Search results for: Normal Antibody Diluent (Phosphate Buffered)
#25695439 2015/02/20 Save this To Up
Effects of pH changes of stock normal saline solution on 5 percent red cell suspension.The red cell suspension (RCS) is a universally used indicator system to demonstrate antigen and antibody reactions in vitro.Saline solutions that are used in its preparation are preferred to be fresh to avoid changes in pH that may affect the results. Thus,buffered saline such as phosphate-buffered saline (PBS) is the ideal diluent because its pH is maintained for a certain period. However,normal saline solution (NSS) is more commonly used because it is inexpensive and easy to make. pH changes in the saline solutions and the RCSs were monitored for 1 week. Macroscopic examination of changes in degree of redness of RCS was also observed. Red blood cell (RBC) indices of the ethylenediaminetetraacetic acid(EDT A)-anticoagulated blood used in the preparation of the RCS were measured in the performance of an automated complete blood count. Qualitative examination of the crenation of RBCs was done on the prepared blood smears and graded by three registered medical technologists. Percentage crenation was then determined using an improved Neubauer counting chamber. Three trials were performed, and results were averaged. Statistical analysis showed hat there were significant differences in the average pH of PBS and NSS and the average pH of RCS-PBS and RCS-NSS over 1 week. RBC indices measured in EDTA-anticoagulated donor blood showed no significant difference. Macroscopic examination of changes in degree of redness of the RCS showed that color darkened over 1 week but only by a small degree. Qualitative and quantitative examination of crenation of RBCs in RCS-PBS and RCS-NSS both showed no significant differences over 1 week. The experimental group (RCS-NSS) continuously showed a higher grade of crenation than the control group (RCS-PBS). Crenation of RBCs still manifests microscopically despite the lack of a significant relationship between the pH of the saline solutions and the degree and percentage of crenation. Crenation, therefore,cannot be attributed to pH alone but occurs as a result of other factors.
1675 related Products with: Effects of pH changes of stock normal saline solution on 5 percent red cell suspension.Phenol Red, sodium salt * Phenol Red Solution Normal Antibody Diluent Alcian Blue Solution, pH Alcian Blue Solution, pH Colloidal Iron Stock Sol Congo Red Solution Eosin-Phloxine Solution Giemsa Stock Solution Phosphotungstic Acid Hem Jenner Stock Solution May-Grunwald Stock Solut
#22444703 2012/03/26 Save this To Up
Administration of bovine anti-IGF-1 immunoglobulin to dietary protein deficient rats alters dietary intake and plasma IGF-1 binding profiles, but does not affect change in body mass.The potential of antibodies raised against insulin-like growth factor-1 (IGF-1) as a treatment to enhance the anabolic actions of IGF-1 has been demonstrated in both rodent and ruminant models. We investigated whether treatment of genetically normal rats with anti-IGF-1 immunoglobulin (Ig, raised in cattle) would enhance growth and if anti-IGF-1 Ig treatment would ameliorate live-weight loss in genetically normal rats offered a severely protein-restricted diet. Scatchard analysis was used to characterise ammonium sulphate precipitated bovine anti-IGF-1 Ig. Anti-IGF-1 Ig binding to 125I-IGF-1 yielded an almost linear Scatchard plot, with a Hill co-efficient of 0.951 ± 0.012, indicating a single class of IGF-1 binding sites. The affinity of anti-IGF-1 Ig for IGF-1 was 2.14 ± 0.66 × 109 l/mol. The non-immune Ig preparation did not bind IGF-1. Rats were offered either a diet with a normal protein level (20%) or protein restricted (4% protein), and each dietary group was further treated with twice-daily i.p. injections of either diluent phosphate buffered saline, non-immune Ig or anti-IGF-1 Ig. Dietary protein level had a significant effect on live-weight gain, but there was no effect of non-immune Ig or anti-IGF-1 Ig on live-weight gain. Treatment with anti-IGF-1 Ig prevented the significant depression of cumulative dietary intake observed in diluent, and non-immune Ig treated groups offered the 4% protein diet. The cumulative dietary intake of the anti-IGF-1 Ig treated, 4% dietary protein group did not differ significantly from those of the groups offered the 20% protein diet. In addition, within the 4% dietary protein group, rats treated with non-immune Ig exhibited a cumulative feed intake that was intermediate between that of the diluent treated and anti-IGF-1 Ig treated groups (P < 0.05). Size exclusion chromatography was used to characterise in vitro 125I-IGF-1 binding in end-point plasma from each treatment group. In comparison to control groups, anti-IGF-1 Ig treatment resulted in substantially increased 125I-IGF-1 binding in the 30 to 40 kDa region and a concomitant reduction in elution of free 125I-IGF-1. Protein restriction markedly depressed IGF-1 binding at ∼150 kDa in the plasma of diluent and non-immune Ig treated groups. Anti-IGF-1 Ig treatment was effective in preventing this decrease in ∼150 kDa binding. Thus, anti-IGF-1 Ig appears to have a beneficial effect on dietary intake in protein-restricted rats, which is associated with induced changes in IGF-1 binding profiles in plasma.
1218 related Products with: Administration of bovine anti-IGF-1 immunoglobulin to dietary protein deficient rats alters dietary intake and plasma IGF-1 binding profiles, but does not affect change in body mass.Rabbit Anti-Rat Androgen Goat Anti-Human Vitamin D Mouse Anti-Insulin-Like G Rat monoclonal anti mouse Rat monoclonal anti mouse Rat monoclonal anti mouse Rat monoclonal anti mouse Rat monoclonal anti mouse Hamster anti mouse Insuli Rabbit Anti-Human Toll In Human Insulin-like Growth Mouse Anti-Human IGF Anti
#7886694 1995/04/10 Save this To Up
Broad cytolytic specificity of myotoxin II, a lysine-49 phospholipase A2 of Bothrops asper snake venom.The cytotoxic activity of Bothrops asper myotoxin II, a lysine-49 phospholipase A2 isoform, on different cell types in culture, was investigated. Myotoxin II caused a dose-dependent cytolytic effect on all cell types tested, characterized by rapid release of cytoplasmic lactic dehydrogenase and drastic morphological cell alterations. Quantitative differences in the susceptibility to myotoxin II among cell types fell within a relatively narrow range, and in general, the toxin was cytolytic at concentrations of 50-100 micrograms/ml (3-7 microM), when assays were performed using culture medium as a diluent. Toxin activity was markedly enhanced if phosphate-buffered saline was utilized instead of medium. The cytotoxic activity of myotoxin III, an aspartate-49 isoform from the same venom, on both endothelial cells and skeletal muscle myoblasts was higher than that of myotoxin II, suggesting that, although phospholipase A2 activity is clearly not required for the induction of cell damage, it may have an enhancing role. In contrast to B. asper myotoxins, other basic phospholipases A2 with myotoxic activity in vivo (notexin from Notechis scutatus, and two enzymes isolated from Vipera russelli venom) did not affect endothelial cells and myoblasts. Pretreatment of cells with neuraminidase, tunicamycin, or protamine, did not alter their susceptibility to myotoxin II. At low temperatures (2-4 degrees C) myotoxin II was devoid of cytolytic effect. Washing and neutralization experiments using heparin with low affinity for antithrombin or mouse monoclonal antibody MAb-3 suggest that at low temperatures myotoxin II binds very weakly to the cells, and that its normal interaction with the putative target is probably not only based on charge, but that a membrane penetration event may be required.
1749 related Products with: Broad cytolytic specificity of myotoxin II, a lysine-49 phospholipase A2 of Bothrops asper snake venom.Allergens, Phospholipase Phospholipase A2 XIIA ant Recombinant Human Secrete Rabbit Anti-CPLA2 alpha P Rabbit Anti-CPLA2 alpha P Rabbit Anti-CPLA2 alpha P Rabbit Anti-CPLA2 alpha P Rabbit Anti-CPLA2 alpha P Rabbit Anti-CPLA2 alpha P Rabbit Anti-CPLA2 alpha P Rabbit Anti-CPLA2 alpha P Rabbit Anti-CPLA2 alpha P
#3114387 1987/10/20 Save this To Up
Calcium enhances the sensitivity of immunofluorescence for pemphigus antibodies.Indirect immunofluorescence (IF) to detect pemphigus and pemphigoid autoantibodies is commonly performed with monkey esophagus (ME) as substrate and phosphate-buffered saline (PBS) as a diluent. The purpose of this study was to evaluate comparative IF titers using human skin (HS) as substrate with variations in the buffers employed. Substrates (ME or HS) were incubated in PBS, Tris-acetate-buffered saline (TAS), TAS with 5 mM CaCl+2 (TAS-Ca+2), and PBS or TAS with 1 mM EDTA, prior to incubation with pemphigus or pemphigoid sera for indirect IF. We examined sera from 11 patients with pemphigus vulgaris (PV), 10 patients with Brazilian pemphigus foliaceus (BPF), and 4 patients with bullous pemphigoid. In 20 of 21 pemphigus sera, endpoint indirect IF titers were highest on normal skin with TAS-Ca+2. Six sera (2 PV and 4 BPF) had endpoints that were 5 double dilutions higher than the endpoints obtained with ME and PBS. Six sera (3 PV and 3 BPF) were 4 double dilutions higher, 7 sera (3 PV and 4 BPF) were 2-3 double dilutions higher, and 2 PV sera were equivalent with both substrate/buffers. Preincubation of either tissue with EDTA prior to indirect IF abolished PV and BPF antibody binding completely. Exposure to EDTA after the tissue was incubated with PV or BPF sera did not affect indirect IF titers. In the presence of Ca+2, the antigen was resistant to trypsin in concentrations of 0.001%; however, in the absence of added Ca+2 it was destroyed by 0.0001% trypsin. These differences were not observed with bullous pemphigoid sera; all 4 sera had similar endpoint indirect IF titers. This study shows a significant increase in the sensitivity of indirect IF assays for pemphigus autoantibodies by the use of Ca+2-supplemented buffers on human skin. This finding may also have implications for procedures designed to purify and/or detect pemphigus antigens.
1955 related Products with: Calcium enhances the sensitivity of immunofluorescence for pemphigus antibodies.Rat Anti-CCT theta Antibo Rabbit Anti-Theophylline Sheep Anti-Theophylline 3 Multiple organ cancer tis Multiple organ tumor tiss Mouse Anti-Bacteroides th Cellufine Formyl , 50 ml Cellufine Formyl Media Cellufine Formyl , 500 ml Cellufine Formyl Media Cellufine Formyl Media Calcium Stain Kit (Modif
#7042969 1982/07/22 Save this To Up
A quantitative indirect immunofluorescent assay for zona pellucida antibodies.A dilution series of a standard antiserum, raised in rabbit, against intact porcine oocytes was tested by an indirect immunofluorescent assay under a variety of conditions. Maximal antibody binding was obtained in phosphate-buffered saline with sucrose and sodium azide as a serum diluent and wash buffer, with relatively long incubation and wash periods, and in some cases heat-inactivation of sera. Factors found to influence the antibody binding were: alteration of the zonae by fixation; the presence of sucrose, galactose or glycerol; addition of protein to the buffer; heat inactivation of serum; substitution of phosphate by borate buffer; and replacement of the labelled second antibody by labelled Protein A. Antisera produced against acid- and heat-solubilized zonae differed from the standard antiserum in their binding capacity.l Control sera (anti-porcine spleen, adjuvant injected, and normal) were all completely negative.
1582 related Products with: A quantitative indirect immunofluorescent assay for zona pellucida antibodies.QuantiChrom™ Formaldehy EIA for Quantitative Dete EIA for Quantitative Dete zona pellucida binding pr Glucose Assay With the La Cultrex In Vitro Angiogen Endothelial Tube Formatio QuantiChrom™ LDH Cytoto QuantiChrom™ Nitric Oxi QuantiChrom™ Acetylchol QuantiChrom™ α-Amylase QuantiChrom™ Formaldehy
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