Bmp2

  • Official Full Name

    bone morphogenetic protein 2

  • Overview

    The protein encoded by this gene belongs to the transforming growth factor-beta (TGFB) superfamily. The encoded protein acts as a disulfide-linked homodimer and induces bone and cartilage formation. [provided by RefSeq, Jul 2008]
  • Synonyms

    BMP2; bone morphogenetic protein 2; BDA2; BMP2A; BMP-2A; bone morphogenetic protein 2A;

  • Recombinant Proteins
  • GMP Proteins
  • Cell & Tissue Lysates
  • Transfected Stable Cell Lines
  • Protein Pre-coupled Magnetic Beads
  • Cattle
  • Chicken
  • Dog
  • Human
  • Human/Mouse/Rat
  • Human/Mouse/Rat/Rhesus/Canine
  • Mouse
  • Pig
  • Rabbit
  • Rat
  • CHO
  • CHO-K1
  • E. coli
  • E.coli
  • HEK293
  • Human
  • Human Cell
  • Human cells
  • Mammalian Cell
  • Mammalian cells
  • Nicotiana Tobacum
  • Wheat Germ
  • Yeast
  • C
  • His
  • Fc
  • GST
  • His (Fc)
  • Avi
  • His(C
  • ter)
  • His|GST
  • His|S
  • His|T7
  • SUMO
  • N/A
  • N
  • hFc
  • Tag Free
Species Cat.# Product name Source (Host) Tag Protein Length Price
Human BMP2-23H Active Recombinant Human BMP2 CHO N/A
Human BMP2-30H Active Human BMP2 Human N/A
Human BMP2-17H Active Recombinant Human BMP2 Nicotiana Tobacum N/A
Human BMP2-56H Active Recombinant Human BMP2, HIgG1 Fc-tagged, mutant CHO Fc
Human BMP2&BMP7-709H Active Recombinant Human BMP2&BMP7 E.coli N/A
Human BMP2-01HG Active GMP Recombinant Human BMP-2 Protein CHO-K1
Human BMP2-01H Recombinant Human BMP2 protein E.coli N/A 115
Human BMP2-123H GMP Recombinant Human BMP2 E.coli N/A
Human BMP2-867H Recombinant Human BMP2 protein(Gln283~Arg396), His-tagged E. coli N-His Gln283~Arg396
Human BMP2-261H Recombinant Human BMP2 Protein, GST-tagged Wheat Germ GST
Human BMP2-124H Active Recombinant Human BMP2, Fc-tagged CHO Fc
Human BMP2-31084TH Recombinant Human BMP2 N/A
Human BMP2-22H Recombinant Human Bone Morphogenetic Protein-2 CHO N/A
Human BMP2-560H Recombinant Human BMP2 protein, His & GST-tagged E.coli His/GST Gln283~Arg396
Human BMP2-10249H Recombinant Human BMP2, GST-tagged E.coli GST 1-396a.a.
Human BMP2-561H Recombinant Human BMP2 protein, His-tagged E.coli His Leu24~Arg396
Human BMP2-210H Recombinant Human BMP2 protein, His/S-tagged E.coli His/S
Human BMP2-259H Recombinant Human BMP2 protein, His-tagged E.coli His
Human BMP2-260H Recombinant Human BMP2 Protein, GST-tagged Wheat Germ GST
Human BMP2-3075HCL Recombinant Human BMP2 cell lysate Human Cell N/A
Human BMP2-1119H Recombinant Human BMP2 protein E.coli Ala284-Arg396
Human BMP2-11H Recombinant Active Human BMP2 Protein, His-tagged(C-ter) E.coli His(C-ter)
Human BMP2-136H Recombinant Human BMP2 Protein E.coli
Human BMP2-2596H Recombinant Human BMP2 protein, His-SUMO-tagged E.coli His-SUMO 283-396aa
Human BMP2-129HG Active GMP Recombinant Human BMP2 protein, Fc-tagged HEK293 Fc DNA sequence encoding Human BMP-2(NP_001191.1 ) was expressed with Fc tag at the C-terminal.
Human BMP2-1839H Active Recombinant Human BMP2 protein E.coli N/A Ala 284 - Arg 396
Human BMP2-08HG Active Recombinant Human BMP2 Protein (Gln283-Arg396), GMP Grade CHO Gln283-Arg396
Human BMP2-0778H Recombinant Human BMP2 Protein (Gln283-Arg396), C-His tagged Yeast C-His Gln283-Arg396
Human BMP2-5352H Recombinant Human BMP2 protein, His-tagged Yeast His 283-396aa
Human BMP2-1597H Recombinant Human BMP2 Protein (Gln283-Arg396) E.coli Tag Free Gln283-Arg396
Human BMP2-398H Active Recombinant Human BMP2 Protein E.coli Tag Free
Human BMP2-011H Active Recombinant Human BMP2 Protein E.coli
Human BMP2-02H Recombinant Human/Mouse/Rat/Bovine/Porcine BMP2 Protein E.coli
Human BMP2-5101H Recombinant Human BMP2 Protein (Gln283-Arg396), N-Fc tagged Mammalian cells N-Fc Gln283-Arg396
Human BMP2-03H Active Recombinant Human BMP2 Protein, Animal Free Human cells
Human BMP2-277H Active Recombinant Human BMP2 Protein (Gln283-Arg396), C-His tagged, Animal-free, Carrier-free E.coli C-His Gln283-Arg396
Human BMP2-437B Active Recombinant Human BMP2 Protein E.coli
Human BMP2-132H Human Bone morphogenetic Protein-2 (rDNA derived) Reference standard N/A
Human BMP2-119HG Active GMP Recombinant Human BMP2 Protein CHO N/A
Mouse BMP2-2430M Recombinant Mouse BMP2 Protein Mammalian Cell His
Mouse Bmp2-562M Recombinant Mouse Bmp2 protein, His-tagged E.coli His Gln281~Arg394
Mouse Bmp2-211M Recombinant Mouse Bmp2 protein, His/S-tagged E.coli His/S
Mouse BMP2-1052M Recombinant Mouse BMP2 Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
Mouse BMP2-1052M-B Recombinant Mouse BMP2 Protein Pre-coupled Magnetic Beads HEK293
Rat BMP2-996R Recombinant Rat BMP2 Protein Mammalian Cell His
Rat Bmp2-565R Recombinant Rat Bmp2 protein, His-tagged E.coli His Ser49~Ile243
Rat Bmp2-212R Recombinant Rat Bmp2 protein, His/S-tagged E.coli His/S
Rat BMP2-654R-B Recombinant Rat BMP2 Protein Pre-coupled Magnetic Beads HEK293
Rat BMP2-654R Recombinant Rat BMP2 Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
Rabbit BMP2-566R Recombinant Rabbit BMP2 protein, His-tagged E.coli His Lys284~Val388
Dog BMP2-558D Recombinant Dog BMP2 protein, His-tagged E.coli His Ser50~Gln218 (Accession # J9P401)
Dog BMP2-559D Recombinant Dog BMP2 protein, His-tagged E.coli His Gly219~Ser350 (Accession # J9P401)
Cattle BMP2-567C Recombinant Cattle BMP2 protein, His-tagged E.coli His Ser219~Lys392
Cattle BMP2-557C Recombinant Cattle BMP2 protein, His & T7-tagged E.coli His/T7 Leu24~Arg395 (Accession # A5PJI9)
Human/Mouse/Rat BMP2-06H Active Recombinant Human/Mouse/Rat BMP2 Protein E.coli
Human/Mouse/Rat BMP2-05H Active Recombinant Human/Mouse/Rat BMP2 Protein E.coli
Human/Mouse/Rat/Rhesus/Canine BMP2-16H Active Recombinant Human/Mouse/Rat/Rhesus/Canine BMP2 protein(Gln283-Arg396), hFc-tagged HEK293 N-hFc Gln283-Arg396
Pig BMP2-564P Recombinant Pig BMP2 protein, His-tagged E.coli His Pro274~Lys382 (Accession # E1AXT2)
Pig BMP2-563P Recombinant Pig BMP2 protein, His-tagged E.coli His Leu117~Gly267 (Accession # E1AXT2)
Chicken BMP2-5929C Recombinant Chicken BMP2 Mammalian Cell His
  • Background
  • Quality Guarantee
  • Case Study
  • Involved Pathway
  • Protein Function
  • Interacting Protein
  • Other Resource

What is bmp2 protein?

The BMP2 protein, or Bone Morphogenetic Protein 2, is a transformative member of the growth factor-beta superfamily extensively implicated in innumerable developmental processes. The inherent property of BMP2 to stimulate bone and cartilage growth, as a regenerative and non-mitogenic extracellular protein, has led to the utilization of BMP2 as a therapeutic agent for bone healing and repair.

BMP2 was first discovered during the 1960s through studies focused on osteoinductive substances. The exact timeframe of BMP2's discovery is somewhat fuzzy, owing to the multitude of intrinsic components involved in bone development. Historically, the discovery of BMP2 was a significant stride in the study of developmental biology, as it highlighted the existence of secreted proteins that could direct cellular fate.

The BMP2 gene is situated on the short arm of chromosome 20 at locus 20p12. The gene encompasses seven exons, with transcription resulting in a precursor protein that is subsequently cleaved to generate the mature protein. The BMP2 protein structure comprises a monomer that is part of a larger homodimer or heterodimer complex. This larger complex is stabilized by a disulfide bond and demonstrates a distinct 'cystine knot' like configuration.

What is the function of bmp2 protein?

BMP2 is instrumental in inducing bone and cartilage formation. It regulates growth, differentiation, chemotaxis, and apoptosis in a myriad of cell types, including mesenchymal cells, epithelial cells, hematopoietic cells, neuronal cells, etc. Essentially, BMP2 acts as a vital regulator during embryogenesis and postnatal development, molding various organs, including teeth, limbs, heart, and the nervous system. In adults, its role further extends to maintaining homeostasis of tissues such as bone and cartilage.

Bmp2 related signaling pathway

BMP2 signaling is performed chiefly via canonical SMAD-dependent and non-canonical SMAD-independent pathways. The SMAD-dependent pathway is the primary signal transduction pathway for TGF-β superfamily members, including BMP2. Here, transduced signals from cell surface to nucleus regulate gene transcription. Conversely, the SMAD-independent pathways include MAPK pathway, PI3K/Akt pathway, and PKC pathway, primarily involved in the regulation of cytoskeletal dynamics and cell mobility.

BMP2 Related Diseases

  • Fibrodysplasia Ossificans Progressiva (FOP): Also known as "Stone Man Syndrome," this is a rare disease in which the body's soft tissues progressively turn into bone. BMP2, along with other proteins, play a significant role in the abnormal bone growth.
  • Heterotopic Ossification (HO): This condition also involves abnormal bone growth in areas like muscles and tendons. Increased levels of BMP2 can kick start the process of ossification, leading to this condition.
  • Atherosclerosis: BMP2 plays a role in the formation of bone-like tissue in the arteries, a critical aspect of atherosclerosis.
  • Congenital Heart Defects: Children born with heart defects may have mutations in the BMP2 gene. It plays an important role in heart development, and disruptions can cause defects.
Bone morphogenetic protein-2 as a novel biomarker for refractory chronic rhinosinusitis with nasal polyps (Kim, J. Y., 2021)

Bone morphogenetic protein-2 as a novel biomarker for refractory chronic rhinosinusitis with nasal polyps (Kim, J. Y., 2021)

Biomedical Application of BMP2 Protein

  • Bone Regeneration: BMP2 is used as a clinical tool to stimulate bone regeneration. It is used in spinal fusion, fractures, and also in dental implants where bone growth is required.
  • Cartilage Repair: BMP2 can stimulate chondrocytes, the cells that produce cartilage, making it potentially beneficial for cartilage repair.
  • Cancer Treatment: Due to its role in cell growth and death, BMP2 can potentially be used as a novel therapeutic target or diagnostic biomarker for various cancers.
  • Wound Healing: Studies suggest BMP2 can enhance wound healing and tissue repair, potentially shortening recovery times after surgery or injury.

High Purity

SDS-PAGE

Fig1. SDS-PAGE (BMP2-01H) (PROTOCOL for western blot)

High Bioactivity & Detection Sensitivity

BMP2 activity Bioactivity

Fig2. BMP2 activity Bioactivity is determined using a BMP2-responsive firefly luciferase reporter in stably transfected HEK293T cells. Cells are treated with a serial dilution of BMP2 for 6 hours. Firefly luciferase activity is measured and normalized to the control Renilla luciferase activity. EC50 = 7.81 ng/mL (0.3 nM).

Case study 1: Janki J Patel, 2015

One strategy to reconstruct large bone defects is to prefabricate a vascularized flap by implanting a biomaterial scaffold with associated biologics into the latissimus dorsi and then transplanting this construct to the defect site after a maturation period. This strategy requires the ability to quickly (<1 h within an operating room) and efficiently bind biologics to scaffolds. It also requires the ability to localize biologic delivery.

In this study, the efficacy of binding bone morphogenetic protein-2 (BMP2) to poly-ɛ-caprolactone (PCL) was investigated using adsorption and conjugation as a function of time. Adsorbed 65 μg/mL BMP2 solution resulted in the greatest regenerated bone volume (15.0±3.0 mm3), elastic modulus (20.1±3.0 MPa), and %bone ingrowth in the scaffold interior (17.2%±5.4%) when compared with conjugation.

Thus this article indicates that adsorption may be optimal for the clinical application of prefabricating bone flaps due to BMP2 binding in a short exposure time, retained BMP2 bioactivity, and bone growth adhering to scaffold geometry and into pores with healthy marrow development.

BMP2 binding to PCL discs via adsorption or conjugation

Fig1. BMP2 binding to PCL discs via adsorption or conjugation. PCL discs were exposed to 1.4 μg/mL BMP2solution for 0.5, 1, 5, or 16 h at 23°C or 4°C. BMP2 was quantified with an ELISA (n=3). BMP2, bonemorphogenetic protein-2; ELISA, enzyme-linked immunoabsorbant assay.

Fig2. Conjugated and adsorbed BMP2 released from PCL

Fig2. Conjugated and adsorbed BMP2 released from PCL. Cumulative release of BMP2 from PCL scaffolds into DPBS whenexposed to 20 μg/mL BMP2 for 1 h at 23°C. Release environment conditions were sterile,37°C, 5% CO2, and 95% humidity. *p<0.05

Fig3. Conjugation produced bone that closely followed PCL surface geometry

Fig3. Conjugation produced bone that closely followed PCL surface geometry. Adsorption produced bone growth into the pores in addition to following surface geometry. Two representative samples from each group are shown. Bright white areas indicate bone formation (blue arrow), and gray areas are scaffold (red*). Dark areas (orange dashed lines) indicate pores.

Fig4. Hematoxylin and eosin images of PCL/BMP2 scaffold pores

Fig4. Hematoxylin and eosin images of PCL/BMP2 scaffold pores. Both of the adsorbed groups (20 and 65?μg/mL) showed blood, bone, and fatty marrow growth into the scaffold pore space. Bright-field images of scaffold pores taken at 10× magnification. b, bone; f, fibrous tissue; m, marrow; s, scaffold. Negative controls consisted mainly of fibrous tissue.

Case Study 2: Ali H Hassan, 2016

The aim of the present study was to develop and examine a new non-invasive injectable graft for the repair of alveolar bone clefts using recombinant human bone morphogenetic protein-2 (rhBMP-2) encapsulated within injectable liposomal in situ gel (LIG).

Different liposomal formulations loaded with rhBMP-2 were prepared, and the effects of the preparation methods and lipid content on the efficiency of rhBMP-2 encapsulation within the liposomes were studied. Critical size alveolar defects were surgically created in the maxillae of 30 New Zealand rabbits and treated with different injectable formulae, including rhBMP-2 liposomes and in situ gel (rhBMP-2-LIG).

The results indicated that the prepared rhBMP-2-LIG prolonged the release and residence time of BMP-2 within rabbits for more than 7 days. BMP-2-LIG is a promising delivery device for the repair of alveolar bone defects associated with cleft deformities.

Fig1. Mean plasma levels of BMP-2 after the local injection of 5 mg/kg of BMP-2 isotonic saline into defects inrabbits

Fig1. Mean plasma levels of BMP-2 after the local injection of 5 mg/kg of BMP-2 isotonic saline into defects inrabbits. These experimental variables were optimum for the release of rhBMP-2, reflecting the availability of thiscompound at the defect. (A), BMP-2 in unilamellar liposomal suspension (B), BMP-2 dispersed in the in situ gel(C),rhBMP-2-LIG-3 formula (D) and negative control (E).

Fig2. The newly formed bone was surrounded with fibro-vascular tissues and this defect might be fully repaired withtime

Fig2. The newly formed bone was surrounded with fibro-vascular tissues and this defect might be fully repaired withtime. Photomicrograph of a bone defect in Group A, Group B (slides stained with H&E, at 4×(B1) and 40×(B2)), Group C(slides stainedwith H&E, at 4×(C1) and 40×(C2)), Group D (slides stained with H&E, at 4×(D*,’) and40×(D;,”)) and Group E (slides stained with H&E, at 4×(E*) and 10×(E’).

Bmp2 involved in several pathways and played different roles in them. We selected most pathways Bmp2 participated on our site, such as Cytokine-cytokine receptor interaction, Hedgehog signaling pathway, TGF-beta signaling pathway, which may be useful for your reference. Also, other proteins which involved in the same pathway with Bmp2 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

Pathway Name Pathway Related Protein
Cytokine-cytokine receptor interactionIFNB;IFNA2;IL20;GDF5;LOC100033925;IL11RA2;KIT;CCR8L;TGFBR1B
Hedgehog signaling pathwayWNT4A;SHHA;WNT1;STK36;GLI3;GLI2B;PRKACA;CSNK1G2B;DYRK1AA
TGF-beta signaling pathwayID2;THBS1;ZFYVE9;BMPR1BA;ACVR1BA;ROCK2B;SMAD3A;SMAD1;NODAL
Hippo signaling pathwayLATS2;CTNNA2;APC2;CCND3;BMP6;PPP1CA;GSK3B;BMP8B;AJUBA
Signaling pathways regulating pluripotency of stem cellsID4;ID2;LIFR;INHBE;TBX3;SMAD5;WNT16;SOX2;GRB2
Pathways in cancerITGB1;Fzd4;FOXO1;RHOA;GSK3B;BCR;ABL1;LAMB2;GNG5
Basal cell carcinomaWNT10B;WNT7A;SMO;WNT9A;WNT3;WNT1;GLI3;BMP4;WNT4

Bmp2 has several biochemical functions, for example, BMP receptor binding, SMAD binding, co-receptor binding. Some of the functions are cooperated with other proteins, some of the functions could acted by Bmp2 itself. We selected most functions Bmp2 had, and list some proteins which have the same functions with Bmp2. You can find most of the proteins on our site.

Function Related Protein
BMP receptor bindingBMP8A;BMP2B;BMP4;BMP7B;PYCARD;BMP6;BMP8B;BMP7;BMP2
SMAD bindingSMURF2;SKILB;ACVR1;EID2;FKBP1A;TGFBR3;SNW1;RNF111;ACVR1B
co-receptor bindingBMP2;NEO1;HFE;DKK1;BMP4;TFR2
cytokine activityIl2;Ccl27a;TNFSF8;TNFSF4;TNFSF14;CMTM2;IFNW1;Il1f8;TNFSF12
growth factor activityRABEP1;FGF10B;LFT2;VEGFB;F2;IL6;FGF9;FGF8;GMFB
phosphatase activator activityBMP2;FRS2;GTF2F1
protein bindingEFCAB4B;TWF2;NR1D2;SLC52A2;WBP2NL;HERPUD1;RARRES3;ELL;SHMT1
protein heterodimerization activitySYCP2;USF1;PKNOX1;HER5;PBX1;HIST1H4E;H2-AA;HIST1H4J;HIST1H4G
receptor bindingFGF12B;HSPA1B;F7;FGF24;IAPP;GLA;TNFSF10;CNPY3;TENM2
retinol dehydrogenase activityADH4;SDR16C5;RDH11;RDH8;SDR9C7;AKR1C3;RDH1;HSD17B6;DHRS3
transforming growth factor beta receptor bindingINHBAB;TGFB1A;GDF5;FKBP1A;GDF2;BMP4;BMP10;INHBA;BMP2B

Bmp2 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with Bmp2 here. Most of them are supplied by our site. Hope this information will be useful for your research of Bmp2.

BMPR1A; FSTL1; BMPR1B; NOG; WFIKKN2

Gene Family

TGF

Research Area

Related articles

Olivares-Navarrete, R; Hyzy, SL; et al. Coordinated regulation of mesenchymal stem cell differentiation on microstructured titanium surfaces by endogenous bone morphogenetic proteins. BONE 73:208-216(2015).
Xu, LL; Liu, Y; et al. U0126 promotes osteogenesis of rat bone-marrow-derived mesenchymal stem cells by activating BMP/Smad signaling pathway. CELL AND TISSUE RESEARCH 359:537-545(2015).
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Reviews
05/06/2023

    We have tested the recombinant protein in our ELISAs and it performs well.

    02/01/2023

      I'm pleased with your recombinant products. It is done well in our experiment.

      01/29/2023

        Very nice puchase experience with all of you.

        08/06/2022

          I’ve used the products you provided, and they all work good in my study.

          04/09/2021

            Thanks so much! Your protein performed really well,

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