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Key Documents

M4786

Sigma-Aldrich

Met-Gly-Met-Met

≥97%

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About This Item

Empirical Formula (Hill Notation):
C17H32N4O5S3
CAS Number:
Molecular Weight:
468.65
MDL number:
UNSPSC Code:
12352200
PubChem Substance ID:

Assay

≥97%

form

solid

technique(s)

cell culture | mammalian: suitable

storage temp.

−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)

InChI key

BOCWTHDHJPOLAY-UHFFFAOYSA-N

Amino Acid Sequence

Met-Gly-Met-Met

Biochem/physiol Actions

Met-Gly-Met-Met is a peptide substrate.

Storage Class Code

13 - Non Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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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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