The cross reactivity of SRP6155 human BMP2 with rat has not been checked. However, literature indicates a high level of sequence homology between human and rat BMP2 (Freire et al., 2012; Freire et al., 2015) and VEGFA (Avivi et al., 1999; Ferrara, 2002) proteins. Accordingly, in many studies, human recombinant BMP2 and VEGFA have been used successfully in bone regeneration experiments in the rat (Park et al., 2003; Li et al., 2016). It is likely that SRP6155 should work with rat samples.
SRP6155
BMP-2 human
recombinant, expressed in HEK 293 cells, ≥95% (SDS-PAGE)
Sinónimos:
BMP-2A, Bone morphogenetic protein 2, Bone morphogenetic protein 2A
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About This Item
Código UNSPSC:
12352202
NACRES:
NA.32
En este momento no podemos mostrarle ni los precios ni la disponibilidad
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origen biológico
human
recombinante
expressed in HEK 293 cells
Ensayo
≥95% (SDS-PAGE)
Formulario
lyophilized
potencia
20-100 ng/mL ED50
mol peso
30-38 kDa (homodimer, glycosylated)
envase
pkg of 10 μg
técnicas
cell culture | mammalian: suitable
Nº de acceso NCBI
Condiciones de envío
dry ice
temp. de almacenamiento
−70°C
Información sobre el gen
human ... BMP2(650)
Descripción general
BMP2 (bone morphogenetic protein 2) belongs to the transforming growth factor-β (TGFβ) superfamily. BMP-2 is expressed in a variety of tissues such as lung, spleen, brain, liver, prostate ovary, and small intestine.[1] BioVision′s BMP-2 is produced in a serum-free, chemically defined media. Production in human 293 cells offers authentic glycosylation, contributing to stability in cell growth media and other applications.BMP2 is a candidate gene for the autosomal dominant disease of fibrodysplasia (myositis) ossificans progressiva.
Aplicación
BMP-2 human has been used to study the biological role of it on adult renal progenitor cells under in vitro and in vivo conditions.[2]
Acciones bioquímicas o fisiológicas
BMPs (bone morphogenetic proteins) promote and regulate bone development, growth, remodeling and repair, in both prenatal development and postnatal growth of eye, heart, kidney, skin, and other tissues.[3] During bone repair, BMP-2 controls the expression of Runt-related transcription factor 2 (Runx2) and Osterix (Osx), thereby enhancing migration, proliferation and osteogenic differentiation of mesenchymal stem cells.[4] In addition to its osteogenic activity, BMP-2 also plays an important role in cardiac morphogenesis.[5]
Forma física
Lyophilized from a solution of 50 mM sodium acetate, pH 4.5, with 50 mM NaCl.
Nota de preparación
Centrifuge the vial prior to opening.
Reconstitución
Reconstitute in sterile PBS containing 0.1% endotoxin-free, recombinant human serum albumin.
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
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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
Rick Visser et al.
Tissue engineering. Part A, 20(1-2), 34-44 (2013-07-19)
Osteogenesis is a complex, multifactorial process in which many different signals interact. The bone morphogenetic proteins (BMPs) are the most potent inducers of osteoblastic differentiation, although very high doses of BMPs in combination with collagen type I formulations have to
Ivo Dumic-Cule et al.
International orthopaedics, 38(9), 1979-1985 (2014-07-18)
Bone morphogenetic protein (BMP)-2 and -7 are used in patients with long-bone fractures, nonunions and spinal fusions. It is unknown whether their potential systemic bioavailability following local bone administration might affect skeletal metabolism. To answer this question, we examined effects
BMP-2 induces a profibrotic phenotype in adult renal progenitor cells through Nox4 activation.
Simone S, et al.
American Journal of Physiology: Renal Physiology, 303, F23-F34 (2012)
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
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Could you please provide information on the cross-reactivity of SRP6155 with rats?
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