form
powder
color
white
storage temp.
−20°C
SMILES string
CC(O)=O.CC(C)C[C@H](N)C(=O)N[C@@H](CC(C)C)C(O)=O
InChI
1S/C12H24N2O3.C2H4O2/c1-7(2)5-9(13)11(15)14-10(12(16)17)6-8(3)4;1-2(3)4/h7-10H,5-6,13H2,1-4H3,(H,14,15)(H,16,17);1H3,(H,3,4)/t9-,10-;/m0./s1
InChI key
JEUHGRPWUPRNDP-IYPAPVHQSA-N
Amino Acid Sequence
Leu-Leu
Biochem/physiol Actions
Leucylleucine (Leu-Leu) may be used to study the functionality of dileucine motifs such as the motif responsible for internalization and targeting of vesicular acetylcholine transporter and clathrin adaptors AP-1 and AP-2. Leucylleucine may be used to study growth supplement requirements in vitro.
Storage Class Code
11 - 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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Biochimie, 70(4), 535-542 (1988-04-01)
Different strains of Lactococcus lactis ssp. cremoris hydrolyze peptides at different rates while the cell-free extracts of these strains all show the same or much higher rates of hydrolysis. These observations indicate that the uptake of peptides is the rate-limiting
Clinical science (London, England : 1979), 82(3), 283-290 (1992-03-01)
1. We assessed the efficacy of nitrogen absorption from luminal L-leucine (1.2 and 12 mmol/l) and from isonitrogenous L-leucyl-L-leucine (0.6 and 6.0 mmol/l) in a preparation of vascularly and luminally perfused rat small intestine by measuring luminal leucyl-leucine disappearance and
Traffic (Copenhagen, Denmark), 8(5), 512-522 (2007-04-25)
Efficient cholinergic transmission requires accurate targeting of vesicular acetylcholine transporter (VAChT) to synaptic vesicles (SVs). However, the signals that regulate this vesicular targeting are not well characterized. Although previous studies suggest that the C-terminus of the transporter is required for
Current microbiology, 49(5), 361-365 (2004-10-16)
Oenococcus oeni has numerous amino acid requirements for growth and dipeptides could be important for its nutrition. In this paper the individual or combined effect of dipeptides on growth of O. oeni X2L in synthetic media deficient in one or
Journal of cell science, 112 Pt 18, 3115-3125 (1999-08-27)
Endothelin-converting enzyme (ECE-1) is a type II integral membrane protein which plays a key role in the biosynthetic pathway of the vasoconstricting endothelins. Three ECE-1 isoforms, differing by their N-terminal cytoplasmic tails, are generated from a single gene. When expressed
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