A4596
ANTI-FLAG® M1 Agarose Affinity Gel
동의어(들):
Anti-ddddk, Anti-dykddddk
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크기 선택
제품정보 (DICE 배송 시 비용 별도)
NACRES:
NA.32
UNSPSC Code:
12352203
Conjugate:
agarose conjugate
Species reactivity:
-
Application:
—
Citations:
81
conjugate
agarose conjugate
Quality Level
antibody product type
primary antibodies
form
suspension
isotype
IgG12b
capacity
≥0.6 mg/mL, gel binding capacity
storage temp.
−20°C
General description
ANTI-FLAG® M1 Agarose Affinity Gel is a purified IgG2B monoclonal antibody covalently attached to agarose.
Application
For purification of N-terminal FLAG fusion proteins. Since binding is Ca2+-dependent, proteins can be eluted with a buffer containing EDTA, as well as by the standard methods using either FLAG peptide or glycine-HCl buffer, pH 3. ANTI-FLAG M1 does not bind to Met-FLAG fusion proteins, so this resin is not appropriate for purifying unprocessed, cytoplasmically expressed fusion proteins.
Affinity gel is for calcium mediated purification of N-terminal FLAG fusion proteins.
immunoprecipitation (IP): suitable
Elution - FLAG peptide, Glycine, pH 3.5 EDTA
Learn more product details in our FLAG® application portal.
Affinity gel is for calcium mediated purification of N-terminal FLAG fusion proteins.
immunoprecipitation (IP): suitable
Elution - FLAG peptide, Glycine, pH 3.5 EDTA
Learn more product details in our FLAG® application portal.
Biochem/physiol Actions
Binding specificity: Free N-Terminus of FLAG sequence
N-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-C
N-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-C
Features and Benefits
- Typically purify fusion proteins from crude lysates to single band purity in just one chromatography step.
- Fusion protein may be eluted from affinity resin by mild elution with EDTA.
- A solution of FLAG peptide can be used for gentle, non-denaturing elution of FLAG fusion proteins.
Physical form
Suspension of beaded agarose in 50% glycerol containing 10 mM sodium phosphate, 150 mM NaCl, pH 7.4, 0.02% (w/v) sodium azide
Other Notes
ANTI-FLAG® M1 does not bind to Met-FLAG fusion proteins, so this resin is not appropriate for purifying unprocessed, cytoplasmically expressed fusion proteins.
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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저장 등급
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Ai Lu et al.
Biochemical and biophysical research communications, 513(3), 746-752 (2019-04-17)
Phosphoribosylformylglycinamidine synthase (PFAS) is an essential enzyme in de novo synthesis of purine. Previously, PFAS has been reported to modulate RIG-I activation during viral infection via deamidation. In this study, we sought to identify potential substrates that PFAS can deamidate.
E Di Zazzo et al.
TheScientificWorldJournal, 2014, 565839-565839 (2014-08-13)
Recent studies have shown that hyperinsulinemia may increase the cancer risk. Moreover, many tumors demonstrate an increased activation of IR signaling pathways. Phosphatidylinositol 3-kinase (PI3K) is necessary for insulin action. In epithelial cells, which do not express GLUT4 and gluconeogenic
Bo Zhou et al.
Journal of molecular endocrinology, 55(3), 231-243 (2015-09-17)
Progranulin (PGRN) has recently emerged as an important regulator for insulin resistance. However, the direct effect of PGRN in vivo and the underlying role of progranulin in adipose insulin resistance involving the autophagy mechanism is not fully understood. In this
Fenju Lai et al.
Chinese journal of cancer, 31(9), 440-448 (2012-08-03)
A recently identified protein, FAN1 (FANCD2-associated nuclease 1, previously known as KIAA1018), is a novel nuclease associated with monoubiquitinated FANCD2 that is required for cellular resistance against DNA interstrand crosslinking (ICL) agents. The mechanisms of FAN1 regulation have not yet
Yong-Feng Han et al.
Cell research, 24(12), 1445-1465 (2014-11-26)
The SU(VAR)3-9-like histone methyltransferases usually catalyze repressive histone H3K9 methylation and are involved in transcriptional gene silencing in eukaryotic organisms. We identified a putative SU(VAR)3-9-like histone methyltransferase SUVR2 by a forward genetic screen and demonstrated that it is involved in
관련 콘텐츠
Protein expression technologies for various expression systems supporting research, therapeutics, and vaccine production.
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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