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M4786
Met-Gly-Met-Met
≥97%
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About This Item
Empirische Formel (Hill-System):
C17H32N4O5S3
CAS-Nummer:
Molekulargewicht:
468.65
MDL-Nummer:
UNSPSC-Code:
12352200
PubChem Substanz-ID:
Assay
≥97%
Form
solid
Methode(n)
cell culture | mammalian: suitable
Lagertemp.
−20°C
SMILES String
CSCCC(N)C(=O)NCC(=O)NC(CCSC)C(=O)NC(CCSC)C(O)=O
InChI
1S/C17H32N4O5S3/c1-27-7-4-11(18)15(23)19-10-14(22)20-12(5-8-28-2)16(24)21-13(17(25)26)6-9-29-3/h11-13H,4-10,18H2,1-3H3,(H,19,23)(H,20,22)(H,21,24)(H,25,26)
InChIKey
BOCWTHDHJPOLAY-UHFFFAOYSA-N
Amino Acid Sequence
Met-Gly-Met-Met
Biochem./physiol. Wirkung
Met-Gly-Met-Met is a peptide substrate.
Lagerklassenschlüssel
13 - Non Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
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Amino-terminal extension present in the methionine aminopeptidase type 1c of Mycobacterium tuberculosis is indispensible for its activity
Kanudia et al.
BMC Biochemistry, 12, online-online (2011)
Pavitra Kanudia et al.
BMC biochemistry, 12, 35-35 (2011-07-07)
Methionine aminopeptidase (MetAP) is a ubiquitous enzyme in both prokaryotes and eukaryotes, which catalyzes co-translational removal of N-terminal methionine from elongating polypeptide chains during protein synthesis. It specifically removes the terminal methionine in all organisms, if the penultimate residue is
Oswaldo Hernandez-Hernandez et al.
Journal of chromatography. A, 1428, 202-211 (2015-08-19)
This work explores the use of both hydrophilic interaction liquid chromatography (HILIC) and reverse phase liquid chromatography (RPLC) for the separation and subsequent characterization of bovine caseinomacropeptide (CMP) phosphopeptides and O-glycopeptides using a quadrupole-time-of-flight (QTOF) mass spectrometer with electrospray ionization.
Aline Marschner et al.
Biochimie, 115, 35-43 (2015-04-30)
Methionine aminopeptidases play a major role in posttranslational protein processing and are therefore promising targets for the discovery of novel therapeutical agents. We here describe the heterologous expression, purification, and characterization of recombinant Trypanosoma brucei methionine aminopeptidase, type 1 (TbMetAP1).
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