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Inflammatory cell expression of Toll-like receptor-2 (TLR2) within refractory periapical granuloma.

Toll-like receptor-2 (TLR2) is highly important within the immune system. Characterization of the expression of TLR2 within inflammatory cells in periapical lesions could help in diagnosis and management of refractory cases. The aim of the study is identification of Toll-like receptor (TLR2) through immunohistochemical and immunofluroscence expression in inflammatory cells within refractory periapical granuloma cases. Eight cases of refractory periapical granuloma were selected out of 772 cases. Histological examination and immunohistochemical staining with polyclonal rabbit antihuman TLR2, monoclonal mouse antihuman CD38, CD68 and CD83 primary antibodies, as well as immunofluorescence staining with goat anti-rabbit TLR2, donkey anti-mouse CD38, CD68 and CD83 primary antibodies was conducted. Positive controls, negative controls and experimental sections with no primary antibody were included in the study. Qualitative analysis and double immunofluorescence technique was used to characterize the TLR cells. In periapical granuloma, lymphocytes (CD38 cells) expressed the most amount of TLR reactivity followed by macrophages (CD68 cells), and odontogenic epithelial cells. Neutrophils, red blood cells (RBCs) and collagen ground substance were negative to TLR2.  TLR2 was highly expressed by lymphocytes and plasma cells indicative of their major role in the inflammatory process and antigen recognition in refractory periapical granuloma. Dendritic cells expressing TLR2 were low in number suggesting a minor role in sustaining these lesions.

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Human Killer cell immunog Rat Toll Like Receptor 2( Rat monoclonal anti mouse Pressure Injection Cell w Adenosine A2b Receptor Androgen Receptor Ab-1 An Rabbit Anti-Cell death in Bradykinin receptor B1 An Activin receptor-like kin Rabbit Anti-Human Toll-Li Glucagon receptor Mouse Anti DO11.10 T cell

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Modification of solid phase red cell adherence assay for the detection of platelet antibodies in patients with thrombocytopenia.

Platelet refractoriness is caused by HLA antibodies and platelet-specific antibodies. Current methods used to detect antiplatelet antibodies have limitations. Solid phase red cell adherence (SPRCA) lacks sensitivity and requires a second assay using chloroquine-treated intact platelets to specify the response due to anti-HLA. We modified SPRCA by using 2 types of antihuman platelet antibodies with different specificities toward platelet lysate and tested samples from 361 patients (69 with unexplained thrombocytopenia and 292 with poor response to platelet transfusions not explicable by alloimmunization or the clinical situation) and 50 from healthy volunteers. Our method compared favorably with platelet suspension direct immunofluorescence. All samples from healthy volunteers were negative; of the samples from the patient population, 240 were positive (147 samples had only antiplatelet and 3 samples had only anti-HLA antibodies). This modified technique had a sensitivity of 98% and a specificity of 91%.

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Immunohistochemical identification of erythroid precursors in paraffin embedded bone marrow sections: spectrin is a superior marker to glycophorin.

To investigate whether spectrin can be used as an immunohistochemical marker for erythroid precursors in routinely processed paraffin embedded bone marrow sections.

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Mouse Anti-Ca19.9 Sialyl Bone marrow tumor and adj Mouse AntiCytokeratin (ke Mouse AntiNQO1 Target Ant Mouse Anti hPTH PTH rP Ta Mouse AntiCytokeratin (ke Mouse AntiNQO1 Target Ant Bone marrow tumor and nor Mouse AntiHuman TGF beta Mouse AntiCytokeratin (ke Rabbit AntiAPPL1 Target A Mouse AntiCytokeratin (ke

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Antibodies against macaque monoclonal immunoglobulin G in rheumatoid arthritis.

The presence of rheumatoid factors (RF) in the serum of rheumatoid arthritis (RA) patients is commonly evidenced by agglutination tests: the Waaler-Rose assay, based on the use of human red blood cells (RBCs) coated with rabbit anti-RBC antibodies, and the latex test, which uses latex particles coated with denatured human immunoglobulin G (IgG). The aim of the present study was to characterize the RF able to agglutinate human RBCs coated with macaque antihuman RBC IgG antibodies secreted from macaque-mouse heterohybridomas (two from rhesus monkey and one from crab-eating macaque). Human RBCs coated with macaque monoclonal antibodies (MacMoAbs) were used for agglutination tests and these were carried out in parallel with standard tests (Waaler-Rose and latex agglutination tests) on sera from 82 RA patients, 86 patients with other forms of inflammatory chronic arthritis and 47 healthy human subjects. MacMoAb-coated RBCs identified RF in the sera of 66% patients with RA. By contrast, the frequency of positive sera in other inflammatory diseases was 5% and all 47 healthy controls were negative. Antimacaque IgG antibodies were found to be more specific for RF than standard tests, in the sera of patients with RA.

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The monoclonal antibody-specific immobilization of erythrocyte antigens assay (MAIEA) in the investigation of human red-cell antigens and their associated membrane proteins.

The monoclonal antibody-specific immobilization of erythrocyte antigens (MAIEA) technique is an immunoassay devised primarily for locating blood group antigens on specific red-cell membrane proteins. The assay involves the incubation of intact red cells with two antibodies, one human alloantibody, the other a nonhuman antibody, usually a rodent monoclonal antibody, but polyclonal antibodies of rabbit origin have been utilized. For a positive result, both antibodies must bind to the same membrane protein. The red cells are lysed, the membrane solubilized and the trimolecular complex of two antibodies and membrane protein is captured in a well coated with goat antirodent (or rabbit) immunoglobulin. The immobilized complex is then detected by the use of peroxidase-conjugated goat antihuman (or rodent) immunoglobulin. Negative results, due to mutual blocking between the human and animal antibodies when their epitopes are close together on the same molecule, have permitted a degree of localization of epitopes on some proteins. This has been most effective in the mapping of Cromer blood group system antigens on the complement control protein domains of decay-accelerating factor (DAF, CD55), but has also proved informative in the clustering of antigens on the Lutheran and Kell glycoproteins. MAIEA is an effective tool for the identification of antibodies to Knops-system antigens on complement receptor 1 (CR1, CD35) in immunohaematology reference laboratories. These antibodies are clinically unimportant, but must be identified before they can be ignored for transfusion purposes.

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[Capture-R Ready-ID and DiaMed-ID for identification of erythrocyte bound antibodies after acid elution].

The DiaMed-ID (D-ID) gel system is known to be a very sensitive and specific method for the detection of red cell antibodies. In various cases, we failed to find an antibody in the eluate in which red-cell-bound antibodies (IgG) where proven by a positive direct antiglobulin test (DAT). SPRCA (Capture-R, Ready Screen, Immucor; C-R) seems also to be very sensitive, in part due to the antihuman, IgG-coated indicator cells. Therefore, we compared 39 acid eluates from patients who had a positive DAT (monospecific rabbit antihuman IgG) both in the D-ID and in the C-R system. Patients (19 female, 20 male; mean age 62 years) were suspected either to have an autoimmune hemolytic anemia or an alloantibody. Identification of the antibodies was done with the system's own panel cells. Agglutination strength was scored from 1 to 4. Quantification of selected eluates was performed by titration, using the same cells in both systems. From 39 eluates, 31 were positive in the C-R and 25 in the D-ID. Nine eluates were negative in the C-R and 14 in the D-ID. If only eluates with a DAT reaction strength of 2 or lower were considered, obviously more negative results were found with the D-ID technique (p < 0.027) than with the C-R technique. In all eluates the degree of test reaction was stronger in the C-R system. However, titration endpoints of 6 quantified antibodies did not differ significantly. In 2 patients with slightly positive DAT, antibody typing was negative or not clear in the serum. In the corresponding eluates, an anti-K and an anti-JKa could be identified only by the C-R technique. In such instances we recommend to use the C-R technique to prevent transfusion complications.

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Primary antibody GFR alp IDH2 antibody Source Rabb Cytokeratin AE1 (Acidic) EXOTESTTM ready to use ki Mouse Anti-Human CD34 Tar Rabbit Anti-Human Erythro Cytokeratin AE1 (Acidic) Rabbit Anti-Human Androge IDELISA™ Forensic Tetra EXOTESTTM ready to use ki IDH3G antibody Source Rab Rat monoclonal anti mouse

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Identification of IgM as the leprosy patient serum factor responsible for rapid sedimentation of formolized sheep erythrocytes.

The serum of some leprosy patients with impaired specific cellular immunity for Mycobacterium leprae causes rapid sedimentation of formolized sheep erythrocytes, a phenomenon known as the Rubino reaction. The Rubino factor was precipitated from positive sera by 5% (w/v) polyethylene glycol (PEG), bound to a concanavalin A (ConA)-Sepharose column and eluted with D-mannose, and was also eluted from a Mono Q column, pH 8.0, with 0.4 M NaCl. The Rubino factor was eluted in a volume which coincided with that of human serum IgM from a Sepharose 6 column. IgM was present in the preparation obtained by this sequence of chromatographic procedures. The correspondence of IgM with the Rubino factor was demonstrated by the following data: a) the Rubino factor was adsorbed to rabbit IgG antihuman IgM-agarose and the activity was recovered in the acid eluate of the column; b) the Rubino reaction was inhibited in the presence of rabbit antihuman IgM antibodies. This behavior was not observed when the same procedures were carried out using anti-alpha 2-macroglobulin antibodies as a control. The rapid sedimentation of formolized sheep red cells caused by the serum of lepromatous leprosy patients was not inhibited by phenolic glycolipid-I, suggesting that the IgM responsible for the Rubino reaction is not directed to this antigen which is specific for M. leprae. There was no correlation between the positivity of the Rubino reaction and the increase in total serum IgM levels observed in 42% of the lepromatous patients evaluated. The demonstration that the Rubino factor is an IgM now permits the identification of the epitope recognized by it, and this may be used as a tool to understand the specific cellular immune unresponsiveness which characterizes lepromatous leprosy.

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Transcription Factors: T Ofloxacin CAS Number [824 Sheep serum Mouse Factor X total anti Cultrex In Vitro Angiogen Sheep Anti-Human CFB Fact Anti-ADAMTS-13 (A Disinti Sheep Complement Serum 25 Mouse Anti-Insulin-Like G Sheep anti mouse factor I Antibodies, Sheep: FITC Sheep Serum 100ml

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Immunohistochemical studies on postmortem lividity.

An immunohistochemical investigation of postmortem lividity was performed to illuminate localization of hemoglobin (Hb) and the mechanism of fixed lividity. The fixed lividity was defined as an unfading phenomenon by thumb finger pressure. Skin specimens were taken from 68 autopsy cases 7.5-336 h (2 weeks) postmortem. Localization of Hb of the specimens was examined by a labeled streptabidin biotin (LSAB) method using polyclonal (rabbit antihuman hemoglobin antibody) and monoclonal (mouse anti-human hemoglobin monoclonal antibody) antibodies. Positive staining for Hb was observed in various sites of the skin, i.e. in only intravascular erythrocytes, in vascular walls and perivascular tissue including sweat glands and sebaceous glands, in the dermal connective tissue, and in almost all of skin tissue except the horny layer. The diffusion of Hb into skin tissue was observed in 20 of 41 displaceable lividity cases (49%) and 11 of 27 fixed lividity cases (41%). Compared to displaceable lividity, superficial plexi in fixed lividity were filled with erythrocytes, which were markedly immunodetected. These findings support the hypothesis that the fixation of lividity is not due to diffusion of Hb into skin tissue but hemoconcentration in blood vessels.

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Polyclonal rabbit gamma globulins against a human cytotoxic CD4+ T cell clone. I. Clone characteristics and antiblast globulin preparation.

Antihuman lymphocyte rabbit (or horse) gamma globulins used in recipients of organ transplantation are prepared against thymocytes or immortalized cell lines, the only two sources so far allowing enough antigen preparation. These cells lack, however, the surface determinants characteristic of alloreactive blasts involved in the rejection process. We have derived long-term cultures of a panel of alloreactive (untransformed) clones from a rejected kidney. Among them, clone 1E7 has been chosen as a cytotoxic CD4+ (CD2+ CD3+ TCR alpha beta+) clone proliferating against HLA-DR8 targets. This clone (clonality assessed on T cell receptor genomic rearrangements) has been grown using weekly stimulations with the kidney donor-derived EBV cell line and recombinant IL-2. Clone cultures have been adapted to mass production after optimization of culture conditions satisfying pharmaceutical requirements. This procedure warranted a reproducible source of antigen since the functional and phenotypic characteristics of the immunizing 1E7 cells remained identical through the life span of the culture. In addition, the study of the total growth capacity of 1E7 cells showed consistent expansion until the 40th cell cycle, ensuring a progeny that will satisfy the large-scale requirement for a clinical trial. Rabbits were injected with 100 x 10(6) 1E7 cells (21, 14, and 7 days before bleeding). Sera were depleted of agglutinin by red blood cell absorption and globulin antiblast (GAB) prepared by SO4Na precipitation and ion exchange chromatography; 50% complement-mediated target cell lysis and 50% inhibition of E rosette formation and alloproliferation were obtained at GAB dilutions of about 1:250-1:500. Prescreened on cynomolgus monkeys, GAB could significantly prolong skin grafts when given prophylactically. Finally GAB have been used in human recipients of kidney grafts for prophylaxis of early rejection. Results of this pilot study are given in a separate report in this issue. In conclusion we have, for the first time, set up a large-scale preparation of polyclonal globulin against a normal human alloreactive clone, and this new reagent should present several advantages over classic antilymphocyte or antithymocyte sera because it contains specificities against activation antigens and has less crossreactivity variation among batches.

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Polyclonal antibody: Huma anti CD38 Hematopoietic p Rabbit Polyclonal to Myco RABBIT ANTI GSK3 BETA (pS anti Transferrin receptor Rabbit Anti-THAP1 Polyclo anti Cortical thymocytes PLC gamma2(phospho Tyr121 Rabbit Anti-Phospho-MLK3( Rabbit Anti-gamma tubulin Rabbit Anti-TSLP (human) Rabbit Anti-gamma tubulin

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Antihuman plasma glutathione peroxidase antibodies: immunologic investigations to determine plasma glutathione peroxidase protein and selenium content in plasma.

Plasma glutathione peroxidase (GSHPx) (glutathione: H2O2 oxidoreductase) is a unique selenoglycoprotein. Treatment of this enzyme with glycopeptidase F partially deglycosylates it and establishes the presence of N-linked sugar moieties. Antibodies raised in a rabbit against the purified enzyme from plasma were found to be specific, noninhibitory, and capable of precipitating the enzymatic activity. The antibodies precipitated greater than 90% of the GSHPx activity of normal plasma, thus indicating that the selenoenzyme is the main if not the sole GSHPx activity of plasma. The antibodies did not precipitate RBC GSHPx. A slight cross-reactivity of the antibodies was found with rat plasma GSHPx. A GSHPx activity precipitation assay of normal plasma in the presence of selenium (Se)-deficient plasma indicates that no cross-reactive protein in the Se-deficient plasma interferes with the precipitation of the GSHPx activity from normal plasma. Thus, GSHPx protein as well as activity is deficient in plasma in the absence of Se. Antibodies against GSHPx either from RBCs or from plasma were used to specifically immunoprecipitate most of the GSHPx activity from RBCs or plasma, respectively, in healthy individuals to determine the amount of Se associated with the protein. GSHPx accounts for approximately 15% of the Se in RBCs and 12% of the Se in plasma. Thus, in normal individuals, these proteins account for only a fraction of plasma and RBC Se.

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Goat Anti-Human Glutathio Goat Anti-Human Glutathio Prolactin-Inducible Prote Proteins and Antibodies H Bovine prolactin-induced Plasma Proteins: Corn Try Rabbit Plasma US Origin I Native Human Kallikrein, Rabbit Plasma US Origin I Glutathione peroxidase 4 Plasma Proteins: Human Ka Chicken craniofacial deve

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