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L6525

Sigma-Aldrich

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

≥97% (HPLC)

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About This Item

Fórmula empírica (notación de Hill):
C49H83N15O13
Número de CAS:
128340-47-6
Peso molecular:
1090.28
MDL number:
MFCD00133510
UNSPSC Code:
12352202
PubChem Substance ID:
329817639
NACRES:
NA.32

product name

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

assay

≥97% (HPLC)

storage temp.

−20°C

SMILES string

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

Application

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

Biochem/physiol Actions

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.

Substrates

Substrate for HIV protease.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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.
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
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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