Accéder au contenu
Merck
Toutes les photos(1)

Key Documents

SRP3326

Sigma-Aldrich

BMP-2 human

Animal-component free, recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC)

Synonyme(s) :

BMP-2A

Se connecterpour consulter vos tarifs contractuels et ceux de votre entreprise/organisme


About This Item

Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32

Source biologique

human

Produit recombinant

expressed in E. coli

Pureté

≥98% (HPLC)
≥98% (SDS-PAGE)

Forme

lyophilized

Poids mol.

26.0 kDa

Conditionnement

pkg of 10 μg

Impuretés

endotoxin, tested

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

−20°C

Informations sur le gène

human ... BMP2(650)

Description générale

The functional form of BMP-2 (bone morphogenetic protein 2) is a 26kDa protein composed of two identical 114 amino-acid polypeptide chains (monomers) linked by a single disulfide bond. Each BMP-2 monomer is expressed as the C-terminal part of a precursor polypeptide, which also contains a 23 amino-acid signal sequence for secretion, and a 259 amino-acid propeptide. After dimerization of this precursor, the covalent bonds between the propeptide (which is also a disulfide-linked homodimer) and the mature BMP-2 ligand are cleaved by a furin-type protease. Recombinant human BMP-2 is a 26kDa homodimeric disulfide-linked protein consisting of two identical 115 amino acid chains.

Application

BMP-2 human has been used to study the biological role of BMP-2 on adult renal progenitor cells under in vitro and in vivo conditions.

Actions biochimiques/physiologiques

BMP-2 (bone morphogenetic protein 2) is a potent osteoinductive cytokine, capable of inducing bone and cartilage formation in association with an osteoconductive carrier such as collagen and synthetic hydroxyapatite. During bone repair, it controls the expression of Runt-related transcription factor 2 (Runx2) and Osterix (Osx), thereby enhancing migration, proliferation and osteogenic differentiation of mesenchymal stem cells. In addition to its osteogenic activity, BMP-2 appears to play an important role in cardiac morphogenesis, and is expressed in a variety of other tissues including lung, liver, spleen, prostate, ovary, and small intestine.

Forme physique

Lyophilized from 0.1% TFA.

Reconstitution

Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

Déjà en possession de ce produit ?

Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Les clients ont également consulté

Bone morphogenetic proteins: multifunctional regulators of vertebrate development.
Hogan BL
Genes & Development, 10, 1580-1594 (1996)
A role for bone morphogenetic proteins in the induction of cardiac myogenesis.
Schultheiss TM, et al.
Genes & Development, 11, 451-462 (1997)
Vera Hintze et al.
Biomacromolecules, 15(8), 3083-3092 (2014-07-17)
Sulfated glycosaminoglycans (GAGs) can direct cellular processes by interacting with proteins of the extracellular matrix (ECM). In this study we characterize the interaction profiles of chemically sulfated hyaluronan (HA) and chondroitin sulfate (CS) derivatives with bone morphogenetic protein-2 (BMP-2) and
Bone regeneration with low dose BMP-2 amplified by biomimetic supramolecular nanofibers within collagen scaffolds.
Lee SS, et al.
Biomaterials, 34, 452-459 (2013)
Nam Hee Kim et al.
Biomaterials, 35(37), 9888-9896 (2014-09-15)
Though growth factors allow tissue regeneration, the trade-off between their effectiveness and adverse effects limits clinical application. The key issues in current growth factor therapy largely derive from initial burst pharmacokinetics, rapid clearance, and proteolytic cleavage resulting in clinical ineffectiveness

Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..

Contacter notre Service technique