P7457
Carboxy-terminal FLAG-BAP™ Fusion Protein
Sign In to View Organizational & Contract Pricing.
Select a Size
Change View
About This Item
Form:
liquid
Mol wt:
~49 kDa
General 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
Storage Class
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)
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Related Content
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)
Patricia L Pelczar et al.
Journal of bacteriology, 190(16), 5635-5641 (2008-06-17)
GerD of Bacillus subtilis is a protein essential for normal spore germination with either L-alanine or a mixture of L-asparagine, D-glucose, D-fructose, and potassium ions. GerD's amino acid sequence suggests that it may be a lipoprotein, indicating a likely location
Maddalena de Virgilio et al.
Journal of experimental botany, 59(10), 2815-2829 (2008-06-10)
Protein bodies (PB) are stable polymers naturally formed by certain seed storage proteins within the endoplasmic reticulum (ER). The human immunodeficiency virus negative factor (Nef) protein, a potential antigen for the development of an anti-viral vaccine, is highly unstable when