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安全信息

L6525

Sigma-Aldrich

Lys-Ala-Arg-Val-Nle-p-nitro-Phe-Glu-Ala-Nle amide

≥97% (HPLC)

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About This Item

经验公式（希尔记法）:
C49H83N15O13
CAS号:
128340-47-6
分子量:
1090.28
MDL编号:
MFCD00133510
UNSPSC代码:
12352202
PubChem化学物质编号:
329817639
NACRES:
NA.32

产品名称

Lys-Ala-Arg-Val-Nle-p-nitro-Phe-Glu-Ala-Nle amide, ≥97% (HPLC)

质量水平

200

方案

≥97% (HPLC)

储存温度

−20°C

SMILES字符串

CCCC[C@H](NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](Cc1ccc(cc1)[N+]([O-])=O)NC(=O)[C@H](CCCC)NC(=O)[C@@H](NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](C)NC(=O)[C@@H](N)CCCCN)C(C)C)C(N)=O

InChI

1S/C49H83N15O13/c1-7-9-15-33(40(52)67)58-41(68)29(6)57-44(71)36(22-23-38(65)66)60-47(74)37(26-30-18-20-31(21-19-30)64(76)77)62-45(72)34(16-10-8-2)61-48(75)39(27(3)4)63-46(73)35(17-13-25-55-49(53)54)59-42(69)28(5)56-43(70)32(51)14-11-12-24-50/h18-21,27-29,32-37,39H,7-17,22-26,50-51H2,1-6H3,(H2,52,67)(H,56,70)(H,57,71)(H,58,68)(H,59,69)(H,60,74)(H,61,75)(H,62,72)(H,63,73)(H,65,66)(H4,53,54,55)/t28-,29-,32-,33-,34-,35-,36-,37-,39-/m0/s1

InChI key

MJGGTDHEIUOPEB-WBMHOGBOSA-N

Amino Acid Sequence

Lys-Ala-Arg-Val-Nle-pNO2-Phe-Glu-Ala-Nle-NH2

应用

Lys-Ala-Arg-Val-Nle-p-nitro-Phe-Glu-Ala-Nle amide has been used for measuring HIV (human immunodeficiency virus)-1 protease activity.

生化/生理作用

Lys-Ala-Arg-Val-Nle-p-nitro-Phe-Glu-Ala-Nle amide is a synthetic substrate for HIV (human immunodeficiency virus)-1 protease and is commonly used for measuring HIV-1 protease activity.

底物

Substrate for HIV protease.

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

Eyeshields, Gloves, type N95 (US)

法规信息

新产品

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number
0000324453
0000324453
SLCM4157
SLBR3196V
SLBN2572V

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C Dash et al.
The Journal of biological chemistry, 276(4), 2487-2493 (2000-10-24)
The active site cleft of the HIV-1 protease (PR) is bound by two identical conformationally mobile loops known as flaps, which are important for substrate binding and catalysis. The present article reports, for the first time, an HIV-1 PR inhibitor
L H Phylip et al.
Biochemical and biophysical research communications, 171(1), 439-444 (1990-08-31)
Kinetic constants (Km,Kcat) are derived for the hydrolysis of a number of chromogenic peptide substrates by the aspartic proteinase from HIV-2. The effect of systematic replacement of the P2 residue on substrate hydrolysis by HIV-1 and HIV-2 proteinases is examined.
Anita Fehér et al.
The Journal of general virology, 87(Pt 5), 1321-1330 (2006-04-11)
The protease (PR) of Murine leukemia virus (MLV) was expressed in Escherichia coli, purified to homogeneity and characterized by using various assay methods, including HPLC-based, photometric and fluorometric activity measurements. The specificity of the bacterially expressed PR was similar to
Yunfeng Tie et al.
The FEBS journal, 272(20), 5265-5277 (2005-10-13)
HIV-1 protease (PR) and two drug-resistant variants--PR with the V82A mutation (PR(V82A)) and PR with the I84V mutation (PR(I84V))--were studied using reduced peptide analogs of five natural cleavage sites (CA-p2, p2-NC, p6pol-PR, p1-p6 and NC-p1) to understand the structural and
A D Richards et al.
The Journal of biological chemistry, 265(14), 7733-7736 (1990-05-15)
By replacement of the P1' residue in a capsid/nucleocapsid cleavage site mimic with 4-NO2-phenylalanine (Nph), an excellent chromogenic substrate, Lys-Ala-Arg-Val-Leu*Nph-Glu-Ala-Met, for HIV-1 proteinase (kappa cat = 20 s-1, Km = 22 microM) has been prepared. Substitution of the Leu residue

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