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A propos de cet article
Form:
liquid
Mol wt:
~49 kDa
Service technique
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Laissez-nous vous aiderGeneral description
Carboxy-terminal FLAG-BAP Fusion Protein is a 466 amino acid C-terminal FLAG fusion protein of E.coli bacterial alkaline phosphatase (BAP).
Application
Carboxy-terminal FLAG-BAP™ Fusion Protein has been used in the immunoprecipitation of the reporter protein in human embryonic kidney (HEK) cell lysate and as a FLAG-tagged control protein in solid-phase binding assay of spermatogenic immunoglobulin superfamily protein (SgIGSF).
Learn more product details in our FLAG® application portal.
Biochem/physiol Actions
The FLAG sequence comprises of the eight-amino acid sequence AspTyrLysAspAspAspAspLys and is hydrophilic. FLAG fusion proteins are expressed in bacterial, yeast and mammalian cells. FLAG epitope-tagged bacterial alkaline phosphatase is employed in immunoaffinity purification. Alkaline phosphatase based fusion protein have wide clinical applications in immunodetection, enzyme immunoassay and enzyme-linked immunosorbent assay.
Physical form
Supplied in 10 mM Tris, 120 mM NaCl, 0.05 mM ZnCl2
Preparation Note
Dilute the ANTI-FLAG M2 antibody solution to 10 mg/ml
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
Classe de stockage
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Contenu apparenté
Instructions
Cloning of a soluble isoform of the SgIGSF adhesion molecule that binds the extracellular domain of the membrane-bound isoform
Koma Y, et al.
Oncogene, 23(33), 5687-5687 (2004)
Vectors for expression and secretion of FLAG epitope-tagged proteins in mammalian cells
Chubet RG and Brizzard BL
Biotechniques, 20(1), 136-141 (1996)
Eldie Berger et al.
Microbial cell factories, 10, 62-62 (2011-08-05)
Through modification of the flagellin type III secretion pathway of Bacillus halodurans heterologous peptides could be secreted into the medium as flagellin fusion monomers. The stability of the secreted monomers was significantly enhanced through gene-targeted inactivation of host cell extracellular