L5502
Lys-Lys dihydrochloride
≥98% (TLC)
别名:
Dilysine
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关于此项目
经验公式(希尔记法):
C12H26N4O3 · 2HCl
CAS Number:
分子量:
347.28
MDL编号:
UNSPSC代码:
12352209
PubChem化学物质编号:
NACRES:
NA.26
Product Name
Lys-Lys dihydrochloride,
方案
≥98% (TLC)
质量水平
表单
powder
颜色
white
应用
peptide synthesis
储存温度
−20°C
SMILES字符串
Cl.NCCCCC(N)C(=O)NC(CCCCN)C(O)=O
InChI
1S/C12H26N4O3.ClH/c13-7-3-1-5-9(15)11(17)16-10(12(18)19)6-2-4-8-14;/h9-10H,1-8,13-15H2,(H,16,17)(H,18,19);1H
InChI key
ROGKVZGKYWMMAT-UHFFFAOYSA-N
应用
Lysyllysine (Lys-Lys) may be used in studies of prebiotically relevant Salt-Induced Peptide Formation (SIPF) and in for physical chemical analysis.
警示用语:
Warning
危险声明
危险分类
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
靶器官
Respiratory system
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
dust mask type N95 (US), Eyeshields, Gloves
R T MacGillivray et al.
Biochemistry, 39(6), 1211-1216 (2000-02-24)
Serum transferrin is the major iron transport protein in humans. Its function depends on its ability to bind iron with very high affinity, yet to release this bound iron at the lower intracellular pH. Possible explanations for the release of
Lauren P Jackson et al.
Developmental cell, 23(6), 1255-1262 (2012-11-28)
COPI mediates retrograde trafficking from the Golgi to the endoplasmic reticulum (ER) and within the Golgi stack, sorting transmembrane proteins bearing C-terminal KKxx or KxKxx motifs. The structure of KxKxx motifs bound to the N-terminal WD-repeat domain of β'-COP identifies
Heather M Baker et al.
Acta crystallographica. Section D, Biological crystallography, 63(Pt 3), 408-414 (2007-03-01)
Iron uptake by humans depends on the ability of the serum protein transferrin (Tf) to bind iron as Fe(3+) with high affinity but reversibly. Iron release into cells occurs through receptor-mediated endocytosis, aided by the lower endosomal pH of about
Ronghu Wu et al.
Journal of the American Society for Mass Spectrometry, 22(9), 1651-1659 (2011-09-29)
The structure of the proton-bound lysine dimer has been investigated by infrared multiple photon dissociation (IRMPD) spectroscopy and electronic structure calculations. The structures of different possible isomers of the proton-bound lysine dimer have been optimized at the B3LYP/6-31 + G(d) level of
R Puertollano et al.
Molecular biology of the cell, 12(6), 1869-1883 (2001-06-16)
The MAL proteolipid, a component of the integral protein sorting machinery, has been demonstrated as being necessary for normal apical transport of the influenza virus hemagglutinin (HA) and the overall apical membrane proteins in Madin-Darby canine kidney (MDCK) cells. The
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