Only in Titles

           Search results for: goat IgG against mouse fibrinogen   

paperclip

#22970144   2012/09/12 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.

1502 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

Related Pathways

paperclip

#11739763   2001/12/12 Save this To Up

The fibrinogen-binding protein (FgBP) of Streptococcus equi subsp. equi additionally binds IgG and contributes to virulence in a mouse model.

The major cell-wall-associated protein of the equine pathogen Streptococcus equi subsp. equi is an M-like fibrinogen-binding protein (FgBP) which binds equine fibrinogen (Fg) avidly, through residues located at the extreme N-terminus of the molecule. In this study, it is shown that FgBP additionally binds equine IgG-Fc. When tested against polyclonal IgG from ten other animal species, it was found that FgBP binds human, rabbit, pig and cat IgG, but does not bind mouse, rat, goat, sheep, cow or chicken IgG. Through the use of a panel of recombinant FgBP truncates containing defined deletions of sequence, it was shown that residues in the central regions of FgBP are important in IgG binding. An fbp knockout mutant which does not express FgBP on the cell surface was also constructed. Mutant cells failed to autoaggregate, bound no detectable equine Fg or IgG-Fc, were rapidly killed in horse blood, and showed greatly decreased virulence in a mouse model. Results suggest that FgBP is the major surface structure responsible for binding either Fg or IgG, that the molecule has pronounced antiphagocytic properties, and that it is a likely factor contributing to the virulence of wild-type S. equi subsp. equi.

1154 related Products with: The fibrinogen-binding protein (FgBP) of Streptococcus equi subsp. equi additionally binds IgG and contributes to virulence in a mouse model.

Rabbit Anti-APIP Apaf1 In Rabbit Anti-APIP Apaf1 In Rabbit Anti-TNIP2 ABIN2 T Rabbit Anti-TNIP2 ABIN2 T Rabbit Anti-Cell death in Rabbit Anti-Cell death in Mouse Anti-Equine IgG (T) Mouse Anti-Equine IgGa Mouse Anti-Equine IgGb anti-Diazepam Binding Inh anti-Diazepam Binding Inh anti-Vitamin D binding pr

Related Pathways

paperclip

#10600447   1999/12/28 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.

2195 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

Related Pathways

paperclip

#9886911   1999/03/09 Save this To Up

Fibrin monomer increases platelet adherence to tumor cells in a flowing system: a possible role in metastasis?

Considerable evidence exists linking hemostasis and malignancy. Platelet adhesion to tumor cells has been implicated in the metastatic process. Plasma fibrinogen (Fg) and fibrin (Fn) monomer, increased in cancer, may play a role in tumor biology. Binding of Fn monomer to tumor cells and its effect on platelet-tumor cell adhesion in a flowing system were studied. Fn monomer was produced by adding thrombin (1 micro/mL) to FXIII- and plasminogen-free Fg in the presence of Gly-Pro-Arg-Pro (GPRP) amide. Fn monomer binding to live A375 cells was visualized by confocal laser scanning microscopy (CLSM). Adherent cells were perfused for 1h with Fn monomer, washed and stained in situ with anti-human Fn (American Biogenetic Sciences, Inc.) followed by goat anti-mouse IgG(FITC). Platelet adherence to Fn monomer treated A375 cells was performed under flow conditions by passing platelets (5x10(4)/microl 0.25 mL/min; labeled with the carbocyanine dye DiI) over the tumor cells for 30 min. CLSM images were obtained after washing. There was considerable binding of Fn monomer, but not Fg alone. Platelets adhered relatively weakly to untreated A375 cells and this was not significantly affected by pre-treatment of the tumor cells with fibrinogen or thrombin. However, pre-treatment with Fn monomer resulted in extensive platelet binding to tumor cells, suggesting that coagulation activation and the subsequent increase in circulating Fn monomer may enhance platelet adhesion to circulating tumor cells and thereby facilitate metastatic spread.

1324 related Products with: Fibrin monomer increases platelet adherence to tumor cells in a flowing system: a possible role in metastasis?

Endocrine system benign, anti HSV (II) gB IgG1 (mo anti HCMV IE pp65 IgG1 (m anti HCMV gB IgG1 (monocl Recombinant Human Interfe Cell Meter™ Fluorimetri Cell Meter™ Fluorimetri GLP 1 ELISA Kit, Rat Gluc Glucagon ELISA KIT, Rat G Anti beta3 AR Human, Poly Homogenizer for 24 sample Top five cancer tissue ar

Related Pathways

paperclip

#7543524   1995/09/12 Save this To Up

L-selectin (CD62L) cross-linking signals neutrophil adhesive functions via the Mac-1 (CD11b/CD18) beta 2-integrin.

Emigration of leukocytes at sites of inflammation is initiated by the selectin family of carbohydrate-binding adhesion molecules. Molecular crossbridges initiate rolling of cells along the vascular endothelium where chemokines such as IL-8 and platelet activating factor (PAF) may be presented to their receptors on the leukocyte surface resulting in cell stimulation. Integrin activation appears to be a requirement for subsequent cell localization and diapedesis into the tissue. Several recent reports have demonstrated that ligation and cross-linking of neutrophil L-selectin results in neutrophil activation, including intracellular calcium release, superoxide production, and induction of mRNA for production of IL-8 and TNF-alpha. The purpose of this study was to examine whether ligation and cross-linking of L-selectin would specifically result in activation of beta 2-integrin-dependent adhesion. A fluorescence flow cytometric assay was developed that directly measures Mac-1-dependent cell adhesion. Fluorescent latex beads (2-microns diameter) were adsorbed with albumin or fibrinogen and added in excess to human neutrophils in a shear-stirred suspension. Following stimulation the kinetics of bead capture by neutrophils was continuously measured in real time on the flow cytometer. The onset of bead binding was detected in the presence of extremely low concentrations of PAF (10 pM) or formyl peptide (0.2 nM) stimulation. Ligation of L-selectin with whole IgG DREG200 or DREG56 Ab, but not controls (anti-CD44, -CD45, -CD11a), resulted in a significant potentiation of bead binding. Cross-linking F(ab')2 fragments of DREG200 with a goat anti-mouse F(ab')2 secondary Ab also stimulated beta 2-integrin-dependent adhesion in a dose-dependent fashion. A chimeric form of DREG200 expressing gamma 4 or gamma 1 isotypes of human Fc domain also stimulated cell adhesion when cross-linked. Surface expression of CD18 and an activation-dependent epitope, as detected with mAb24, also increased in response to L-selectin cross-linking. Cross-linking L-selectin induced significant adhesion and transmigration of neutrophils across human umbilical vein endothelial cells. We propose that cross-linking of L-selectin results in a cell signal that directly stimulates beta 2-integrin adhesive responses.

2748 related Products with: L-selectin (CD62L) cross-linking signals neutrophil adhesive functions via the Mac-1 (CD11b/CD18) beta 2-integrin.

Rabbit Anti-Integrin beta Rabbit Anti-Integrin beta Rabbit Anti-Integrin beta Rabbit Anti-Integrin beta Primary antibody IKK bet L-Selectin/CD62L Antibody L-Selectin CD62L Antibody L Selectin CD62L Antibody L Selectin CD62L Polyclon Rabbit Anti-Integrin beta Rabbit Anti-Integrin beta Rabbit Anti-Integrin beta

Related Pathways

  •  
  • No related Items
paperclip

#8463348   1993/05/06 Save this To Up

Plasma protein adsorption to hemodialysis membranes: studies in an in vitro model.

Upon interaction of whole blood with foreign materials, heterogeneous protein films are deposited onto the artificial surface (eg, hemodialysis membranes). The composition of these protein films subsequently affects various processes, eg, thrombogenesis or activation of the complement system. We developed an in vitro model with which we can identify and study proteins interacting with capillaries during hemodialysis. Using this model we studied the cuprophane dialyzer GFS 120 (CP) and the polymethylmetacrylate membrane Filtryzer B2-1.2 (PMMA). Heparinized whole blood from healthy young volunteers was dialyzed on an extracorporeal dialysis machine. After the dialysis procedure the adsorbed material was eluted from the hemodialysis membranes by different eluants and subsequently analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting. A number of proteins could be identified in the eluates of both membrane types. Interestingly, platelet glycoproteins could only be found in PMMA eluates. Albumin, IgG, and antithrombin III were mainly present in the cuprophane eluates. Fibrinogen was demonstrable in all eluates, but in relatively low amounts, and the protein was significantly degraded. Degradation products of antithrombin III and complement factor 3 could also be identified. The process causing the degradation has not yet been identified, but may be due to proteases released from damaged cells.

2470 related Products with: Plasma protein adsorption to hemodialysis membranes: studies in an in vitro model.

Rabbit Anti-Human Toll In Toxoplasma gondii GRA8, r FIV Core Ag, recombinant HIV 1 intergase antigen. Native Influenza HA (A To Native Influenza HA (A To Native Influenza HA (A To MID1 interacting G12-like Cultrex In Vitro Angiogen Proteinase Inhibitor 9 (P Proteinase Inhibitor 9 (P Proteinase Inhibitor 9 (P

Related Pathways

paperclip

#1710235   1991/07/10 Save this To Up

Fibrinogen acts as a bridging molecule in the adherence of Staphylococcus aureus to cultured human endothelial cells.

The propensity of Staphylococcus aureus to cause acute endovascular infections during transient bacteremia is poorly understood. To examine the events leading to the attachment of staphylococci to endothelium, adherence assays were developed to study the role of blood factors in the mediation of staphylococcal adherence to cultured human umbilical vein endothelium in vitro. Results indicate that the preferential attachment of S. aureus to endothelial cells is mediated by fibrinogen adsorbed from plasma onto the endothelial surface. The binding is apparently specific because it could be blocked by goat anti-human fibrinogen antibody in a dose-dependent fashion while nonimmune goat IgG, mouse MAb against AG-1 (a platelet antigen found on the endothelial cell surface), nonspecific mouse MAb and rabbit antibodies to human vitronectin and fibronectin were not inhibitory. Our data also indicate that fibrinogen is a necessary but not the only blood constituent in the mediation of binding of S. aureus to endothelium. This was supported by the finding that fibrinogen alone, at a concentration equivalent to that in plasma, did not potentiate staphylococcal adherence as much as plasma while afibrinogenemic plasma reconstituted with fibrinogen did. Because fibrinogen is known to bind to endothelial cells, our data is consistent with the hypothesis that fibrinogen and additional plasma factor(s), possibly activated during inflammation, promote staphylococcal adherence to endothelium. In addition, the role of the fibrinogen binding receptor of S. aureus as an adherence factor to native endothelium is also suggested.

1134 related Products with: Fibrinogen acts as a bridging molecule in the adherence of Staphylococcus aureus to cultured human endothelial cells.

Human Internal Mammary Ar GFP Expressing Human Inte Mouse Anti-Human Endothel Goat Anti-Human Endotheli Recombinant Human Interfe Cell Meter™ Fluorimetri Cell Meter™ Fluorimetri GLP 1 ELISA Kit, Rat Gluc Cultrex In Vitro Angiogen Human Aortic Artery Endot GFP Expressing Human Aort Human Coronary Artery End

Related Pathways

paperclip

#1899382   1991/03/13 Save this To Up

Construction and characterization of a functional chimeric murine-human antibody directed against human fibrin fragment-D dimer.

Fibrin-directed monoclonal antibodies may be clinically useful for in vitro thrombus imaging and for the targeting of fibrinolytic agents to blood clots. One such murine monoclonal antibody, (mAb-15C5), raised against the fragment-D dimer epitope of cross-linked human fibrin, was previously characterized [Holvoet, P., Stassen, J. M., Hashimoto, Y., Spriggs, D., Devos, P. & Collen, D. (1989) Thromb. Haemostasis 61, 307-313] has recently been cloned and expressed [Vandamme, A.-M., Bulens, F., Bernar, H., Nelles, L., Lijnen, H. R. & Collen, D. (1990) Eur. J. Biochem. 192, 767-775]. In order to reduce the immunogenicity of the murine mAb-15C5 in man, we have now constructed a murine--human chimera of mAb-15C5, by substituting the cDNA sequences encoding the constant regions of the murine kappa light chain and gamma 1 heavy chain by the corresponding human genomic sequences. Both chimeric murine--human Ig chains were cloned into two separately selectable expression vectors, which were contransfected into Chinese hamster ovary (CHO) cells. Murine--human chimeric mAb-15C5 (mAb-15C5Hu) was purified from the conditioned medium of selected cell lines by chromatography on Zn-chelating Sepharose, protein-A-Sepharose and on insolubilized antigen (fragment-D dimer), with a final yield of 29 micrograms/l and a recovery of 33%. SDS/PAGE without reduction revealed a homogeneous band with a mobility similar to that of natural mAb-15C5, whereas after reduction, both the heavy and the light chains had slightly slower mobilities than their natural counterparts. Expression in the presence of tunicamycin suggested that the differences in gamma 1-chain mobility were due to different N-glycosylation patterns. Immunoblotting of proteins from SDS gels showed immunological reactivity of recombinant mAb-15C5Hu with goat anti-(human IgG) IgG and of recombinant and natural murine mAb-15C5 with goat anti-(mouse IgG) IgG. Competitive binding revealed a comparable affinity of recombinant murine mAb-15C5, recombinant mAb-15C5Hu and natural mAb-15C5, for fragment-D dimer, indicating that recombinant mAb-15C5Hu was obtained in a functionally intact form. Thus, mAb-15C5Hu may constitute a useful alternative to mAb-15C5 for in vivo use in man.

2246 related Products with: Construction and characterization of a functional chimeric murine-human antibody directed against human fibrin fragment-D dimer.

Beta Amyloid (40) ELISA K Beta Amyloid (1 42) ELISA Histone H3 (Di-Methyl-Lys DLK1 Antibody Source Rabb CD209 (DC-SIGN) Antibody Doublecortin Antibody Sou DDX3Y antibody Source Rab Desmocollin 2 antibody So DECR1 antibody Source Rab DLST antibody Source Rabb DNAI2 antibody Source Rab dynactin 1 antibody Sourc

Related Pathways

paperclip

#2440338   1987/07/24 Save this To Up

Enzyme-linked coagulation assay. III. Sensitive immunoassays for clotting factors II, VII, and X.

The solid-phase clotting assay utilizing fibrinogen coated on the wells of a microtiter plate and peroxidase-fibrinogen in solution as a substrate for thrombin (enzyme-linked coagulation assay, ELCA) has been modified for use as an immunoassay. Direct inhibition of factors II, VII, and X by polyclonal (rabbit) antibodies and of factor X by monoclonal antibodies has been demonstrated at high dilution of these antibodies and detection of the specific factors using ELCA. Using plates coated with a second antibody (goat anti-mouse IgG) as well as fibrinogen, monoclonal antibodies to factors X and VII were measured by binding the active factor to the plate and detection of the bound factor using ELCA. The assay was very sensitive, permitting the detection of as little as 0.2 ng/ml (30 pg/assay) of monoclonal antibody, or less than 0.4 ng/ml (60 pg/assay) of factor Xa. When plates were coated with monoclonal antibody to factor X and fibrinogen, the assay permitted the identification of distinct epitope specificities for two monoclonal antibodies to factor X by distinct competition of the monoclonal antibodies added in the solution phase for binding of factor Xa to the plate. This assay could be applied generally for immunoassay of clotting factors, and could have application in general as an immunoassay amplification system.

2966 related Products with: Enzyme-linked coagulation assay. III. Sensitive immunoassays for clotting factors II, VII, and X.

Mouse anti-chick type II Mouse anti-chick type II Mouse anti chick type II Mouse anti-chick type II Mouse anti-chick type II Mouse anti chick type II Mouse anti-chick type II Mouse anti-chick type II Mouse anti chick type II Mouse anti-chick type II Mouse anti-chick type II Mouse anti-chick type II

Related Pathways

paperclip

#6328693   1984/07/02 Save this To Up

Comparison of platelet fibrinogen receptors on intact and proteolytically-treated platelets by use of an anti-glycoprotein IIIa monoclonal antibody (MA 123).

A murine monoclonal antibody (MA 123) was selected by screening 153 supernatants of hybridoma cells secreting anti-human platelet antibodies for their ability to inhibit the fibrinogen-induced aggregation of chymotrypsin-treated platelets. MA 123 inhibited the binding of 125I-fibrinogen to ADP-stimulated intact human platelets and to platelets treated with chymotrypsin or pronase. Moreover, it inhibited the fibrinogen-induced aggregation of these platelet suspensions. The degree of inhibition was similar in each of the three types of platelets tested. The interactions of MA 123 with the 125I-labeled surface components of intact and chymotrypsin-treated platelets were studied by immunoprecipitation using Staphylococcus aureus coated with goat anti-mouse IgG, followed by SDS-polyacrylamide gel electrophoresis and autoradiography. MA 123 precipitated the glycoprotein IIb-glycoprotein IIIa (GPIIb-GPIIIa) complex from the surface of detergent solubilized intact human platelets; and it precipitated GPIIIa from the surface of chymotrypsin-treated platelets. Partially purified GPIIIa was also immunoprecipitated by MA 123. Our data suggest that the exposure of fibrinogen receptors by ADP, chymotrypsin or pronase, is associated with alterations of GPIIIa on the platelet surface.

1108 related Products with: Comparison of platelet fibrinogen receptors on intact and proteolytically-treated platelets by use of an anti-glycoprotein IIIa monoclonal antibody (MA 123).

Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti CML Monoclonal Antib Anti CML Monoclonal Antib Anti Human Macrophage Sur Anti malondialdehyde (MDA Anti-apoptotic marker in Anti-basement membrane ma Anti C Reactive Protein A MOUSE ANTI BOVINE ROTAVIR

Related Pathways