Összes fotó(1)
Fontos dokumentumok
H7425
Anti-FLAG®-Peroxidase antibody produced in rabbit
IgG fraction of antiserum
Szinonimák:
Anti-FLAG-HRP Polyclonal Conjugate
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(1)
About This Item
UNSPSC kód:
12352203
NACRES:
NA.43
technika/technikák:
western blot: 1:2000-1:4000 using for detection of amino-terminal FLAG-BAP fusion protein in an E. coli crude cell lysate
application:
WB
citations:
4
Javasolt termékek
Minőségi szint
leírás
buffered aqueous solution
Forma
lyophilized solid
technika/technikák
western blot: 1:2000-1:4000 using for detection of amino-terminal FLAG-BAP fusion protein in an E. coli crude cell lysate
kiszállítva
dry ice
tárolási hőmérséklet
−20°C
Általános leírás
Anti-FLAG antibody is developed in rabbits using purified FLAG fusion protein as immunogen. Whole antiserum is purified using protein A immobilized on agarose to provide the IgG fraction of the antiserum and is conjugated to horseradish peroxidase.
ANTI-FLAG recognizes the FLAG epitope located on FLAG fusion proteins. The antibody reacts with N-terminal, N-terminal-Met, and C-terminal FLAG fusion proteins by immunoblotting. Specific staining is inhibited by the FLAG peptide (N-Asp-Tyr-Lys-Asp-AspAsp-Asp-Lys-C). Applications for the conjugate include Western blots and ELISA.
Epitope tags provide a method to localize gene products in a variety of cell types, study the topology of proteins and protein complexes, identify associated proteins, and characterize newly identified, low abundance, or poorly immunogenic proteins when protein specific antibodies are not available. Tagging with the FLAG peptide sequence may be done at the N-terminus, N-terminus preceded by a methionine residue, C-terminus, or at internal positions of the target protein. FLAG may also be placed in association with other tags. The small size of the FLAG tag or sequence and its high hydrophilicity tend to decrease the possibility of interference with the protein expression, proteolytic maturation, antigenicity, and function. The N-terminal FLAG peptide sequence contains a unique enterokinase cleavage site allowing it to be completely removed from the purified fusion proteins. Cleavage catalyzed by Cu2+ ions of the C-terminal FLAG peptide from a fusion protein has been reported. A sequence motif with five out of eight amino acid residues identical to the FLAG peptide is found in both rat and mouse Mg2+ dependent protein β-phosphatase, as well as in the human and bovine enzyme.
ANTI-FLAG recognizes the FLAG epitope located on FLAG fusion proteins. The antibody reacts with N-terminal, N-terminal-Met, and C-terminal FLAG fusion proteins by immunoblotting. Specific staining is inhibited by the FLAG peptide (N-Asp-Tyr-Lys-Asp-AspAsp-Asp-Lys-C). Applications for the conjugate include Western blots and ELISA.
Epitope tags provide a method to localize gene products in a variety of cell types, study the topology of proteins and protein complexes, identify associated proteins, and characterize newly identified, low abundance, or poorly immunogenic proteins when protein specific antibodies are not available. Tagging with the FLAG peptide sequence may be done at the N-terminus, N-terminus preceded by a methionine residue, C-terminus, or at internal positions of the target protein. FLAG may also be placed in association with other tags. The small size of the FLAG tag or sequence and its high hydrophilicity tend to decrease the possibility of interference with the protein expression, proteolytic maturation, antigenicity, and function. The N-terminal FLAG peptide sequence contains a unique enterokinase cleavage site allowing it to be completely removed from the purified fusion proteins. Cleavage catalyzed by Cu2+ ions of the C-terminal FLAG peptide from a fusion protein has been reported. A sequence motif with five out of eight amino acid residues identical to the FLAG peptide is found in both rat and mouse Mg2+ dependent protein β-phosphatase, as well as in the human and bovine enzyme.
Immunogén
purified FLAG fusion protein
Alkalmazás
For immunoblotting, with 1:2000 – 1:4000 as an initial suggested dilution
Browse additional application references in our FLAG® Literature FLAG® Literature portal.
Browse additional application references in our FLAG® Literature FLAG® Literature portal.
Fizikai forma
Lyophilized powder
Jogi információk
FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany
Jogi nyilatkozat
For Research use only. Not for drug, household, or other uses. Please consult the Safety Data Sheet for information regarding hazards and safe handling practices.
Figyelmeztetés
Danger
Figyelmeztető mondatok
Óvintézkedésre vonatkozó mondatok
Veszélyességi osztályok
Aquatic Chronic 3 - Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - Skin Sens. 1
Tárolási osztály kódja
11 - Combustible Solids
WGK
WGK 3
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R G Chubet et al.
BioTechniques, 20(1), 136-141 (1996-01-01)
The FLAG peptide, AspTyrLysAspAspAspAspLys, has been used as an epitope tag in a variety of cell types. The modification of the cytomegalovirus (CMV) promoter containing vector, pCMV5, to create two transient expression vectors designed for secretion and intracellular expression of
A S Robeva et al.
Biochemical pharmacology, 51(4), 545-555 (1996-02-23)
An expression plasmid for mammalian cells (CLDN10B) has been modified to add nucleotides encoding hexahistidine and the FLAG peptide (H/F) to cDNAs. The new mammalian expression plasmid has been named pDoubleTrouble (pDT). The plasmid and a recombinant baculovirus were used
D P Humphreys et al.
Protein engineering, 12(2), 179-184 (1999-04-09)
The peptide sequence (N)DKTH(C) was investigated as a site for efficient, specific cleavage of a fusion protein by cupric ions using a humanised gamma1 Fab' as a model protein. The native upper hinge (N)DKTH(C) sequence was mutated to create a
K Schäfer et al.
Biochemical and biophysical research communications, 207(2), 708-714 (1995-02-15)
The FLAG peptide has been widely used as a multi-purpose tag for the identification and detection of recombinant FLAG fusion proteins. The practicability of this approach depends on specific detection of FLAG fusion proteins with no or very little cross-reactivity
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