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Merck

A4596

Millipore

ANTI-FLAG® M1 Agarose Affinity Gel

Szinonimák:

Anti-ddddk, Anti-dykddddk

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352203
NACRES:
NA.32

konjugátum

agarose conjugate

Minőségi szint

antitest terméktípus

primary antibodies

form

suspension

izotípus

IgG12b

kapacitás

≥0.6 mg/mL, gel binding capacity

tárolási hőmérséklet

−20°C

Általános leírás

ANTI-FLAG® M1 Agarose Affinity Gel is a purified IgG2B monoclonal antibody covalently attached to agarose.

Egyediség

Binding specificity: Free N-Terminus of FLAG sequence
N-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-C

Alkalmazás

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.

Tulajdonságok és előnyök

  • 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.

Fizikai forma

Suspension of beaded agarose in 50% glycerol containing 10 mM sodium phosphate, 150 mM NaCl, pH 7.4, 0.02% (w/v) sodium azide

Egyéb megjegyzések

ANTI-FLAG® M1 does not bind to Met-FLAG fusion proteins, so this resin is not appropriate for purifying unprocessed, cytoplasmically expressed fusion proteins.

Jogi információk

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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kapcsolódó termék

Product No.
Leírás
Árazás

Tárolási osztály kódja

10 - Combustible liquids

WGK

WGK 3

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

Már rendelkezik ezzel a termékkel?

Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

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
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
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
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

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