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F3290

Millipore

FLAG® Peptide

≥85% (HPLC), lyophilized powder

Synonym(s):

Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys, ddddk peptide, dykddddk peptide

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About This Item

Empirical Formula (Hill Notation):
C41H60N10O20
Molecular Weight:
1012.97
MDL number:
MFCD02262135
UNSPSC Code:
12352202
PubChem Substance ID:
329799698
NACRES:
NA.32

product name

FLAG® Peptide, lyophilized powder

assay

≥85% (HPLC)

Quality Level

200

form

lyophilized powder

mol wt

1012.97 Da

shipped in

wet ice

storage temp.

2-8°C

SMILES string

NCCCC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@@H](N)CC(O)=O)C(O)=O

InChI

1S/C41H60N10O20/c42-11-3-1-5-22(45-36(65)24(13-19-7-9-20(52)10-8-19)47-34(63)21(44)14-29(53)54)35(64)48-26(16-31(57)58)38(67)50-28(18-33(61)62)40(69)51-27(17-32(59)60)39(68)49-25(15-30(55)56)37(66)46-23(41(70)71)6-2-4-12-43/h7-10,21-28,52H,1-6,11-18,42-44H2,(H,45,65)(H,46,66)(H,47,63)(H,48,64)(H,49,68)(H,50,67)(H,51,69)(H,53,54)(H,55,56)(H,57,58)(H,59,60)(H,61,62)(H,70,71)/t21-,22-,23-,24-,25-,26-,27-,28-/m0/s1

InChI key

XZWYTXMRWQJBGX-VXBMVYAYSA-N

General description

The FLAG peptide is used for the competitive elution of amino-terminal, Met-amino-terminal or carboxy-terminal FLAG fusion proteins from the Anti-FLAG M1 or Anti-FLAG M2 antibody (in solution or bound to an agarose gel).

Application

Gently elutes FLAG fusion proteins from ANTI-FLAG® M1 and M2 affinity resins. Usual working concentration is 100 μg/ml. Will not elute 3X FLAG fusion proteins. For this application, use 3X FLAG Peptide, F4799.

Learn more product details in our FLAG® application portal.

Preparation Note

For stock solution, dissolve in TBS (10mM Tris HCL, 150 mM NaCl, pH7.4) to a final concentration of 5 mg/mL.

Other Notes

2024 CiteAb Award Winner for Supplier Succeeding in Parkinson′s Research

Legal Information

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

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Omar H Vandal et al.
Nature medicine, 14(8), 849-854 (2008-07-22)
Acidification of the phagosome is considered to be a major mechanism used by macrophages against bacteria, including Mycobacterium tuberculosis (Mtb). Mtb blocks phagosome acidification, but interferon-gamma (IFN-gamma) restores acidification and confers antimycobacterial activity. Nonetheless, it remains unclear whether acid kills
Zheng Xu et al.
Molecular cell, 35(4), 426-441 (2009-09-01)
Accurate chromosome segregation during mitosis and meiosis depends on shugoshin proteins that prevent precocious dissociation of cohesin from centromeres. Shugoshins associate with PP2A, which is thought to dephosphorylate cohesin and thereby prevent cleavage by separase during meiosis I. A crystal
Kenjiro Hanaoka et al.
Magnetic resonance imaging, 26(5), 608-617 (2008-02-01)
Simple low molecular weight (MW) chelates of Gd(3+) such as those currently used in clinical MRI are considered too insensitive for most molecular imaging applications. Here, we evaluated the detection limit (DL) of a molecularly targeted low MW Gd(3+)-based T(1)
Tong Zhou et al.
Nucleic acids research, 33(1), 289-297 (2005-01-14)
Tyrosyl-DNA phosphodiesterase (TDP1) is a DNA repair enzyme that removes peptide fragments linked through tyrosine to the 3' end of DNA, and can also remove 3'-phosphoglycolates (PGs) formed by free radical-mediated DNA cleavage. To assess whether TDP1 is primarily responsible
Barbara G Mellone et al.
PLoS genetics, 7(5), e1002068-e1002068 (2011-05-19)
Semi-conservative segregation of nucleosomes to sister chromatids during DNA replication creates gaps that must be filled by new nucleosome assembly. We analyzed the cell-cycle timing of centromeric chromatin assembly in Drosophila, which contains the H3 variant CID (CENP-A in humans)
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