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Merck

A2220

ANTI-FLAG® M2 Affinity Gel

purified immunoglobulin, buffered aqueous glycerol solution

동의어(들):

Monoclonal ANTI-FLAG® M2, ANTI-FLAG® M2 Affinity Agarose Gel, Anti-ddddk, Anti-dykddddk

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크기 선택

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제품정보 (DICE 배송 시 비용 별도)

NACRES:
NA.32
UNSPSC Code:
12352203
Conjugate:
agarose conjugate
Clone:
M2, monoclonal
Application:
IP, affinity chromatography
Citations:
1232
기술 서비스
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conjugate

agarose conjugate

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

M2, monoclonal

form

buffered aqueous glycerol solution

analyte chemical class(es)

proteins

technique(s)

affinity chromatography: suitable, immunoprecipitation (IP): suitable

matrix

(4% agarose bead; 45-165μm bead size)

isotype

IgG1

capacity

>0.6 mg/mL, resin binding capacity (FLAG-BAP)

shipped in

wet ice

storage temp.

−20°C

General description

Anti-FLAG M2 Affinity gel is a mouse monoclonal antibody that is covalently attached to agarose. The antibody binds FLAG at the N-terminal, Met-N-terminal, C-terminal and internal locations of fusion proteins. Binding is calcium-independent.

Elution - FLAG® peptide, Glycine, pH 3.5, 3x FLAG® peptide
FLAG® peptide, Glycine, pH3.5, 3x FLAG® peptide

Immunogen

DYKDDDDK

Application

Anti-FLAG® M2 affinity gel has been used for western blotting, immunoprecipitation and for the purification of FLAG fusion proteins.

Learn more product details in our FLAG® application portal.

Physical form

Suspension in buffered saline containing azide as preservative and 50% glycerol

Legal Information

ANTI-FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany
FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

FLAG® tag, 3x FLAG®, DYKDDDDK tag


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저장 등급

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable



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시험 성적서(COA)

Lot/Batch Number

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문서 라이브러리 방문


프로토콜

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

문서

The FLAG® Expression System is a proven method to express, purify and detect recombinant fusion proteins. Sigma®, the proven provider of FLAG®, now offers a magnetic bead for immunoprecipitation, protein purification, and the study of protein-protein interactions. The ANTI-FLAG® M2 Magnetic Bead is composed of murine derived, anti-FLAG® M2 monoclonal antibody attached to superparamagnetic iron impregated 4% agarose beads, with an average diameter of 50 µm. The M2 antibody is capable of binding to fusion proteins containing a FLAG peptide sequence at the N-terminus, Met-N-terminus, or C-terminus locations in mammalian, bacterial, and plant extracts.

관련 콘텐츠

이온교환, 크기 배제 및 단백질 친화성 크로마토그래피를 포함한 방법을 사용하는 재조합형 단백질 정제를 위한 단백질 정제 기법, 시약 및 프로토콜.

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

관련 콘텐츠 모두 보기

Nora Nonne et al.
Nucleic acids research, 38(4), e20-e20 (2009-12-04)
MicroRNAs (miRNAs) bind to Argonaute proteins, and together they form the RISC complex and regulate target mRNA translation and/or stability. Identification of mRNA targets is key to deciphering the physiological functions and mode of action of miRNAs. In mammals, miRNAs
Yu Ti Cheng et al.
Proceedings of the National Academy of Sciences of the United States of America, 108(35), 14694-14699 (2011-08-30)
The nucleotide-binding domain and leucine-rich repeats containing proteins (NLRs) serve as immune receptors in both plants and animals. Overaccumulation of NLRs often leads to autoimmune responses, suggesting that the levels of these immune receptors must be tightly controlled. However, the
William G Roach et al.
The Biochemical journal, 403(2), 353-358 (2007-02-06)
Insulin stimulation of the trafficking of the glucose transporter GLUT4 to the plasma membrane is controlled in part by the phosphorylation of the Rab GAP (GTPase-activating protein) AS160 (also known as Tbc1d4). Considerable evidence indicates that the phosphorylation of this