M4786
Met-Gly-Met-Met
≥97%
Sign In to View Organizational & Contract Pricing.
Select a Size
About This Item
Empirical Formula (Hill Notation):
C17H32N4O5S3
CAS Number:
Molecular Weight:
468.65
UNSPSC Code:
12352200
PubChem Substance ID:
MDL number:
assay
≥97%
form
solid
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)
SMILES string
CSCCC(N)C(=O)NCC(=O)NC(CCSC)C(=O)NC(CCSC)C(O)=O
InChI key
BOCWTHDHJPOLAY-UHFFFAOYSA-N
technique(s)
cell culture | mammalian: suitable
storage temp.
−20°C
Biochem/physiol Actions
Met-Gly-Met-Met is a peptide substrate.
Storage Class
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
新产品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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).
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service