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Recombinant Human BMP2

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Product Source Size Cat. No. Price
Recombinant Human BMP2 E. coli10 µg Z100085 $130.00
1.0 mg Z100089 $3,500.00
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Data Sheet
Print Version
Alternative Names BMP-2, BMP-2A
Recombinant Human Bone Morphogenetic Protein 2 (BMP2)
Description BMPs are proteins that act to induce the differentiation of mesenchymal-type cells into chondrocytes and osteoblasts before initiating bone formation. They promote the differentiation of cartilage-forming cells and bone-forming cells near sites of fractures but also at ectopic locations. Some of the proteins induce the synthesis of alkaline phosphatase and collagen in osteoblasts. Some BMPs act directly on osteoblasts and promote their maturation while at the same time suppressing myogenous differentiation. Other BMPs promote the conversion of typical fibroblasts into chondrocytes and are capable also of inducing the expression of an osteoblast phenotype in non-osteogenic cell types. Intracellular signaling following engagement of receptors for some BMP proteins has been shown to involve the action of SMAD proteins. BMP-2 wild type binds to its cellular receptors via two distinct binding epitopes. The large epitope 1 is responsible for the high-affinity binding to the BMPR-IA receptor, the smaller epitope 2 provides the low-affinity binding to the receptor BMPR-II. Recombinant Human Bone Morphogenetic Protein-2 is a homodimeric, non-glycosylated polypeptide chain containing two 115 amino acid subunits with a total molecular mass of 26kDa.
Gene Symbol BMP2
Gene ID 650
Accession No. P12643
Source E. coli
Appearance Lyophilized Powder
Molecular Weight 26.0 kDa
Endotoxin Level <1.0 EU/μg of recombinant protein as determined by the LAL method
Purity >95% as determined by SDS-PAGE
Bioactivity The ED50 as determined by its ability to induce alkaline phosphatase production by C2C12 myogenic cells was found to be less than 50 ng/mL
Formulation Lyophilized from a 0.2 μm filtered solution in 20 mM AcOH pH 6.5
Reconstitution A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.
Storage The lyophilized protein is stable for at least one year from date of receipt at -70°C. Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8°C for one month, or at -20°C for six months, with a carrier protein without detectable loss of activity. Avoid repeated freeze/thaw cycles.
Usage For research use only. Not for diagnostic or therapeutic use.
Product Documents
Product References
FAQs
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How are endotoxin levels measured?
1. For estimating the endotoxin levels; we use the LAL (Limulus Amebocyte Lysate) method: The lysate from horseshoe crab amebocytes clots in the presence of very low endotoxin. This reaction is the basis of the Limulus amebocyte lysate (LAL) assay which was approved by the FDA in 1970.

· Endotoxin is generally measured in Endotoxin Units per milliliter (EU/mL).

· For recombinant proteins: EU is reported per microgram of protein.

· One EU = 0.1-0.2 ng endotoxin/µg of protein.

· At abm, we do the LAL chromogenic assays that can detect down to 0.01 EU/ml.
With regard to the BSA levels in some Growth Factors and Cytokines, can you please provide an explanation as to why they are so high?
The amount of BSA, as part of the formulation of a protein, can vary considerably depending on how much BSA was deemed optimum/necessary for protein stability in combination with /in-lieu of - other possible additives. The aforementioned formulations are somewhat analogous to the “carrier” versions of many formulations from “R and D systems” that have as high as 50 µg of BSA per µg of the recombinant protein product. If, needed or desired, abm scientists can substitute BSA for other stabilizing additives for most formulations.
Are your Escherichia coli sourced growth factors: 1) Human derived materials free? 2) Recombinant proteins free?
Yes, all of abm's growth factors made in Escherichia coli using recombinant technology contain no human derived-products or other recombinant proteins. In the rare cases of BSA presence, this will be mentioned in the product's formulation.