Recombinant Human/Mouse/Rat BMP-2 Protein

Beta LifeScience SKU/CAT #: BL-1735NP
BL-1735NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-1735NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human/Mouse/Rat BMP-2 Protein

Beta LifeScience SKU/CAT #: BL-1735NP
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Product Overview

Description Recombinant Human/Mouse/Rat Bone Morphogenetic Protein 2 is produced by our E.coli expression system and the target gene encoding Gln283-Arg396 is expressed.
Accession P12643
Synonym Bone Morphogenetic Protein 2; BMP-2; Bone Morphogenetic Protein 2A; BMP-2A; BMP2; BMP2A
Gene Background Bone Morphogenetic Protein-2 (BMP-2) is one of the bone-growth regulatory factors that belong to the transforming growth factor-beta (TGF-beta) superfamily of proteins. BMPs are synthesized as large precursor molecules, which are cleaved by proteolytic enzymes. The active form of BMP-2 can consist of a dimer of two identical proteins or a heterodimer of two related bone morphogenetic proteins.
Molecular Mass 13.3 KDa
Apmol Mass 13 KDa, reducing conditions
Formulation Lyophilized from a 0.2 μm filtered solution of 10mM HAc-NH4Ac, 4% D-Mannitol, pH 4.0.
Endotoxin Less than 0.001 ng/µg (0.01 EU/µg) as determined by LAL test.
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution Always centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in 50mM Acetic Acid.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping The product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

Target Details

Target Function Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including cardiogenesis, neurogenesis, and osteogenesis. Induces cartilage and bone formation. 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. Can also signal through non-canonical pathways such as ERK/MAP kinase signaling cascade that regulates osteoblast differentiation. Stimulates also the differentiation of myoblasts into osteoblasts via the EIF2AK3-EIF2A-ATF4 pathway by stimulating EIF2A phosphorylation which leads to increased expression of ATF4 which plays a central role in osteoblast differentiation.
Subcellular Location Secreted.
Protein Families TGF-beta family
Database References
Tissue Specificity Particularly abundant in lung, spleen and colon and in low but significant levels in heart, brain, placenta, liver, skeletal muscle, kidney, pancreas, prostate, ovary and small intestine.

Gene Functions References

  1. These results not only call into question the use of VEGFA alone in bone regeneration, but also highlight the importance in BTE of appropriately formulated combined delivery of VEGFA and BMP2. PMID: 29386057
  2. This work indicates that NELL-1, HMGB1, and CCN2 might enhance bone defect healing via the recruitment of endogenous cells and induction of vascularization and act via different processes than BMP2. PMID: 28463604
  3. Serum BMP2 and Smad4 levels in patients with senile osteoporotic fracture were significantly lower than those in normal controls PMID: 29938690
  4. conclude that SUMO3-tagged hBMP2 is more suited for generation of soluble form of the protein and addition of SUMO3 tag does not affect the functional activity of hBMP2 PMID: 29574511
  5. The present study identified a change in miR-22, miR-140, and BMP-2 expression in the synovial fluid of patients with osteoarthritis before and after arthroscopic debridement. PMID: 29429984
  6. The study revealed an enhanced sensitivity of aortic valve interstitial cells to osteogenic inductors in aortic stenosis patients, which indicates probable implication of OPN, OPG, and BMP2 genes in pathogenesis of aortic valve calcification. PMID: 29308559
  7. The rhBMP2 monomer and dimer were eluted at 0.9 M and 0.6 M NaCl, respectively. The alkaline phosphatase assay of rhBMP2 (0, 50, 100, 200, and 400 ng/ml) was analyzed on C2C12 cells and maximum 200 ng/ml activity was observed in dose dependent manner PMID: 29333457
  8. In contrast to BMP-2, BMP-7 concomitantly inhibited the expression of profibrotic genes PMID: 28102712
  9. The binding free energies indicate that ALK-3 preferably binds to BMP-2 instead of BMP-9. The structural analysis shows that ALK-3 binding with BMP-2 occurs in a perfectly symmetry pathway, whereas this symmetry is lost for possible ALK-3 interactions with BMP-9 PMID: 28869862
  10. The results demonstrate the efficacy of HPP-GC hydrogel in minimizing the diffusive loss of rhBMP-2 from the implantation site, compared to the collagen hydroxyapatite scaffold. PMID: 28847606
  11. The in vitro results suggest that altered BMP2 regulatory function at rs1884302 may contribute to the etiology of sagittal nonsyndromic craniosynostosis. The in vivo results indicate that differences in regulatory activity depend on the presence of a C or T allele at rs1884302. PMID: 28985029
  12. Collectively, according to our study, rhIL-6 could induce the extracellular calcification and osteogenic differentiation of human artery smooth muscle cells through upregulating endogenous BMP2 in vitro. This may be one of the underlying mechanisms of the overwhelming vascular calcification in rheumartoid arthritis. PMID: 28134597
  13. HUCB-MSC transfected with mTAT/PEI were shown to express more BMP-2 protein and mRNA. PMID: 28951869
  14. These results showed that BMP2 activated SMAD1/5/8 phosphorylation and up-regulated BAMBI mRNA in human granulosa-lutein cells. PMID: 28578012
  15. BMP-2 can enhance HUVEC proliferation, migration and angiogenesis through P38, ERK and Akt/m-TOR pathway. PMID: 27886213
  16. Study shows that recombinant human bone morphogenetic protein-2 activates hippo signaling through RASSF1 in esophageal cancer cells PMID: 27230238
  17. SNPs in BMP2 can predict grade >/= 2 or 3 RP after radiotherapy for NSCLC and improve the predictive power of MLD model. PMID: 28574846
  18. CTGF and BMP2 are induced following myocardial ischemia in mice and humans. PMID: 28460577
  19. Missense mutations in COL6A1, COL11A2, FGFR1, and BMP2 genetically predispose patients to ossification of posterior longitudinal ligaments. PMID: 27246988
  20. Computational analysis on conformational dynamics of BMP-2 has been presented. PMID: 27426435
  21. there was a significant association in men between BMP2 genetic variant (rs235756) and hypertension in the genetically homogeneous Finnish population; no significant association between BMP2 rs235768 (A>T) and hypertension was found PMID: 29390526
  22. Adding NMP as an adjunct to rhBMP-2-coated BCP produced inconsistent effects on bone regeneration, resulting in no significant benefit compared to controls. PMID: 28680881
  23. observations regarding the dysregulation of these gatekeepers of neuronal viability may have important implications in understanding the iAbeta1-42 mediated effects observed in AD PMID: 29470488
  24. This study demonstrates that viscous collagen gel can be an effective carrier for rhBMP-2 delivery into surgical sites, and that the injectable rhBMP-2-containing collagen gel may be applied for the enhancement of tendon-bone interface healing PMID: 26177709
  25. Synergistic effects of BMP-2, BMP-6 or BMP-7 with human plasma fibronectin onto hydroxyapatite coatings. PMID: 28434979
  26. High-dose recombinant human bone morphogenetic protein-2 impacts histological and biomechanical properties of a cervical spine fusion segment: results from a sheep model. PMID: 26053675
  27. Report osteoblast-like transformation of epithelial breast cancer cells that have undergone epithelial-mesenchymal transition followed by bone morphogenetic protein-2 stimulation. RUNX2 functions as a master mediator of this process. PMID: 27806311
  28. Taken together, our results suggest that DHCA may be developed as an efficient therapeutic for osteoporosis by regulating osteoblastogenesis through its estrogenic effects. PMID: 29253565
  29. BMP2-transduced BMSCs can maintain the chondrocyte-like phenotype in PRP gel in vitro, and the combined use of these two agents can significantly promote repair of the degenerated discs in vivo PMID: 26169838
  30. these results suggest that the BMP2 gene polymorphism may be related to the development of allograft rejection and graft dysfunction in kidney transplant recipients PMID: 28583517
  31. Data show that the GREMLIN 2 (GREM2) expression during Induced Pluripotent Stem Cell (hiPS) cell cardiac differentiation follows the expression pattern of cardiac-specific genes. PMID: 28125926
  32. Results identify a novel 4671-bp tandem duplication downstream of BMP2, which is associated with brachydactyly type A2 . The duplication highly overlaps the sequences reported previously but has a different breakpoint and a different flanking microhomology. PMID: 29129813
  33. miR-106b inhibited osteoblastic differentiation and bone formation partly through directly targeting bone morphogenetic protein 2. PMID: 28108317
  34. BMP2 decreases gap junction intercellular communication of luteinized human granulosa cells by downregulating Cx43 expression through an ALK2/ALK3-mediated SMAD-dependent signaling pathway. PMID: 27986931
  35. BMP2 also requires Src for filamentous actin polymerization in Tgfbr3(-/-) epicardial cells. PMID: 26645362
  36. The deletion contained 17 protein coding genes including PROKR2 and BMP2, both of which are expressed during embryological development of the pituitary gland. PROKR2 mutations have been associated with hypopituitarism but a heterozygous deletion of this gene with hypopituitarism is a novel observation. PMID: 28586151
  37. both bone morphogenetic protein 2 (BMP2) and BMP6 are proangiogenic in vitro and ex vivo and that the BMP type I receptors, activin receptor-like kinase 3 (ALK3) and ALK2, play crucial and distinct roles in this process. PMID: 28733457
  38. sequential presentation of PDGF to BMP-2 led to increased tubule formation over simultaneous delivery of these growth factors. PMID: 27650131
  39. Bone Morphogenetic Protein-2, But Not Mesenchymal Stromal Cells, Exert Regenerative Effects on Canine and Human Nucleus Pulposus Cells PMID: 27829314
  40. The structure of Grem2-GDF5 complex has revealed a number of key findings for DAN-family mediated BMP2 inhibition. PMID: 27524626
  41. Bioluminescence imaging reveals increased MSC survival when implanted in BMP-2 PAHs. PMID: 27581621
  42. Bone morphogenetic protein 2 promotes osteogenesis of bone marrow stromal cells in type 2 diabetic rats via the Wnt signaling pathway PMID: 27702654
  43. monocytes interact specifically with Chitosan-Fibrinogen (Ch-Fg) via TLR-4, triggering particular intracellular signalling pathways (ERK and JNK, but not p38), downstream of TLR-4. Functionally, Ch-Fg induced monocytes to produce the osteogenic mediator BMP-2. PMID: 27856281
  44. This study showed that si-Grem2 increased the BMP-2-induced osteogenic differentiation of hBMSCs via the BMP-2/Smad/Runx2 pathway. PMID: 27335248
  45. Low doses of IL1B activate the BMP/Smad signaling pathway to promote the osteogenesis of periodontal ligament stem cells, but higher doses of IL1B inhibit BMP/Smad signaling through the activation of NF-kappaB and MAPK signaling, inhibiting osteogenesis. PMID: 27415426
  46. Increased miR-93-5p in trauma-induced osteonecrosis of the femoral head patients inhibited osteogenic differentiation, which may be associated with BMP-2 reduction. PMID: 28797104
  47. RANKL promotes VC by inducing BMP-2 release from HAECs PMID: 27339040
  48. KDM5A-mediated H3K4me3 modification participated in the etiology of osteoporosis and may provide new strategies to improve the clinical efficacy of BMP2 in osteoporotic conditions. PMID: 27512956
  49. fabricated scaffolds were well coated with DOPA as well as grafted with rhBMP2 at a quantity of 22.7+/-5ng when treatment with 100ng/ml rhBMP2 and 153.3+/-2.4ng when treated with 500ng/ml rhBMP2. This grafting enables rhBMP2 to be released in a sustained pattern. PMID: 26868173
  50. Data suggest pituitary cells secrete factor (TSP1) that binds to and inhibits action of BMP2 and BMP4; von Willebrand type C domain of TSP1 is likely responsible for this BMP2/4-binding activity. These studies were initially conducted using cultured cells from ovine pituitary gland and mouse cell line; interactions were confirmed using recombinant human proteins. (TSP1 = thrombospondin-1; BMP = bone morphogenetic protein) PMID: 28747434


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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