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Merck

P7457

Carboxy-terminal FLAG-BAP Fusion Protein

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UNSPSC Code:
12352202
NACRES:
NA.32
MDL number:
Form:
liquid
Mol wt:
~49 kDa
Servicio técnico
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form

liquid

Quality Level

mol wt

~49 kDa

shipped in

dry ice

storage temp.

−20°C

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


Clase de almacenamiento

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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Contenido relacionado

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)
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