V900409
L-Lysine
Vetec™, reagent grade, ≥98%
Synonym(s):
(S)-2,6-Diaminocaproic acid
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About This Item
Recommended Products
grade
reagent grade
product line
Vetec™
Assay
≥98%
form
powder
reaction suitability
reaction type: solution phase peptide synthesis
color
white to off-white
mp
215 °C (dec.) (lit.)
SMILES string
NCCCC[C@H](N)C(O)=O
InChI
1S/C6H14N2O2/c7-4-2-1-3-5(8)6(9)10/h5H,1-4,7-8H2,(H,9,10)/t5-/m0/s1
InChI key
KDXKERNSBIXSRK-YFKPBYRVSA-N
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Legal Information
Vetec is a trademark of Merck KGaA, Darmstadt, Germany
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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Pharmaceutical research, 20(2), 237-246 (2003-03-15)
The purpose of this study was to demonstrate specific receptor-mediated targeting of phagocytes by functional surface coatings of microparticles, shielding from nonspecific phagocytosis and allowing ligand-specific interactions via molecular recognition. Coatings of the comb polymer poly(L-lysine)-g-poly(ethylene glycol) (PLL-g-PEG) were investigated
Neuropathology and applied neurobiology, 40(6), 670-685 (2014-04-23)
Loss of nuclear TDP-43 characterizes sporadic and most familial forms of amyotrophic lateral sclerosis (ALS). TDP-43 (encoded by TARDBP) has multiple roles in RNA processing. We aimed to determine whether (1) RNA splicing dysregulation is present in lower motor neurones
Oncotarget, 6(13), 11327-11341 (2015-04-11)
Large oncosomes (LO) are atypically large (1-10 µm diameter) cancer-derived extracellular vesicles (EVs), originating from the shedding of membrane blebs and associated with advanced disease. We report that 25% of the proteins, identified by a quantitative proteomics analysis, are differentially
Nature, 499(7457), 223-227 (2013-07-05)
The variant antigen Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1), which is expressed on the surface of P. falciparum-infected red blood cells, is a critical virulence factor for malaria. Each parasite has 60 antigenically distinct var genes that each code
Science (New York, N.Y.), 341(6145), 1238858-1238858 (2013-08-03)
Pathogens dramatically affect host cell transcription programs for their own profit during infection, but in most cases, the underlying mechanisms remain elusive. We found that during infection with the bacterium Listeria monocytogenes, the host deacetylase sirtuin 2 (SIRT2) translocates to
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