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Merck
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Key Documents

P7457

Sigma-Aldrich

Carboxy-terminal FLAG-BAP Fusion Protein

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About This Item

Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32

Forme

liquid

Niveau de qualité

Poids mol.

~49 kDa

Conditions d'expédition

dry ice

Température de stockage

−20°C

Description générale

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.

Actions biochimiques/physiologiques

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.

Autres remarques

Control protein

Forme physique

Supplied in 10 mM Tris, 120 mM NaCl, 0.05 mM ZnCl2

Notes préparatoires

Dilute the ANTI-FLAG M2 antibody solution to 10 mg/ml

Informations légales

FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany
FLAG-BAP is a trademark of Sigma-Aldrich Co. LLC

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Vectors for expression and secretion of FLAG epitope-tagged proteins in mammalian cells
Chubet RG and Brizzard BL
Biotechniques, 20(1), 136-141 (1996)
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)
David O McDonald et al.
Journal of molecular medicine (Berlin, Germany), 87(10), 971-980 (2009-08-12)
Thyroid peroxidase (TPO) is the key enzyme in thyroid hormone production and a universal autoantigen in Graves' and other autoimmune thyroid diseases. We wished to explore the expression of TPO and whether it was affected by thionamide antithyroid drugs. We
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
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

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