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Recombinant Human BMP4 Protein

Cat # Size Price Quantity
63150120 μg$220
631502100 μg$625

  Bulk/Custom

Product Details

ApplicationBioassay
FormatLyophilized from sterile 30% Acetonitrile, 1/1000 TFA.
Expression HostE.coli
Research AreasEmbryogenesis, Osteogenesis, Organogenesis
Target NameBMP4, Bone Morphogenetic Protein 4, Bone Morphogenetic Protein 2B, BMP2B
SpeciesHuman
accession numberP12644
SourcesA DNA sequence encoding the human BMP4 (P12644) (Ser293-Arg408, E399D) was expressed with an N-terminal Met.
Molecular WeightThe recombinant Human BMP4 consists of 117 amino acids and predicts a molecular mass of 13.25 kDa.
Affinity TagNone
Purity≥ 95 % as determined by SDS-PAGE.
Regulatory StatusRUO
Endotoxin level< 1.0 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 BMP4 (bone morphogenetic protein 4) is a secreted growth factor belonging to the transforming growth factor-β (TGF-β) superfamily. It plays a critical role in embryonic development, tissue patterning, and organogenesis, including bone and cartilage formation, limb development, and neural differentiation. BMP4 is synthesized as a precursor protein that undergoes proteolytic cleavage to generate a mature, biologically active dimer. Structurally, the mature BMP4 protein forms a disulfide-linked homodimer characterized by a conserved cystine knot motif typical of TGF-β family members.

BMP4 exerts its function by binding to heteromeric complexes of type I and type II serine/threonine kinase receptors on the cell surface, primarily BMPR1A (ALK3), BMPR1B (ALK6), and BMPR2. Upon ligand binding, these receptors phosphorylate SMAD1/5/8 proteins, which then associate with SMAD4 and translocate to the nucleus to regulate gene expression. BMP4 activity is tightly regulated by extracellular antagonists such as noggin, chordin, and gremlin, which bind BMP4 and prevent receptor interaction.

Dysregulation of BMP4 signaling has been implicated in various diseases, including cancer, fibrosis, and developmental disorders. Overexpression or aberrant signaling can contribute to tumor progression, epithelial–mesenchymal transition, and abnormal tissue remodeling, while insufficient activity may impair normal development.

Therapeutically, BMP4 and its signaling pathway are being explored in regenerative medicine, particularly for bone repair and tissue engineering. Modulating BMP4 activity, either by recombinant proteins or inhibitors, offers potential strategies for treating skeletal defects, fibrotic diseases, and cancer.

Data Sheets

Recombinant Human BMP4 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.

Have a product or application question? Consult our FAQs or contact us.