B2787

Sigma

 

Biotinylated Molecular Weight Marker

mol wt 6,500-180,000 Da

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Description

ComponentsThis product contains:
• α2-macroglobulin (human plasma)
• β-galactosidase (E. coli)
• phosphorylase b (rabbit muscle)
• catalase (bovine liver)
• alcohol dehydrogenase (equine liver)
• carbonic anhydrase (bovine erythrocyte)
• trypsin inhibitor (soy bean)
• lysozyme (chicken egg)
• aprotinin (bovine lung)

Each vial contains approximately 33% protein, 33% NaCl and 33% sucrose.
ApplicationFor SDS-PAGE and protein transfer, the Biotinylated Molecular Weight Standard Mixture contains proteins, which have been biotin conjugated for use as SDS-PAGE standards for the estimation of the molecular weights of blotted proteins.1 Visualization is accomplished using streptavidin-peroxidase (Cat. No. S5512) and a color development reagent such as 4-Chloro-1-naphthol (Cat. No. C8890), eliminating the need to cut out separate lanes for general protein stains and can be performed simultaneously with immunostaining procedures. These standards may be used with either the Laemmli2 or the Weber and Osborn3, SDS-PAGE procedures.
Other NotesContains nine biotinylated proteins (approx 0.1 mg total).
ReconstitutionEach vial is reconstituted with 1 mL of 1x sample buffer (Cat. No. S3401) and incubated for 2-3 minutes at 100 °C.

Properties

formlyophilized powder
usage vial sufficient for 200 applications (on 10 cm × 10 cm mini gels)
mol wtmol wt 6,500-180,000 Da
packagingvial of 0.1 mg protein (also contains 0.1 mg NaCl and 0.1 mg sucrose)
storage temp.−20°C

Safety

Hazard CodesB
WGK Germany2

References

Cited Reference1. Della-Penna, D., Christoffersen, R., Bennett, A.,, Biotinylated proteins as molecular weight standards on western blots. Anal. Biochem. 152, 329-332, (1986) Abstract
 2. Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685, (1970) Abstract
 3. Weber, K. and Osborn, M., The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244, 4406-4412, (1969) Abstract