HIV Protease Substrate IV

Modify Date: 2025-08-26 18:35:49

HIV Protease Substrate IV structure	Common Name	HIV Protease Substrate IV
	CAS Number	128340-47-6	Molecular Weight	1090.28000
	Density	N/A	Boiling Point	N/A
	Molecular Formula	C₄₉H₈₃N₁₅O₁₃	Melting Point	N/A
	MSDS	USA	Flash Point	N/A

Use of HIV Protease Substrate IV

HIV Protease Substrate IV is a substrate of HIV protease. HIV Protease Substrate IV can be used to measure the activity of HIV (human immunodeficiency virus) -1 protease[1].

Name	Lys-Ala-Arg-Val-Nle-p-nitro-Phe-Glu-Ala-Nle amide
Synonym	More Synonyms

Description	HIV Protease Substrate IV is a substrate of HIV protease. HIV Protease Substrate IV can be used to measure the activity of HIV (human immunodeficiency virus) -1 protease[1].
Related Catalog	Research Areas >> Infection Signaling Pathways >> Metabolic Enzyme/Protease >> HIV Protease
References	[1]. Chaudhury S, et, al. Identification of structural mechanisms of HIV-1 protease specificity using computational peptide docking: implications for drug resistance. Structure. 2009 Dec 9;17(12):1636-1648.

Molecular Formula	C₄₉H₈₃N₁₅O₁₃
Molecular Weight	1090.28000
Exact Mass	1089.63000
PSA	472.95000
LogP	5.10380

HIV Protease Substrate IV MSDS(Chinese)

Personal Protective Equipment	Eyeshields;Gloves;type N95 (US);type P1 (EN143) respirator filter
RIDADR	NONH for all modes of transport

Characterization of the murine leukemia virus protease and its comparison with the human immunodeficiency virus type 1 protease.

J. Gen. Virol. 87(Pt 5) , 1321-30, (2006)

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 fluo...

Molecular basis for substrate recognition and drug resistance from 1.1 to 1.6 angstroms resolution crystal structures of HIV-1 protease mutants with substrate analogs.

FEBS J. 272(20) , 5265-77, (2005)

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 ...

Interactions of a novel inhibitor from an extremophilic Bacillus sp. with HIV-1 protease: implications for the mechanism of inactivation.

J. Biol. Chem. 276(4) , 2487-93, (2001)

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 re...

HIV Substrate,KARVNleF(4-NO2)EANle-NH2