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A9469

Sigma-Aldrich

Monoclonal ANTI-FLAG® M2-Alkaline Phosphatase antibody produced in mouse

clone M2, purified immunoglobulin, buffered aqueous glycerol solution

Synonym(s):
Anti-ddddk, Anti-dykddddk, Monoclonal ANTI-FLAG® M2 antibody produced in mouse
NACRES:
NA.32

Quality Level

biological source

mouse

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

M2, monoclonal

form

buffered aqueous glycerol solution

species reactivity

all

concentration

~1 mg/mL

application(s)

indirect ELISA: 1:20,000

isotype

IgG1

immunogen sequence

DYKDDDDK

conjugate

alkaline phosphatase conjugate

shipped in

wet ice

storage temp.

−20°C

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General description

Monoclonal ANTI-FLAG® M2-Alkaline Phosphatase is a purified IgG 1 mouse antibody covalently conjugated to calf intestinal alkaline phosphatase (AP). The antibody conjugate binds to FLAG® fusion proteins and will recognize the FLAG® epitope at any position in the fusion protein (N-terminal, Met-N-terminal, C-terminal or internal FLAG® peptides).

Application

Monoclonal ANTI-FLAG® M2-Alkaline Phosphatase antibody produced in mouse has been used:
  • in direct tissue blot immunoassay of sweet orange petioles samples
  • in screening internalization of delta opioid receptor
  • for screening cell-free protein expression using ELISA

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

Physical form

Solution in Tris buffered saline containing 50% glycerol plus stabilizer and preservative

Legal Information

ANTI-FLAG is a registered trademark of Sigma-Aldrich Co. LLC
FLAG is a registered trademark of Sigma-Aldrich Co. LLC

Storage Class Code

12 - Non Combustible Liquids

WGK Germany

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

Integration of cell-free protein coexpression with an enzyme-linked immunosorbent assay enables rapid analysis of protein-protein interactions directly from DNA
Layton CJ and Helling HW
Protein Science, 20(8), 1432-1438 (2011)
Waithaka Mwangi et al.
Journal of leukocyte biology, 78(2), 401-411 (2005-04-29)
Induction of immune responses against microbial antigens using DNA is an attractive strategy to mimic the immunity induced by live vaccines. Although DNA vaccines are efficacious in murine models, the requirement for multiple immunizations using high doses in outbred animals...
Matthew T Doherty et al.
The Journal of biological chemistry, 287(47), 39369-39379 (2012-10-06)
Myb repeats ∼52 amino acid residues in length were first characterized in the oncogenic Myb transcription factor, which contains three tandem Myb repeats in its DNA-binding domain. Proteins of this family normally contain either one, two, or three tandem Myb...
Mun Kyoung Kim et al.
Molecular and cellular biology, 30(10), 2411-2423 (2010-03-10)
The small nuclear RNA (snRNA)-activating protein complex (SNAPc) is essential for transcription of genes coding for the snRNAs (U1, U2, etc.). In Drosophila melanogaster, the heterotrimeric DmSNAPc recognizes a 21-bp DNA sequence, the proximal sequence element A (PSEA), located approximately...
Beth A Rasala et al.
PloS one, 7(8), e43349-e43349 (2012-09-01)
Microalgae have recently received attention as a potential low-cost host for the production of recombinant proteins and novel metabolites. However, a major obstacle to the development of algae as an industrial platform has been the poor expression of heterologous genes...

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