Recombinant Human Bone Morphogenetic Protein 2 (BMP2), Active

Name: Recombinant Human Bone Morphogenetic Protein 2 (BMP2), Active
Brand: Beta LifeScience
SKU: BLC-06000P
Availability: InStock

Greater than 95% as determined by SDS-PAGE.

Collections: Cytokines, Cytokines and growth factors, Growth factors and receptors, Recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Bone Morphogenetic Protein 2 (BMP2), Active is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 95% as determined by SDS-PAGE.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	The ED50 as determined by the cytolysis of MC3T3-E1 cells is less than 2 μg/ml
Uniprotkb	P12643
Target Symbol	BMP2
Synonyms	BDA2; BMP-2; BMP-2A; Bmp2; BMP2_HUMAN; BMP2A; Bone morphogenetic protein 2; Bone morphogenetic protein 2A
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	Tag-Free
Complete Sequence	QAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNSTNHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR
Expression Range	283-396aa
Protein Length	Full Length of Mature Protein
Mol. Weight	13.3 kDa
Research Area	Signal Transduction
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 μm Filtered 10 mM NH4-HAC, pH 4.0
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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	HGNC: 1069 OMIM: 112261 KEGG: hsa:650 STRING: 9606.ENSP00000368104 UniGene: Hs.73853
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

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
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
Serum BMP2 and Smad4 levels in patients with senile osteoporotic fracture were significantly lower than those in normal controls PMID: 29938690
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
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
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
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
In contrast to BMP-2, BMP-7 concomitantly inhibited the expression of profibrotic genes PMID: 28102712
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
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
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
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
HUCB-MSC transfected with mTAT/PEI were shown to express more BMP-2 protein and mRNA. PMID: 28951869
These results showed that BMP2 activated SMAD1/5/8 phosphorylation and up-regulated BAMBI mRNA in human granulosa-lutein cells. PMID: 28578012
BMP-2 can enhance HUVEC proliferation, migration and angiogenesis through P38, ERK and Akt/m-TOR pathway. PMID: 27886213
Study shows that recombinant human bone morphogenetic protein-2 activates hippo signaling through RASSF1 in esophageal cancer cells PMID: 27230238
SNPs in BMP2 can predict grade >/= 2 or 3 RP after radiotherapy for NSCLC and improve the predictive power of MLD model. PMID: 28574846
CTGF and BMP2 are induced following myocardial ischemia in mice and humans. PMID: 28460577
Missense mutations in COL6A1, COL11A2, FGFR1, and BMP2 genetically predispose patients to ossification of posterior longitudinal ligaments. PMID: 27246988
Computational analysis on conformational dynamics of BMP-2 has been presented. PMID: 27426435
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
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
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
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
Synergistic effects of BMP-2, BMP-6 or BMP-7 with human plasma fibronectin onto hydroxyapatite coatings. PMID: 28434979
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
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
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
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
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
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
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
miR-106b inhibited osteoblastic differentiation and bone formation partly through directly targeting bone morphogenetic protein 2. PMID: 28108317
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
BMP2 also requires Src for filamentous actin polymerization in Tgfbr3(-/-) epicardial cells. PMID: 26645362
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
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
sequential presentation of PDGF to BMP-2 led to increased tubule formation over simultaneous delivery of these growth factors. PMID: 27650131
Bone Morphogenetic Protein-2, But Not Mesenchymal Stromal Cells, Exert Regenerative Effects on Canine and Human Nucleus Pulposus Cells PMID: 27829314
The structure of Grem2-GDF5 complex has revealed a number of key findings for DAN-family mediated BMP2 inhibition. PMID: 27524626
Bioluminescence imaging reveals increased MSC survival when implanted in BMP-2 PAHs. PMID: 27581621
Bone morphogenetic protein 2 promotes osteogenesis of bone marrow stromal cells in type 2 diabetic rats via the Wnt signaling pathway PMID: 27702654
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
This study showed that si-Grem2 increased the BMP-2-induced osteogenic differentiation of hBMSCs via the BMP-2/Smad/Runx2 pathway. PMID: 27335248
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
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
RANKL promotes VC by inducing BMP-2 release from HAECs PMID: 27339040
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
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
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

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.