MOUSE ANTI LEISHMANIA MAJOR SURFACE PROTEASE gp63

Price:
360 EUR
432 USD
298 GBP
known as: MOUSE ANTI LEISHMANIA MAJOR SURFACE PROTEASE gp63
Catalog number: genta-ABS0185
Product Quantity: 0.5 ml
Category:
Supplier: AbD

   CAPTCHA Image   Reload Image

Gene target: leishmania major surface protease gp63

Related genes to: MOUSE ANTI LEISHMANIA MAJOR SURFACE PROTEASE gp63

Symbol : gp63 NIH gene
LocusTag : PPYV_gp63
description : structural phage protein
type of gene : protein-coding
Modification date : 2015-06-26
Symbol : protease NIH gene
LocusTag : Opavgp2
description : neutral protease large subunit
type of gene : protein-coding
Modification date : 2015-06-26

Related Pathways to: MOUSE ANTI LEISHMANIA MAJOR SURFACE PROTEASE gp63

Gene about :protease
Pathway :Ce Proteasome Degradation
protease

Related product to: MOUSE ANTI LEISHMANIA MAJOR SURFACE PROTEASE gp63

Related Articles about: MOUSE ANTI LEISHMANIA MAJOR SURFACE PROTEASE gp63

The crystal structure of a multidomain protease inhibitor (HAI-1) reveals the mechanism of its auto-inhibition.

- Source :PubMed

Site-1 protease, a novel metabolic target for glioblastoma.

Sterol regulatory element binding proteins (SREBPs) are transcriptional regulators of lipids which promote glioblastoma growth. Here, we investigate the effect of inhibiting expression of SREBP target genes in human glioblastoma cells. This was achieved by using PF-429242 to inhibit site-1 protease (S1P), an enzyme required for SREBP activation. Treatment with PF-429242 decreased glioblastoma cell viability, induced apoptosis and downregulated steroid, isoprenoid and unsaturated fatty acid biosynthetic pathways. Several pro-inflammatory genes were upregulated. Collectively, these regulates demonstrate the potential of S1P as a target for glioblastoma therapy. - Source :PubMed

Drug Resistance Mechanism of L10F, L10F/N88S and L90M mutations in CRF01_AE HIV-1 protease: Molecular dynamics simulations and binding free energy calculations.

HIV-1 protease plays a crucial role in viral replication and maturation, which makes it one of the most attractive targets for anti-retroviral therapy. The majority of HIV infections in developing countries are due to non-B subtype. Subtype AE is spreading rapidly and infecting huge population worldwide. The mutations in the active site of subtype AE directly impair the interactions with the inhibitor. The non-active site mutations influence the binding of the inhibitor indirectly and their resistance mechanism is not well understood. It is important to design new effective inhibitors that combat drug resistance in subtype AE protease. In this work, we examined the effect of non active site mutations L10F, L10F/N88S and L90M with nelfinavir using molecular dynamics simulation and binding free energy calculations. The simulations suggested that the L10F and L10F/N88S mutants decrease the binding affinity of nelfinavir, whereas the L90M mutant increases the binding affinity. The formation of hydrogen bonds between nelfinavir and Asp30 is crucial for effective binding. The benzamide moiety of nelfinavir shows large positional deviation in L10F and L10F/N88S complexes and the L10F/N88S mutation changes the hydrogen bond between the side chain atoms of 30th residue and the 88th residue. Consequently the hydrogen bond interaction between Asp30 and nelfinavir are destroyed leading to drug resistance. Our present study shed light on the resistance mechanism of the strongly linked mutation L10F/N88S observed experimentally in AE subtype. - Source :PubMed

Effect of pH on dentin protease inactivation by carbodiimide.

A water-soluble crosslinking agent, 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC), has been used as a pretreatment of acid-etched dentin to inactivate matrix-bound endogenous dentin proteases. The aim of this study was to evaluate the effect of pH on the inactivation capacity of EDC. Demineralized dentin beams (1 × 2 × 6 mm) were divided into six groups (n = 8 per group). Then, EDC (0.3 M) was solubilized in distilled water with pH of 2, 4, 6, 7, 9, or 11. Control EDC was solubilized in 0.1 M 2-(N-morpholino) ethanesulfonic acid (MES) buffer and its pH was adjusted to 6. The dentin beams were pretreated for 1 min with EDC at each pH or with EDC in MES buffer at pH 6.0 and then incubated in 1 ml of simulated body fluid (pH 7.2) for 1, 3, 7, or 14 d. Untreated beams served as controls. At each study time-point, the dry mass of dentin beams was assessed and the incubation media were analyzed for carboxyterminal telopeptide of type-I collagen (ICTP) and C-terminal telopeptide of type I collagen (CTX) using specific ELISAs. Data were subjected to repeat-measures anova. The results of the study indicated that specimens pretreated with EDC in MES buffer showed the lowest collagen degradation in terms of mass loss and release of telopeptides, while specimens pretreated in alkaline media showed the highest collagen degradation. This study indicates that the pH of the EDC solution plays an important role in the stability of dentin protease inactivation. - Source :PubMed

The role of the LB structural loop and its interactions with the PDZ domain of the human HtrA3 protease.

Human HtrA3 protease is a proapoptotic protein, involved in embryo implantation and oncogenesis. In stress conditions the protease is activated by removal of its N-terminal domain. The activated form, ΔN-HtrA3L is a homotrimer composed of the protease (PD) and PDZ domains. The LB structural loop of the PD is longer by six amino acid residues than its counterparts of other human HtrA proteins and interacts with the PDZ in a way not observed in other known HtrA structures. By size exclusion chromatography of the ΔN-HtrA3L mutated variants we found that removal of the additional LB loop residues caused a complete loss of the proper trimeric structure while impairing their interactions with the PDZ domain decreased the amount of the trimers. This indicates that the LB loop participates in stabilization of the ΔN-HtrA3L oligomer structure and suggests involvement of the LB-PDZ interactions in the stabilization. Removal of the additional LB loop residues impaired the ΔN-HtrA3L activity against the peptide and protein substrates, including the antiapoptotic XIAP protein, while a decrease in the LB-PDZ interaction caused a diminished efficiency of the peptide cleavage. These results indicate that the additional LB residues are important for the ΔN-HtrA3L proteolytic activity. Furthermore, a monomeric form of the ΔN-HtrA3L is proteolytically inactive. In conclusion, our results suggest that the expanded LB loop promotes the ΔN-HtrA3L activity by stabilizing the protease native trimeric structure. - Source :PubMed

Gentaur adresses


GENTAUR Europe BVBA
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45
Fax 0032 16 50 90 45
info@gentaur.com
GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50
Fax 01 43 25 01 60
france@gentaur.com
dimi@gentaur.com
GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531
Fax 020 8445 9411
uk@gentaur.com
GENTAUR Poland Sp. z o.o.
ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
Tel 058 710 33 44
Fax 058 710 33 48
poland@gentaur.com
GENTAUR Nederland BV
Kuiper 1
5521 DG Eersel Nederland
Tel 0208-080893
Fax 0497-517897
nl@gentaur.com
GENTAUR SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6, 24122 Bergamo
Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com
GENTAUR bulgaria
53 Iskar Str. Kokalyane,
Sofia 1191
Tel 0035929830070
Fax 0035929830072
sofia@gentaur.com
GENTAUR Spain
Tel 0911876558
spain@gentaur.com
GENTAUR USA
Genprice Inc, Logistics
547 Yurok Circle
San Jose, CA 95123
invoicing/ accounting:
6017 Snell Ave, Suite 357
San Jose, CA. 96123
Tel 001 408 780 0908
jane@gentaur.com