P7582
Amino-terminal FLAG-BAP™ Fusion Protein
Synonym(s):
Amino-terminal Fusion Protein, BAP Fusion Protein, FLAG-BAP Fusion Protein
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About This Item
Form:
liquid
Mol wt:
~49 kDa
General description
Amino-terminal FLAG-BAP™ Fusion Protein is a 467 amino acid N-terminal FLAG fusion protein of E. coli bacterial alkaline phosphatase (BAP) with a calculated molecular mass of 49.3kDa. The N-terminal FLAG-BAP Fusion Protein migrates as a 45−55kDa band by SDS-PAGE depending on electrophoresis conditions. FLAG-BAP™ Fusion Protein has biotechnological applications and is used in the screening of recombinant fusion proteins.
The Amino-terminal FLAG-BAP Fusion Protein is a control prorein used to confirm the funtional integrity of the anti-FLAG M1 and M2 monoclonal antibodies in applications such as western blotting, immunoprecipitation, ELISA, electron microscopy, and FACS.
Application
Amino-terminal FLAG-BAP™ Fusion Protein has been used as a standard in enzyme-linked immunosorbent assay (ELISA) for osteopontin quantification and in western blotting based quantification of Flag-Wnt8 and Drosophila melanogaster transcription factor interactome.
Learn more product details in our FLAG® application portal.
Physical form
Protein is supplied in 10 mM Tris, 120 mM NaCl,
0.05 mM ZnCl2 in 50% glycerol, pH 8.0.
0.05 mM ZnCl2 in 50% glycerol, pH 8.0.
Other Notes
Control protein
Legal Information
FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany
FLAG-BAP is a trademark of Sigma-Aldrich Co. LLC
Storage Class
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Related Content
Instructions
BAP-fusion: A versatile molecular probe for biotechnology research
Biotechnology: Research, Technology and Applications, 327-345 (2008)
A Comprehensive Drosophila melanogaster Transcription Factor Interactome
Shokri L, et al.
Cell Reports, 27(3), 955-970 (2019)
Exploring the separation power of mixed-modal resins for purification of recombinant osteopontin from clarified Escherichia coli lysates
Guo S, et al.
Biotechnology Progress, 35(1), e2722-e2722 (2019)