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Merck

A9469

Sigma-Aldrich

ANTI-FLAG® M2 monoclonal antibody produced in mouse

clone M2, purified immunoglobulin, buffered aqueous glycerol solution

Sinónimos:

Anti-ddddk, Anti-dykddddk

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About This Item

UNSPSC Code:
41106514
NACRES:
NA.32

biological source

mouse

Quality Level

conjugate

alkaline phosphatase conjugate

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

M2, monoclonal

form

buffered aqueous glycerol solution

species reactivity

all

concentration

~1 mg/mL

technique(s)

indirect ELISA: 1:20,000

isotype

IgG1

immunogen sequence

DYKDDDDK

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... ALPL(249)

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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

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

Physical form

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

Legal Information

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

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

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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
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)
Beth A Rasala et al.
Plant biotechnology journal, 9(6), 674-683 (2011-05-04)
Microalgae have the potential to be a valuable biotechnological platform for the production of recombinant proteins. However, because of the complex regulatory network that tightly controls chloroplast gene expression, heterologous protein accumulation in a wild-type, photosynthetic-competent algal chloroplast remains low.
Seongjoon Kang et al.
Biology, 7(2) (2018-05-09)
Chlamydomonas reinhardtii (Chlamydomonas) strains that are toxic to mosquito larvae because they express chloroplast transgenes that are based on the mosquitocidal proteins of Bacillus thuringiensis subsp. israelensis (Bti) could be very useful in mosquito control. Chlamydomonas has several advantages for
M F Divin et al.
British journal of pharmacology, 156(7), 1044-1053 (2009-02-18)
Adenylyl cyclase sensitization occurs on chronic agonist activation of mu-opioid receptors and is manifested by an increase in cAMP levels (overshoot) on challenge with antagonist. It has been proposed that a long lasting constitutively active receptor is formed on chronic

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