Only in Titles

Search results for: Anti-ADAM-33, Catalytic Domain produced in rabbit Antibody

paperclip

Error loading info... Pleas try again later.
paperclip

Error loading info... Pleas try again later.
paperclip

#20601114   2010/06/23 To Up

Endogenous H2O2 produced by Streptococcus pneumoniae controls FabF activity.

FabF elongation condensing enzyme is a critical factor in determining the spectrum of products produced by the FASII pathway. Its active site contains a critical cysteine-thiol residue, which is a plausible target for oxidation by H2O2. Streptococcus pneumoniae produces exceptionally high levels of H2O2, mainly through the conversion of pyruvate to acetyl-P via pyruvate oxidase (SpxB). We present evidence showing that endogenous H2O2 inhibits FabF activity by specifically oxidizing its active site cysteine-thiol residue. Thiol trapping methods revealed that one of the three FabF cysteines in the wild-type strain was oxidized, whereas in an spxB mutant, defective in H2O2 production, none of the cysteines was oxidized, indicating that the difference in FabF redox state originated from endogenous H2O2. In vitro exposure of the spxB mutant to various H2O2 concentrations further confirmed that only one cysteine residue was susceptible to oxidation. By blocking FabF active site cysteine with cerulenin we show that the oxidized cysteine was the catalytic one. Inhibition of FabF activity by either H2O2 or cerulenin resulted in altered membrane fatty acid composition. We conclude that FabF activity is inhibited by H2O2 produced by S. pneumoniae.
Rachel Benisty, Aharon Yehonatan Cohen, Alexandra Feldman, Zvi Cohen, Nurith Porat

1870 related Products with: Endogenous H2O2 produced by Streptococcus pneumoniae controls FabF activity.

1 ml100ul100ul100ul100ul10 ug1 mL100ug100ug100ul 96 Tests 100 assays

Related Pathways

paperclip

#19549486   2009/06/24 To Up

Modulation of the immunogenicity of the Trypanosoma congolense cysteine protease, congopain, through complexation with alpha(2)-macroglobulin.

The protozoan parasite Trypanosoma congolense is the main causative agent of livestock trypanosomosis. Congopain, the major lysosomal cysteine proteinase of T. congolense, contributes to disease pathogenesis, and antibody-mediated inhibition of this enzyme may contribute to mechanisms of trypanotolerance. The potential of different adjuvants to facilitate the production of antibodies that would inhibit congopain activity was evaluated in the present study. Rabbits were immunised with the recombinant catalytic domain of congopain (C2), either without adjuvant, with Freund's adjuvant or complexed with bovine or rabbit alpha(2)-macroglobulin (alpha(2)M). The antibodies were assessed for inhibition of congopain activity. Rabbits immunised with C2 alone produced barely detectable anti-C2 antibody levels and these antibodies had no effect on recombinant C2 or native congopain activity. Rabbits immunised with C2 and Freund's adjuvant produced the highest levels of anti-C2 antibodies. These antibodies either inhibited C2 and native congopain activity to a small degree, or enhanced their activity, depending on time of production after initial immunisation. Rabbits receiving C2-alpha(2)M complexes produced moderate levels of anti-C2 antibodies and these antibodies consistently showed the best inhibition of C2 and native congopain activity of all the antibodies, with maximum inhibition of 65%. Results of this study suggest that antibodies inhibiting congopain activity could be raised in livestock with a congopain catalytic domain-alpha(2)M complex. This approach improves the effectiveness of the antigen as an anti-disease vaccine candidate for African trypanosomosis.
Laura Elizabeth Joan Huson, Edith Authié, Alain Francçois Boulangé, James Phillip Dean Goldring, Theresa Helen Taillefer Coetzer

2954 related Products with: Modulation of the immunogenicity of the Trypanosoma congolense cysteine protease, congopain, through complexation with alpha(2)-macroglobulin.

1 kit(96 Wells)500 Units 100 G250 ug1 100ul100 U100.00 ul1 kit(96 Wells)

Related Pathways

paperclip

Error loading info... Pleas try again later.
paperclip

Error loading info... Pleas try again later.
paperclip

#10559435   // To Up

Immunogold labeling of rosette terminal cellulose-synthesizing complexes in the vascular plant vigna angularis

The catalytic subunit of cellulose synthase is shown to be associated with the putative cellulose-synthesizing complex (rosette terminal complex [TC]) in vascular plants. The catalytic subunit domain of cotton cellulose synthase was cloned using a primer based on a rice expressed sequence tag (D41261) from which a specific primer was constructed to run a polymerase chain reaction that used a cDNA library from 24 days postanthesis cotton fibers as a template. The catalytic region of cotton cellulose synthase was expressed in Escherichia coli, and polyclonal antisera were produced. Colloidal gold coupled to goat anti-rabbit secondary antibodies provided a tag for visualization of the catalytic region of cellulose synthase during transmission electron microscopy. With a freeze-fracture replica labeling technique, the antibodies specifically localized to rosette TCs in the plasma membrane on the P-fracture face. Antibodies did not specifically label any structures on the E-fracture face. Significantly, a greater number of immune probes labeled the rosette TCs (i.e., gold particles were 20 nm or closer to the edge of the rosette TC) than did preimmune probes. These experiments confirm the long-held hypothesis that cellulose synthase is a component of the rosette TC in vascular plants, proving that the enzyme complex resides within the structure first described by freeze fracture in 1980. In addition, this study provides independent proof that the CelA gene is in fact one of the genes for cellulose synthase in vascular plants.
Kimura, Laosinchai, Itoh, Cui, Linder, Brown

2098 related Products with: Immunogold labeling of rosette terminal cellulose-synthesizing complexes in the vascular plant vigna angularis

100.00 ug96tests1

Related Pathways

paperclip

#10029538   // To Up

Relationship between phospholamban and nucleotide activation of cardiac sarcoplasmic reticulum Ca2+ adenosinetriphosphatase.

A strong connection with nucleotide activation of Ca2+ATPase and phospholamban inhibition has been found. Phospholamban decreases the number of activatable Ca2+ATPase without affecting substrate affinity or the ability of nucleotide to serve its dual modulatory roles, i.e., catalytic and regulatory. Low concentrations of certain nucleotide mimetics, quercetin, tannin, and ellagic acid, with structural similarity to adenine can unmask phospholamban's inhibitory effect while concurrently acting as competitive inhibitors of nucleotide binding. Micromolar concentrations of tannin (EC50 approximately 0.3 microM) and ellagic acid (EC50 approximately 3 microM) stimulated Ca2+ uptake and calcium-activated ATP hydrolysis at submicromolar Ca2+ in isolated cardiac sarcoplasmic reticulum (SR). Stimulation of Ca2+ATPase was followed by pronounced inhibiton at only slightly higher tannin concentrations (IC50 approximately 3 microM), whereas inhibitory effects by ellagic acid were observed at much greater concentrations (IC50 > 300 microM) than the EC50. A complex relationship between compound, SR protein, and MgATP concentration is a major determining factor in the observed effects. Stimulation was only observed under conditions of phospholamban regulation, while the inhibitory effects were observed in cardiac SR at micromolar Ca2+ and in skeletal muscle SR, which lacks phospholamban. Maximal stimulation of Ca2+ATPase was identical to that observed with the anti-phospholamban monoclonal antibody 1D11. Both compounds appear to relieve the Ca2+ATPase from phospholamban inhibition, thereby increasing the calcium sensitivity of the Ca2+ATPase like that observed with phosphorylation of phospholamban or treatment with monoclonal antibody 1D11. Tannin, even under stimulatory conditions, is a competitive inhibitor of MgATP with a linear Dixon plot. The subsequent inhibitory action of higher tannin concentrations results from competition of tannin with the nucleotide binding site of the Ca2+ATPase. In contrast, ellagic acid produced a curvilinear Dixon plot suggesting partial inhibition of nucleotide activation. The data suggest that nucleotide activation of Ca2+ATPase is functionally coupled to the phospholamban interaction site. These compounds through their interaction with the adenine binding domain of the nucleotide binding site prevent or dissociate phospholamban regulation. Clearly, this portion of Ca2+ATPase needs further study to elucidate its role in phospholamban inhibition.
K E Coll, R G Johnson, E McKenna

2264 related Products with: Relationship between phospholamban and nucleotide activation of cardiac sarcoplasmic reticulum Ca2+ adenosinetriphosphatase.

0.25 mL100ug Lyophilized1,000 tests 1 kit(s) 100ul1 kit(96 Wells)100ug Lyophilized21 mg1 mg100ug Lyophilized1000

Related Pathways

paperclip

#9655252   // To Up

Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts.

M
H Li, D E Bauzon, X Xu, H Tschesche, J Cao, Q A Sang

1414 related Products with: Immunological characterization of cell-surface and soluble forms of membrane type 1 matrix metalloproteinase in human breast cancer cells and in fibroblasts.

100ug Lyophilized 100ul100ug Lyophilized

Related Pathways

    No related Items
paperclip

#7509682   // To Up

Structural characterization of gelonin: evidence for separate antigenic and cytotoxic domains.

The N-terminal sequence of the three isoforms of gelonin is identical. Cyanogen bromide cleavage of gelonin produced fragments of Mr 17,000, 13,000, 11,000 and 7,000. The apparent Mr 17,000 component was identified as the N-terminal fragment and represents the major antigenic domain of the protein as it reacted with antibody to the native protein but this fragment did not inhibit protein synthesis in the in vitro translation assay. Our data may suggest possibilities for separation of antigenic and catalytic domains of this ribosome inactivating protein.
M R Sairam, B R Srinivasa, J Marcil

1136 related Products with: Structural characterization of gelonin: evidence for separate antigenic and cytotoxic domains.

10 mg1 g 50 UG0.2 mg100 mg100ul 1 G100tests 25 G10 mg100μg

Related Pathways