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Merck
CN

P7457

Carboxy-terminal FLAG-BAP™ Fusion Protein

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.32
MDL number:
MFCD00130921

Key Documents

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form

liquid

mol wt

~49 kDa

shipped in

dry ice

storage temp.

−20°C

Quality Level

200

Related Categories

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.

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).

Other Notes

Control protein

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

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)

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
0000471339
0000471339
SLCB6701
SLBH7385V
SLBF9427V

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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
Microbial alkaline phosphatases in bioprocessing
Nalini P, et al.
International Journal of Current Microbiology and Applied Sciences, 4(3), 384-396 (2015)
Improved methodology for the affinity isolation of human protein complexes expressed at near endogenous levels
Domanski M, et al.
Biotechniques, 1-1 (2012)
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)
View All Related Papers

Articles

Anti-FLAG® M2 Magnetic Beads

Comparison of elution techniques for small-scale protein purification of FLAG® tag proteins using anti-FLAG® M2 magnetic beads.

Anti-FLAG® M2磁珠

比较anti-FLAG® M2磁珠的小规模FLAG®标签蛋白纯化的不同洗脱方法。

Protocols

Immunoprecipitation of FLAG Fusion Proteins Using Monoclonal Antibody Affinity Gels

Protocol for immunoprecipitation (IP) of FLAG fusion proteins using M2 monoclonal antibody 4% agarose affinity gels

采用单克隆抗体亲和凝胶进行的FLAG融合蛋白免疫沉淀_蛋白纯化-默克生命科学

免疫沉淀（IP）可用于高效、高产量分离和纯化与FLAG®肽标签融合的蛋白质。此过程采用ANTI-FLAG® M2亲和凝胶进行，后者是一种与琼脂糖树脂共价结合的高度特异性单克隆抗体。

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蛋白表达_重组蛋白_蛋白质生物学-默克生命科学

默克分享基因组学、克隆学和大量分子生物学技术的发展使研究人员能在众多生物系统中表达异源蛋白。表达重组蛋白的能力为研究人员提供了广泛而强大的下游应用空间，以便进一步开展研究。

蛋白纯化

用于纯化重组蛋白的蛋白纯化技术、试剂和方法包括离子交换、排阻层析和蛋白亲和层析。

Protein Expression

Protein expression technologies for various expression systems supporting research, therapeutics, and vaccine production.

Protein Purification

Protein purification techniques, reagents, and protocols for purifying recombinant proteins using methods including, ion-exchange, size-exclusion, and protein affinity chromatography.

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