BMP2 Protein (Homodimer)

Produktnummer ABIN1589575

Recombinant BMP2-Protein exprimiert in Escherichia coli (E. coli) und wurde in 5+ Publikationen erwähnt.

Kurzübersicht für BMP2 Protein (Homodimer) (ABIN1589575)

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

Protein-Typ: Recombinant

Biologische Aktivität: Active

Spezies: Human

Quelle: Escherichia coli (E. coli)

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

Produktdetails

Proteineigenschaft: Homodimer

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

Produktmerkmale: 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.

Endotoxin-Niveau: < 0.1 ng per mg of BMP-2

Anwendungsinformationen

Kommentare:

Cytokines & Growth Factors

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Lyophilized

Rekonstitution: 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

Handhabung: Avoid repeated freeze-thaw cycles.

Lagerung: -20 °C/-80 °C

Informationen zur Lagerung: 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.

Haltbarkeit: 6 months

Referenzen

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." in: 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." in: 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." in: 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." in: 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." in: PLoS ONE, Vol. 9, Issue 1, pp. e86151, (2014) (PubMed).

Antigendetails

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

Andere Bezeichnung: BMP-2

Hintergrund: 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

Molekulargewicht: 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