Search results for: goat serum against rabbit fibrinogen
#22970144 // Save this To Up
Synthesis and evaluation of a conjugate vaccine composed of Staphylococcus aureus poly-N-acetyl-glucosamine and clumping factor A.The increasing frequency, severity and antimicrobial resistance of Staphylococcus aureus infections has made the development of immunotherapies against this pathogen more urgent than ever. Previous immunization attempts using monovalent antigens resulted in at best partial levels of protection against S. aureus infection. We therefore reasoned that synthesizing a bivalent conjugate vaccine composed of two widely expressed antigens of S. aureus would result in additive/synergetic activities by antibodies to each vaccine component and/or in increased strain coverage. For this we used reductive amination, to covalently link the S. aureus antigens clumping factor A (ClfA) and deacetylated poly-N-β-(1-6)-acetyl-glucosamine (dPNAG). Mice immunized with 1, 5 or 10 µg of the dPNAG-ClfA conjugate responded in a dose-dependent manner with IgG to dPNAG and ClfA, whereas mice immunized with a mixture of ClfA and dPNAG developed significantly lower antibody titers to ClfA and no antibodies to PNAG. The dPNAG-ClfA vaccine was also highly immunogenic in rabbits, rhesus monkeys and a goat. Moreover, affinity-purified, antibodies to ClfA from dPNAG-ClfA immune serum blocked the binding of three S. aureus strains to immobilized fibrinogen. In an opsonophagocytic assay (OPKA) goat antibodies to dPNAG-ClfA vaccine, in the presence of complement and polymorphonuclear cells, killed S. aureus Newman and, to a lower extent, S. aureus Newman ΔclfA. A PNAG-negative isogenic mutant was not killed. Moreover, PNAG antigen fully inhibited the killing of S. aureus Newman by antisera to dPNAG-ClfA vaccine. Finally, mice passively vaccinated with goat antisera to dPNAG-ClfA or dPNAG-diphtheria toxoid conjugate had comparable levels of reductions of bacteria in the blood 2 h after infection with three different S. aureus strains as compared to mice given normal goat serum. In conclusion, ClfA is an immunogenic carrier protein that elicited anti-adhesive antibodies that fail to augment the OPK and protective activities of antibodies to the PNAG cell surface polysaccharide.
1799 related Products with: Synthesis and evaluation of a conjugate vaccine composed of Staphylococcus aureus poly-N-acetyl-glucosamine and clumping factor A.(5α,16β)-N-Acetyl-16-[2 (5α,16β)-N-Acetyl-16-ac 5α-N-Acetyl-2'H-androst- 5α-N-Acetyl-2'H-androst- 3-O-Acetyl 5,14-Androstad 3-O-Acetyl-17-O-tert-buty 3β-O-Acetyl-androsta-5,1 Androgen Receptor (Phosph Androgen Receptor (Phosph Rabbit Anti-Human Androge Rabbit Anti-Human Androge Androgen Receptor (Ab 650
#10600447 // Save this To Up
Rouleaux-forming serum proteins are involved in the rosetting of Plasmodium falciparum-infected erythrocytes.Excessive sequestration of Plasmodium falciparum-infected (pRBC) and uninfected erythrocytes (RBC) in the microvasculature, cytoadherence, and rosetting, have been suggested to be correlated with the development of cerebral malaria. P. falciparum erythrocyte membrane protein-1 (PfEMP1) is the parasite-derived adhesin which mediates rosetting. Herein we show that serum proteins are crucial for the rosette formation of four strains of parasites (FCR3S1, TM284, TM180, and R29), whereas the rosettes of a fifth strain (DD2) are serum independent. Some parasites, e.g., FCR3S1, can be depleted of all rosettes by washes in heparin and Na citrate and none of the rosettes remain when the parasite is grown in foetal calf serum or ALBUMAX. Rosettes of other parasites are less sensitive; e.g., 20% of TM180 and R29 and 70% of TM284 rosettes still prevail after cultivation. A serum fraction generated by ion-exchange chromatography and poly-ethylene-glycol precipitation restored 50% of FCR3S1 and approx 40 to 100% of TM180 rosettes. In FCR3S1, antibodies to fibrinogen reverted the effect of the serum fraction and stained fibrinogen bound to the pRBC surface in transmission electron microscopy. Normal, nonimmune IgM and/or IgG was also found attached to the pRBC of the four serum-dependent strains as seen by surface immunofluorescens. Our results suggest that serum proteins, known to participate in rouleaux formation of normal erythrocytes, produce stable rosettes in conjunction with the recently identified parasite-derived rosetting ligand PfEMP1.
2097 related Products with: Rouleaux-forming serum proteins are involved in the rosetting of Plasmodium falciparum-infected erythrocytes.Mouse Anti-Plasmodium fal Mouse Anti-P. falciparum Sterile filtered goat se Sterile filtered goat se Sterile filtered mouse s Sterile filtered rat ser anti HSV (II) gB IgG1 (mo anti HCMV IE pp65 IgG1 (m anti HCMV gB IgG1 (monocl Goat Anti-Human, Mouse AR Native Influenza HA (A Br Native Influenza HA (A Br
#9271167 // Save this To Up
Human IgG binding ability of streptococcal M3 protein: its related complement activation-dependent M3 protein polymerization.We previously showed that M3 protein bound both fibrinogen and human serum albumin. Here, I report that M3 protein also has affinity for human immunoglobulin G. In contrast, M3 protein did not show affinity for polyclonal immunoglobulin G from other mammalian species (rabbit and goat). On the human immunoglobulin G molecule, the Fab domain was mainly responsible for the interaction with M3 protein, although the Fc region had a low degree of interaction with the M3 protein. Also, since the 35 kDa C-terminal fragment of M3 protein bound human immunoglobulin G, the binding site for human immunoglobulin G on M3 protein is present in this portion of the protein. The M3 protein-human immunoglobulin G complexes initiated complement activation via both classical and alternative pathways in normal human serum. When C3 was precipitated in the fluid phase with anti-C3 antibody and analyzed by SDS-PAGE under reducing conditions, M3 protein coprecipitated with the complexes and was polymerized. However, there was no polymerization of M3 protein when incubated with normal human serum treated with magnesium-ethyleneglycol-bis-(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid in the presence of M3 protein. Thus, this polymerization is mostly mediated via the classical activation pathway. It is probably helpful for the understanding of the antiphagocytic activity of M protein.
2435 related Products with: Human IgG binding ability of streptococcal M3 protein: its related complement activation-dependent M3 protein polymerization.Rabbit Anti-IEX1 Differen Rabbit Anti-IEX1 Differen anti FAS IgG1 (monoclonal Mouse Anti-Human Retinol Parathyroid Hormone Relat Parathyroid Hormone Relat Human S100 Calcium Bindin ribosome binding protein ribosome binding protein calcium binding protein P Myotubularin related prot SH3 domain-binding protei
#8574521 // Save this To Up
Mechanism for antigen detection on deplasticized epoxy sections.The purpose of this investigation was to explain why deplasticizing of epoxy sections gives higher immunogold labeling than non-deplasticizing. The methods used were the following: (1) Comparison of the ratio of immunogold labeling of deplasticized and non-deplasticized sections with gold particles of different sizes and comparison of this ratio with respect to sections of different thickness, (2) the tilt method (Brorson et al., 1994). Human kidney tissue with amyloid A depositions, human fibrin, and human pituitary tissue were embedded, sections were deplasticized on grids, treated with anti-Aa, anti-fibrinogen or anti-ACTH (ACTH = adrenocorticotropic hormone), and reembedded on grids. Indications of significant antibody penetration were found only at the periphery of structures (ACTH-vesicles). This penetration was about 30 nm. The ratios of immunogold labeling of deplasticized and non-deplasticized sections were approximately 2, 5 and 1 for amyloid, fibrin and ACTH, respectively, and were independent of the gold particle size. No significant differences of gold labeling were found between thicker and thinner deplasticized epoxy sections regardless the gold particle size. No significant differences of gold labeling between deplasticized epoxy sections and LR-White sections were found on interior areas of ACTH-vesicles or amyloid A plaques. The increased labeling of deplasticized epoxy sections compared to normal epoxy sections seemed to be mainly a surface phenomenon. The practical significance of this observation is that deplasticizing of epoxy sections may be a better method for localizing antigens at the periphery of structures than the use of other resin embedding media. Deplasticizing of epoxy sections may be a method of choice in a pathological laboratory to detect antigens in routinely embedded tissues.
Mouse Anti-Ca19.9 Sialyl MOUSE ANTI BORRELIA BURGD Beta Amyloid (40) ELISA K Beta Amyloid (1 42) ELISA Mouse AntiHuman TGF beta Rabbit (polyclonal) AntiH Mouse AntiLamin A Target Mouse AntiLamin B2 Target Mouse AntiCytokeratin (ke Mouse AntiCytokeratin (ke Mouse AntiCytokeratin (ke Mouse AntiCytokeratin (ke
#8059954 // Save this To Up
A microtiter plate assay for factor XIII A-chain-fibrin interactions.Factor XIII A-chain-fibrin interactions regulate factor XIIIa formation and fibrin cross-linking. A microtiter plate assay was developed for studying these interactions. Microtiter plate wells were coated with fibrinogen and converted to fibrin by thrombin. After blocking the wells with bovine serum albumin, factor XIII A-chain was added and binding was monitored by incubating first with anti-factor XIII followed by anti-rabbit IgG-alkaline phosphatase. Enzymatic hydrolysis of p-nitrophenyl phosphate was quantitated by the absorbance at 405 nm. BInding was specific, sensitive, rapid, saturable, and reversible, requiring only nanograms of either factor XIII or fibrin. Binding was time- and concentration-dependent and independent of divalent cations. The bound material was identified as factor XIII A-chain by sodium dodecylsulfate-polyacrylamide gel electrophoresis and immunoblotting. Factor XIII binding was inhibited > 75% by 250 mM sodium chloride or 250 nM anti-factor XIII IgG. The method was also suitable for demonstrating binding using 0.8% plasma or with r-factor XIII expressed in Saccharomyces cerevisiae or Escherichia coli. This method is suitable for identifying the binding sites that are important for plasma factor XIII activation and factor XIIIa activity.
MarkerGeneTM Fluorescent Transcription Factors: T Growth Differentiation Fa Human Platelet Derived Gr Human Platelet Derived Gr Amplite™ Luciferase Rep Amplite™ Luciferase Rep Amplite™ Luciferase Rep Amplite™ Gaussia Lucife Amplite™ Gaussia Lucife Amplite™ Renilla Lucife Amplite™ Renilla Lucife
#8384497 // Save this To Up
Haemostatic derangements associated with arenavirus infection in the guinea-pig: radioimmunoassay of fibrinopeptide A to assess thrombin action in infected animals.Pichinde virus infection of inbred guinea-pigs is a model for arenaviral infections in humans. Infected animals experience reduced levels of multiple coagulation factors caused by either consumption coagulopathy or impaired factor synthesis. A radioimmunoassay (RIA) of guinea-pig fibrinopeptide A (gFPA) has been developed to measure the degree of thrombin action in vivo. gFPA was synthesized via the solid-phase method and conjugated to bovine serum albumin (BSA). A double antibody RIA was established employing goat anti-rabbit IgG to precipitate the primary complex composed of either 125I-5-Tyr-gFPA or 125I-12-Tyr-gFPA and rabbit anti-gFPA-BSA. The cross-reaching material was removed by mixing the plasma with 3 vol of ethanol. The supernatant was filtered through a hollow fibre apparatus by centrifugation. Plasma gFPA immunoreactivities of outbred guinea-pigs averaged 6.56 ng/ml. The gFPA-RIA was validated by determining the quantity of gFPA released from thrombin-degraded fibrinogen. A transient elevation of gFPA levels was detected in Pichinde-infected animals by the gFPA-RIA using 125I-12-Tyr-gFPA as a tracer. The pathogenic mechanism by which the increased gFPA levels may lead to the lethality of Pichinde virus infection remains to be elucidated. It is possible that the coagulopathy triggers changes in immune and inflammatory pathways that induces high cytokine concentrations, with deleterious effects on organs such as the heart and lungs.
1989 related Products with: Haemostatic derangements associated with arenavirus infection in the guinea-pig: radioimmunoassay of fibrinopeptide A to assess thrombin action in infected animals.Guinea Pig Anti-Porcine I FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu Interleukins Recombinant Guinea Pig Anti-Haemophil anti HSV (II) gB IgG1 (mo anti HCMV IE pp65 IgG1 (m anti HCMV gB IgG1 (monocl Recombinant Human Interfe Cell Meter™ Fluorimetri
#2680346 // Save this To Up
The specific interaction between fibrin(ogen) and hyaluronan: possible consequences in haemostasis, inflammation and wound healing.We have proposed that fibrin and hyaluronan (HA) are macromolecular regulators during inflammation and wound healing. Here we extend our studies to characterize the specific interaction between fibrin(ogen) and HA. 125I-labelled HA (Mr approximately 32,000) was bound by plastic surfaces coated with human fibrinogen but not bovine serum albumin, ovalbumin, beta-lactoglobin or rabbit immunoglobulin G. 125I-labelled fibrinogen bound to a unique hexylamine derivative of HA coupled to Sepharose and was eluted specifically by HA oligosaccharides in a size-dependent manner. A dot blot assay, in which proteins are adsorbed to nitrocellulose and probed with 125I-HA, also showed specific binding to human fibrinogen. This assay was used to examine fibrinogens from other mammalian species. No specific 125I-HA binding was observed with the protein from horse, rat or cow. Significant binding was detected with human, sheep, rabbit, dog, baboon, goat and pig fibrinogens. Thrombin-induced formation of fibrin clots is also affected by HA, which decreases the lag time before clotting and increases the rate of clot formation. The rate of fibrin polymerization increased over 500% in the presence of 60 microM HA. Furthermore, the structure of the fibrin gel, as assessed by light scattering, was altered by HA or chondroitin sulphate in a concentration-dependent manner. The results support the proposed wound-healing model and indicate that an increase in circulating HA levels could adversely affect haemostasis and increase the risk of thrombosis or bleeding. The interaction between HA and fibrinogen emphasizes the importance of the liver endothelial cell HA receptor in the removal of glycosaminoglycans from the blood. Cultured cells continuously endocytosing 125I-HA for 4 h reutilized their total cellular HA receptors at least once every 50 min even in the presence of cycloheximide. This endocytotic receptor was therefore shown to be part of a recycling system.
1586 related Products with: The specific interaction between fibrin(ogen) and hyaluronan: possible consequences in haemostasis, inflammation and wound healing.Inflammation (Human) Anti Inflammation (Mouse) Anti Inflammation (Human) Anti Inflammation (Human) Anti Inflammation (Human) Anti Inflammation (Mouse) Anti Multiple organ tumor tiss Androgen Receptor (Phosph Androgen Receptor (Phosph Rabbit Anti-Human Androge Rabbit Anti-Human Androge Androgen Receptor (Ab 650
#3319612 // Save this To Up
Lysosomal and non-lysosomal peptidyl hydrolases of the bloodstream forms of Trypanosoma brucei brucei.African trypanosomes have thiol-dependent proteolytic activity that resembles some of the cathepsin-like activity found in mammalian lysosomes [Lonsdale-Eccles, J. D. & Mpimbaza, G. W. N. (1986) Eur. J. Biochem. 155, 469-473]. Here we show that this activity is found in lysosome-like organelles which we have isolated (density = 1.082 g/cm3 in Percoll) from bloodstream forms of Trypanosoma brucei brucei. They are approximately 250 nm in diameter, are bounded by a single limiting membrane, and contain acid phosphatase. The predominant proteolytic and peptidolytic activity of these organelles has a pH optimum about 6.0, exhibits latency, and has the characteristics of mammalian cathepsin L (and possibly cathepsin H) with respect to its hydrolysis of small fluorogenic peptidyl substrates such as benzyloxycarbonyl-phenylalanyl-arginyl-7-amido-4-methylcoumarin. This substrate appears to be a good marker for trypanosomal lysosomes. The cathepsin-L-like activity is inhibited by the thiol-protease inhibitors, E-64, cystatin, leupeptin and mercurial compounds. The proteolytic activity of the lysosome-like fraction is observed as a single band of activity with an approximate molecular mass of 27 kDa when measured after electrophoresis in the fibrinogen-containing sodium dodecyl sulphate/polyacrylamide gels. The addition of mammalian serum to this purified fraction, or to whole trypanosome homogenates, results in the appearance of additional bands of activity, with a concomitant increase in the total observed proteolytic activity. The serum of some species of animal (e.g. goat and guinea pig) appear to lack the ability to generate this new and increased activity, while rat, rabbit, human and bovine sera exhibit varying capacities to generate the new activity, the cow being the most effective. The apparent molecular masses of the new bands of activity are different for each mammalian species, suggesting that the activator is a species-specific molecule or class of molecules. We also show that Trypanosoma brucei contains soluble peptidolytic activity with an alkaline pH optimum. It is inhibited by the serine-protease inhibitor diisopropylfluorophosphate, but not by inhibitors such as phenylmethylsulphonyl fluoride, alpha 1-antitrypsin, or aprotinin. Nor is it inhibited by the thiol-protease-specific inhibitors E-64 or cystatin, although it is susceptible to inhibition by tosyllysylchloromethane, leupeptin, HgCl2 and p-chloromercuribenzoate. This enzymic activity has a preference for arginyl residues in the primary binding site (the P1 position), as also does the activity from the lysosomes.(ABSTRACT TRUNCATED AT 400 WORDS)
1066 related Products with: Lysosomal and non-lysosomal peptidyl hydrolases of the bloodstream forms of Trypanosoma brucei brucei.Mouse Anti-Trypanosoma br Mouse Anti-Trypanosoma br Cell Navigator™ Lysosom Cell Navigator™ Lysosom Cell Navigator™ Lysosom Cell Navigator™ Lysosom Human Lysosomal acid lipa MarkerGene™ LysoLive™ Ofloxacin CAS Number [824 Anti-ATP6V0A4(ATPase, H+ Anti ATP6V0A4(ATPase, H+ BACTERIOLOGY BACTEROIDES
#2447894 // Save this To Up
Isolation and characterization of a specific antibody population against human fibrinogen.A specific antibody population against human fibrinogen was isolated from a rabbit antiserum by affinity chromatography on fibrinogen-bound Sepharose gel. Using a sensitive competitive radioimmunoassay, the antibody population was found to recognize epitopes on native fibrinogen but crossreacted minimally with fibrinogen fragment D and an early plasmin-degraded fibrinogen A alpha-chain product, but not at all with fragment E or fibrinopeptides A and B. Fibrin monomers shared part of these epitopes. The antibody population crossreacted to a small extent with bovine, horse and baboon fibrinogens and not at all with fibrinogens from sheep, rat, pig, goat, guinea pig, dog and rabbit.
2908 related Products with: Isolation and characterization of a specific antibody population against human fibrinogen.PABP1-dependent poly A-sp Fibrinogen gamma antibody Angiogenesis (Human) Anti Angiogenesis (Human) Anti Apoptosis (Human) Antibod Cytokine (Human) Antibody Cytokine (Human) Antibody Cytokine (Human) Antibody Cytokine (Human) Antibody Cytokine (Human) Antibody Cytokine (Human) Antibody Cytokine (Human) Antibody
#2440301 // Save this To Up
False-positive reaction for fibrin degradation products due to a monoclonal (IgM lambda) cryoglobulin with warm-reactive antibody activity for rabbit IgG.The serum of a patient with prolymphocytic leukemia and a hyperviscosity syndrome contained high levels of IgM, with a monoclonal peak on protein electrophoresis, and had a high titer for fibrin(ogen) degradation products, using a rabbit anti-fibrinogen reagent, without other evidence for disseminated intravascular coagulation. A monoclonal IgM lambda cryoglobulin was identified. It retained reactivity with the fibrin(ogen) degradation products reagent, but failed to react with human IgG by latex fixation. Binding activity for rabbit IgG (and absence of binding activity for human, goat, and bovine IgG) was also demonstrable by double diffusion in agarose, and by enzyme-linked immunoassay. By enzyme-linked immunoassay, binding of both F(ab)2 and Fab and, to a lesser extent, Fc fragments of rabbit IgG was found. Increased binding of heat-denatured rabbit IgG was observed, without inhibition by similarly denatured IgG of other species. The false-positive fibrin(ogen) degradation products reaction in the serum of this patient was due to a unique monoclonal IgM lambda cryoglobulin with warm-reactive antibody activity for an epitope displayed on native and denatured rabbit IgG, but absent on native or denatured human, goat, or bovine IgG, and present in both F(ab)2 and Fc regions of the IgG molecule.
1951 related Products with: False-positive reaction for fibrin degradation products due to a monoclonal (IgM lambda) cryoglobulin with warm-reactive antibody activity for rabbit IgG.RABBIT ANTI GSK3 BETA (pS MOUSE ANTI HUMAN CD15, Pr MOUSE ANTI HUMAN CD15, Pr MOUSE ANTI BOVINE ROTAVIR MOUSE ANTI BORRELIA BURGD succinate-CoA ligase, GDP formin-like 1 antibody So succinate-CoA ligase, ADP Primary antibody Caspase Primary antibody FLIP An MOUSE ANTI CANINE DISTEMP MOUSE ANTI HUMAN CD19 RPE
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45 Fax 0032 16 50 90 45
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50 Fax 01 43 25 01 60
52062 Aachen Deutschland
Tel 0241 40 08 90 86 Fax 0241 55 91 05 36
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
Schweiz Züri +41435006251
Česká republika Praha +420246019719
Ireland Dublin +35316526556
Norge Oslo +4721031366
Finland Helsset +358942419041
Sverige Stockholm +46852503438
Ελλάς Αθήνα +302111768494
Magyarország Budapest +3619980547
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
GENTAUR Nederland BV
5521 DG Eersel Nederland
Tel 0208-080893 Fax 0497-517897
Piazza Giacomo Matteotti, 6, 24122 Bergamo
Tel 02 36 00 65 93 Fax 02 36 00 65 94
53 Iskar Str. 1191 Kokalyane, Sofia