FormatLyophilized from sterile 0.1% TFA, 30% ACN.
Expression HostE.coli
Target NameBMP2, BMP-2,Bone morphogenetic protein 2, bone morphogenetic protein 2A (BMP-2A), BDA2
SpeciesHuman, Mouse, Rat, Rhesus, Canine
accession numberNP_001191.1
SourcesA DNA sequence encoding the mature form of human / mouse / rat / rhesus / canine BMP2 (NP_001191.1) (Gln283-Arg396) was expressed with an initial Met. The mature form sequences of human, mouse, rat, rhesus and canine BMP2 are identical.
Molecular WeightThe recombinant human / mouse / rat / rhesus / canine BMP2 consists of 115 amino acids and has a predicted molecular mass of 13 KDa. It migrates as an approximately 14 KDa band in SDS-PAGE under reducing conditions.
Affinity TagNone
Purity≥95% as determined by SDS-PAGE.
Regulatory StatusRUO
Endotoxin level< 0.1 EU per μg protein
Protein ConcentrationLyophilized
Storage and HandlingSamples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Background Information

Human bone morphogenetic protein 2 (BMP-2), also known as BMP2, is a secreted growth factor belonging to the transforming growth factor-beta (TGF-β) superfamily. It plays a critical role in embryonic development, skeletal formation, cartilage differentiation, and bone remodeling. BMP-2 stimulates mesenchymal stem cells and progenitor cells to differentiate into osteoblasts, promoting extracellular matrix production and mineralization. It also participates in tissue repair and the maintenance of skeletal homeostasis.



Human BMP-2 is synthesized as a precursor protein of 396 amino acids, which undergoes proteolytic processing to generate the mature growth factor. The mature protein contains 114 amino acids per monomer and forms a biologically active, disulfide-linked homodimer. Each monomer adopts a characteristic cystine-knot structure stabilized by three intramolecular disulfide bonds, a hallmark of the TGF-β superfamily. This structure supports protein stability, receptor binding, and biological activity.



BMP-2 binds to specific cell-surface serine/threonine kinase receptors, primarily BMP receptor type IA (BMPR-IA/ALK3) and BMP receptor type IB (BMPR-IB/ALK6), together with type II receptors such as BMPR-II, activin receptor type IIA (ActRIIA), and activin receptor type IIB (ActRIIB). Receptor complex formation activates downstream signaling, particularly the SMAD1/5/9 pathway, as well as non-SMAD pathways such as MAPK, regulating gene expression, cell differentiation, and tissue development. Extracellular proteins, including noggin and chordin, can bind BMP-2 and inhibit its signaling.



Dysregulated BMP-2 signaling is associated with abnormal bone formation, skeletal disorders, tissue fibrosis, and aspects of cancer progression, although its effects depend on the tissue and disease context. Recombinant human BMP-2 (rhBMP-2) is used clinically in selected orthopedic and spinal fusion procedures to promote bone regeneration. It is also being investigated for bone defect repair, dental and craniofacial reconstruction, and tissue engineering. However, excessive or inappropriate BMP-2 activity can cause complications, including ectopic bone formation and inflammation, making controlled delivery and dosage important considerations in therapeutic applications.

Data Sheets

Recombinant Human, Mouse, Rat, Rhesus, Canine BMP-2 Protein TDS

Frequently Asked Questions

What are InnoCyto's Cytokines and Growth Factors?
These are recombinantly expressed signaling proteins, including interleukins, interferons, chemokines, and growth factors, that mediate cell communication, proliferation, differentiation, and immune activation. They are produced for use as research reagents to stimulate, modulate, or study cellular responses in vitro and in vivo.
What expression systems are these proteins produced in, and does it matter for my application?
Cytokines and growth factors may be produced in mammalian, insect, or E. coli expression systems depending on the protein, and the system affects properties like glycosylation, folding, and bioactivity. Non-glycosylated proteins from E. coli are often suitable for cell culture stimulation assays, while glycosylation-dependent proteins may require mammalian- or insect-expressed versions for full biological activity — check the product page for the expression system and recommended applications.
How is bioactivity measured and confirmed for each lot?
Bioactivity is typically confirmed using a functional cell-based assay (e.g., proliferation, differentiation, or reporter assay) relevant to the specific cytokine or growth factor, and is reported as an EC50/ED50 value or specific activity (units/mg) on the Certificate of Analysis. Always reference the lot-specific CoA rather than assuming activity is identical across lots or products.
Are these proteins carrier-free, and does that matter for my experiment?
Carrier-free formulations (without BSA or other stabilizing proteins) are available for applications where carrier protein could interfere with downstream analysis, such as certain in vivo studies or proteomic work, while carrier-containing formulations offer improved stability for routine cell culture use. Choose the format that matches your assay's sensitivity to background protein content.
Can these cytokines and growth factors be used for in vivo studies?
Mouse proteins may be used in vivo, but suitability depends on your endotoxin requirements for in vivo use. Endotoxin minimum threshholds vary by product and are indicated on the individual product page. Always confirm the endotoxin specification and formulation on the Certificate of Analysis before using a product in an in vivo setting.

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