BMP2 Protein (Homodimer)

N° du produit ABIN1589575

Protéine Recombinant BMP2 exprimée dans Escherichia coli (E. coli) et a été mentionnée dans 5+ publications.

Aperçu rapide pour BMP2 Protein (Homodimer) (ABIN1589575)

Antigène: BMP2 (Bone Morphogenetic Protein 2 (BMP2))

Type de proteíne: Recombinant

Activité biologique: Active

Origine: Humain

Source: Escherichia coli (E. coli)

Pureté: > 95 % by SDS-PAGE. Visualized by silver stain

Détail du produit

Attributs du protein: Homodimer

Séquence: MQAKHKQRKR LKSSCKRHPL YVDFSDVGWN DWIVAPPGYH AFYCHGECPF PLADHLNSTN HAIVQTLVNS VNSKIPKACC VPTELSAISM LYLDENEKVV LKNYQDMVVE GCGCR

Attributs du produit: Length (AA): 115
Chromosomal location: 20p12
Measured by the ability of BMP-2 to induce alkaline phosphatase production by C2C12 myogenic cells. The ED50 for this effect is typically 0.3-0.8 µg/mL.

niveau d'endotoxine: < 0.1 ng per mg of BMP-2

Information d'application

Commentaires:

Cytokines & Growth Factors

Restrictions: For Research Use only

Stockage

Format: Lyophilized

Reconstitution: The lyophilized BMP-2 is best soluble in 50 mM acetic acid at a concentration of 0.1 mg/mL but should be also soluble in most aqueous buffers when the pH is below 6.0.

Buffer: 50 mM acetic acid

Conseil sur la manipulation: Avoid repeated freeze-thaw cycles.

Stock: -20 °C/-80 °C

Stockage commentaire: Lyophilized samples are stable for greater than six months at -20 °C to -70 °C. Reconstituted BMP-2 should be stored in working aliquots at -20 °C.

Date de péremption: 6 months

Référence

Yao, Li, Xiong, Zeng, Xu, Wang: "Hollow hydroxyapatite microspheres/chitosan composite as a sustained delivery vehicle for rhBMP-2 in the treatment of bone defects." dans: Journal of materials science. Materials in medicine, Vol. 26, Issue 1, pp. 5336, (2015) (PubMed).

Schliephake, Rublack, Förster, Schwenzer, Reichert, Scharnweber: "Functionalization of titanium implants using a modular system for binding and release of VEGF enhances bone-implant contact in a rodent model." dans: Journal of clinical periodontology, Vol. 42, Issue 3, pp. 302-10, (2015) (PubMed).

Haversath, Hülsen, Böge, Tassemeier, Landgraeber, Herten, Warwas, Krauspe, Jäger: "Osteogenic differentiation and proliferation of bone marrow-derived mesenchymal stromal cells on PDLLA?+?BMP-2-coated titanium alloy surfaces." dans: Journal of biomedical materials research. Part A, (2015) (PubMed).

Suliman, Xing, Wu, Xue, Pedersen, Sun, Døskeland, Nickel, Waag, Lygre, Finne-Wistrand, Steinmüller-Nethl, Krueger, Mustafa: "Release and bioactivity of bone morphogenetic protein-2 are affected by scaffold binding techniques in vitro and in vivo." dans: Journal of controlled release : official journal of the Controlled Release Society, Vol. 197, pp. 148-57, (2014) (PubMed).

Wölfle, Fiedler, Dürselen, Reichert, Scharnweber, Förster, Schwenzer, Reichel, Ignatius, Brenner: "Improved anchorage of Ti6Al4V orthopaedic bone implants through oligonucleotide mediated immobilization of BMP-2 in osteoporotic rats." dans: PLoS ONE, Vol. 9, Issue 1, pp. e86151, (2014) (PubMed).

Détail du antigène

Antigène: BMP2 (Bone Morphogenetic Protein 2 (BMP2))

Autre désignation: BMP-2

Sujet: Human Bone Morphogenetic Protein-2 (BMP-2) is a disulfide-bonded homodimeric protein with an apparent molecular weight of 26 kDa. BMP-2 regulates similarly to its nearest homologue BMP-4 diverse fundamental processes during embryonic development: BMP-2 and other BMP proteins have great potential for medical therapeutic applications, in particular because they allow or at least accelerate the ossification of extensive bone lesions. The amino acid sequence of recombinant human BMP-2 starts with MQAKHKQ (position 283) containing the Met from the E. coli expression vector. BMP-2 is a heparin binding protein.
Synonyms: bone morphogenetic protein 2, BDA2, BMP2A, bone morphogenetic protein 4, ZYME, BMP2B, OFC11, BMP2B1, MCOPS6

Poids moléculaire: 26.0 kDa

NCBI Accession: NM_001200, NP_001191

UniProt: P12643

Pathways: Regulation of Hormone Metabolic Process, Regulation of Hormone Biosynthetic Process, Regulation of Muscle Cell Differentiation, Growth Factor Binding, Positive Regulation of fat Cell Differentiation