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           Search results for: Rabbit Anti-OPN (rat, mouse) Polyclonal Antibody, PE-Cy3 Conjugated   

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#27494306   2016/09/16 Save this To Up

Facile Preparation of Stable Antibody-Gold Conjugates and Application to Affinity-Capture Self-Interaction Nanoparticle Spectroscopy.

Protein-nanoparticle conjugates are widely used for conventional applications such as immunohistochemistry and biomolecular detection as well as emerging applications such as therapeutics and advanced materials. Nevertheless, it remains challenging to reproducibly prepare stable protein-nanoparticle conjugates with highly similar optical properties. Here we report an improved physisorption method for reproducibly preparing stable antibody-gold conjugates at acidic pH using polyclonal antibodies from a wide range of species (human, goat, rabbit, mouse, and rat). We find that gold particles synthesized using citrate alone or in combination with tannic acid are similar in size but display variable colloidal stability when conjugated to polyclonal antibodies. The variability in conjugate stability is due to differences in the pH and composition of the original gold colloid, which prevents reproducible preparation of stable antibody conjugates without additional purification of the particles prior to conjugation. Sedimentation-based purification of gold particles synthesized using different methods enabled reproducible generation of antibody-gold conjugates with high stability and similar plasmon wavelengths. We also find that antibody conjugates prepared using our improved procedure display excellent performance when applied to a high-throughput immunogold assay (affinity-capture self-interaction nanoparticle spectroscopy, AC-SINS) for identifying monoclonal antibodies with low self-association, high solubility, and low viscosity. The stable antibody conjugates prepared with various types of gold colloid result in robust and reproducible AC-SINS measurements of antibody self-association using extremely dilute (microgram per mL) and unpurified antibody solutions. We expect that this improved methodology will be useful for reproducibly preparing stable antibody-gold conjugates for diverse applications.

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TOM1-like protein 2 antib TOK-1 alpha antibody Sour TOM1L1 antibody Source Ra PRDX1 Antibody Peptide-af Rabbit Anti-CLCA4 Polyclo Rabbit Anti-GPR78 Polyclo MOUSE ANTI BOVINE ROTAVIR Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Shiga Toxin 1 antibody, M

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#27617027   2016/09/12 Save this To Up

Chi-Ju-Di-Huang-Wan protects rats against retinal ischemia by downregulating matrix metalloproteinase-9 and inhibiting p38 mitogen-activated protein kinase.

Retinal ischemia is a retinal disorder related to retinal vascular occlusion, glaucoma, diabetic retinopathy and age-related macular degeneration. The study aimed to evaluate the protective effects and underlying mechanisms of Chi-Ju-Di-Huang-Wan (CJDHW) against retinal ischemia in rats.

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Human Serine threonine-pr Human Matrix metalloprote Rat matrix metalloprotein ELISA Human , Matrix Meta ELISA Human , Cartilage O Anti-Serine Threonine-Pro anti-ATM Protein Kinase p Anti-ATM Protein Kinase p Anti-ATM Protein Kinase p Anti-ATM Protein Kinase p Anti-ATM Protein Kinase S Mouse Anti-Human Matrix M

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#25333799   2014/10/22 Save this To Up

Synthetic teichoic acid conjugate vaccine against nosocomial Gram-positive bacteria.

Lipoteichoic acids (LTA) are amphiphilic polymers that are important constituents of the cell wall of many Gram-positive bacteria. The chemical structures of LTA vary among organisms, albeit in the majority of Gram-positive bacteria the LTAs feature a common poly-1,3-(glycerolphosphate) backbone. Previously, the specificity of opsonic antibodies for this backbone present in some Gram-positive bacteria has been demonstrated, suggesting that this minimal structure may be sufficient for vaccine development. In the present work, we studied a well-defined synthetic LTA-fragment, which is able to inhibit opsonic killing of polyclonal rabbit sera raised against native LTA from Enterococcus faecalis 12030. This promising compound was conjugated with BSA and used to raise rabbit polyclonal antibodies. Subsequently, the opsonic activity of this serum was tested in an opsonophagocytic assay and specificity was confirmed by an opsonophagocytic inhibition assay. The conjugated LTA-fragment was able to induce specific opsonic antibodies that mediate killing of the clinical strains E. faecalis 12030, Enterococcus faecium E1162, and community-acquired Staphylococcus aureus strain MW2 (USA400). Prophylactic immunization with the teichoic acid conjugate and with the rabbit serum raised against this compound was evaluated in active and passive immunization studies in mice, and in an enterococcal endocarditis rat model. In all animal models, a statistically significant reduction of colony counts was observed indicating that the novel synthetic LTA-fragment conjugate is a promising vaccine candidate for active or passive immunotherapy against E. faecalis and other Gram-positive bacteria.

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Mouse Anti-Gram Positive Acid Fast Bacteria (AFB) Acid Fast Bacteria (AFB) SYNTHETIC S ADENOSYL L HO Polyclonal anti conjugate Rabbit Anti-IAA (Indole-3 Rabbit Anti-IAA (Indole-3 Rabbit Anti-IAA (Indole-3 Rabbit Anti-IAA (Indole-3 Rabbit Anti-IAA (Indole-3 Rabbit Anti-IAA (Indole-3 Rabbit Anti-IAA (Indole-3

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#18228334   2008/01/29 Save this To Up

Production of polyclonal antisera.

Polyclonal antibody preparations contain multiple antibody molecules recognizing different epitopes on an antigen molecule. Good quality polyclonal antisera are useful for a number of applications-e.g., immunoprecipitation, immunoblotting, and ELISAs-where the binding of more than one antibody molecule per antigen molecule improves the sensitivity of the assay. It is possible to produce polyclonal antibodies in a variety of species, and this make it possible to detect multiple immunoreactions. The protocols in this unit describe the production of polyclonal antisera specific for protein antigens in rabbits, rats, mice, and hamsters using complete Freund's adjuvant (CFA) or other adjuvants. In addition, the unit presents a method for preparing serum from blood. Polyclonal antipeptide antisera can be produced by substituting carrier-conjugated peptides for the purified protein antigens.

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Custom Polyclonal Antibod Anti VGLUT-1 Rat, polyclo Anti VGLUT 1 Rat, polyclo Anti VGLUT 1 Rat, polyclo Rabbit Polyclonal to Myco GSK3â(Phospho Ser9) Anti c Jun (Phospho Ser73) Ant Elk 1 (Phospho Ser383) An PDK1 (Phospho Ser241) Ant Raf1 (Phospho Ser259) Ant GSK3á (Phospho Ser21) An MEK 2 (Phospho Thr394) An

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#15038619   2004/03/24 Save this To Up

A competitive ELISA for albumin in rat urine.

Nephropathy is characterized by urinary micro albumin. Rats are usually used in experimental studies. But, there was no specific and simple method for detecting rat urinary albumin. A specific, easily performed, and sensitive method for quantitatively determining rat urinary albumin is needed. Using rabbit anti-rat albumin polyclonal antibody, biotinylated goat anti-rabbit IgG, avidin conjugated peroxidase, and TMB (3,3',5,5'-tetramethylbenzidine) as substrate, a competitive ELISA for rat albumin in urine was developed. With this method, the urinary albumin in diabetic and normal rats was detected. This method was sensitive to 30 ng/mL and reproducibly quantifies rat urinary albumin levels in the range of 0.05-5 microg/mL. The rabbit anti-rat albumin polyclonal antibody showed no cross reaction with bovine and human serum albumins and rat IgG, and showed little cross-reaction with mouse albumin. The intra-assay CV was less than 10%. The urinary albumin markedly increased in diabetic rats. Since quantifying urinary albumin was very important in the experimental study of diabetic nephropathy, the results from our experiments indicated that this competitive ELISA could be used for quantification of rat urinary albumin.

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Glucagon ELISA KIT, Rat G Beta Amyloid (42) ELISA K GLP 1 ELISA Kit, Rat Gluc Beta Amyloid (40) ELISA K Rat intestinal fatty acid Rat Visceral adipose spec Rat Albumin ELISA Kit ELRGCI Rat IgG anti chick ELRGBI Rat IgG anti bovin ELRGPI Rat IgG anti porci ELRGRI Rat IgG anti rat t ELRGHI Rat IgG anti human

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#15020090   2004/03/15 Save this To Up

Dual enhancement of triple immunofluorescence using two antibodies from the same species.

Triple immunofluorescence method with two mouse monoclonal antibodies and another rabbit polyclonal antibody was established with catalyzed reporter deposition (CARD) amplification on thick floating sections from the rat cerebellum. One of the monoclonal antibodies (anti-calbindin), diluted maximally, probed with anti-mouse IgG-horseradish peroxidase (HRP) and amplified with Cy5-conjugated tyramide, immunolabeled cerebellar Purkinje cells and their arborization. Subsequently, a rabbit polyclonal IgG (anti-glial fibrillary acidic protein (anti-GFAP)), probed with anti-rabbit IgG-HRP, amplified with biotin-tyramide and visualized with fluorescein-isothiocyanate (FITC)-streptavidin, immunolabeled Bergmann's glia. Another mouse monoclonal IgG (anti-SNAP25), probed with anti-mouse IgG-rhodamine without CARD amplification, selectively visualized synaptic sites, because the maximal dilution of the other monoclonal antibody (anti-calbindin) was below the detection threshold of this anti-mouse IgG-rhodamine. Separation of the two signals (calbindin and SNAP25), each detected through mouse monoclonal antibody, was then based on the difference of sensitivity either with or without CARD amplification. Triple immunofluorescence is possible when just one of the three primary antibodies is from different species. Intensification of two of the three signals provides further advantages to examine immunolocalization of multiple epitopes on histological sections.

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TCP-1 theta antibody Sour Anti-SARS Spike Protein I Mouse Anti-SARS Nucleocap Mouse Anti-SARS Spike IgG Anti-SARS Nucleocapsid Pr Rat Anti-CCT theta Antibo Rabbit Anti-Theophylline Sheep Anti-Theophylline 3 Goat Anti-Human Dual oxid Mouse monoclonal anti-fla Multiple organ cancer tis Multiple organ tumor tiss

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#10989131   2000/12/11 Save this To Up

Design and application of a polyclonal peptide antiserum for the universal detection of leptin protein.

An epitope-specific polyclonal antiserum was produced in rabbits immunized against a synthetic 15 amino acid peptide (QRVTGLDFIPGLHPV) derived from the coding sequence reported for the porcine leptin gene (GenBank Accession No. U59894). This peptide contains a core sequence comprised of eight amino acids (GLDFIPGL) that is totally conserved in all leptin proteins studied to date. Purified recombinant human, mouse, rat, pig, and chicken leptin proteins were separated by polyacrylamide gel electrophoresis (SDS-PAGE) and electro-blotted onto PVDF membranes. Western blots were developed employing the leptin-specific peptide antiserum with an alkaline-phosphatase-conjugated anti-rabbit IgG second antibody chromogenic system. The peptide antiserum was found to be highly specific for leptin which exhibited an estimated molecular weight of about 16 kDa for all species analyzed. The sensitivity of the Western blot assay was not sufficient to permit the direct detection of leptin in chicken serum or plasma. However, with this assay we were able to detect native leptin protein in an enriched fraction prepared from chicken plasma using a combination of gel filtration and ion exchange column chromatography. Slot blots indicated a potential application of the immunostaining technique for quantitative analysis of leptin protein. Finally, the peptide antiserum was successfully employed to localize leptin protein by immunohistochemical staining of thin sections prepared from adipose (chicken and pig) and liver (chicken) tissue samples. This study is the first to report a polyclonal peptide antiserum that apparently recognizes intact leptin protein, both native and recombinant, regardless of the species of origin.

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NATIVE HUMAN PROLACTIN, P RABBIT ANTI GSK3 BETA (pS Polyclonal Antibody Bone Rabbit Anti-Streptavidin Rabbit Anti-WNK3 protein Rabbit Anti-WNK3 protein Rabbit Anti-PRRSV M prote Rabbit Anti-PRRSV M prote Rabbit Anti-PRRSV M prote Rabbit Anti-HE4 Epididyma Rabbit Anti-HE4 Epididyma Rabbit Anti-Rex1 Zinc fin

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#10727257   2000/05/09 Save this To Up

Development of time-resolved immunofluorometric assays for rat follicle-stimulating hormone and luteinizing hormone and application on sera of cycling rats.

The aim of this study was to develop time-resolved immunofluorometric assays (TR-IFMA) for measuring rat (r)FSH and rLH. The advantages of these IFMAs are higher sensitivity due to lower background values, higher specificity as only intact molecules of FSH and LH can be measured, and a very long shelf life of the nonradioactive biotin antigens compared with radiolabeled iodine antigens. For rFSH, IFMAs are lacking, while for rLH, if present, the resources for antibodies are scarce or the mouse monoclonal antibodies (mMAbs) against LHalpha are inactive with FSH. Thus specific antibodies need to be obtained. With the final TR-IFMAs, rFSH and rLH levels were assessed during the estrous cycle and compared with those obtained with the more classical RIAs and fluoroimmunoassays (FIAs). Two IFMAs for rFSH were developed with mMAbs against the recombinant human (rec h)FSHbeta subunit (FSH56A) attached to the wall and two different rabbit polyclonal antibodies (PAbs) against the alpha subunit of rec hFSH (R93-2705) or recombinant rat (rec r)LH (R95-2715) conjugated with biotin as signal antibody. With both IFMAs, rFSH holo-molecules can be measured. Rat FSH standards could be assessed between 0.02 and 10 ng/ml with a detection limit of 0.05 and 0.24 ng/ml in buffer and serum, respectively. These detection limits in four IFMAs were 8- to 16-fold lower than those in RIAs and FIAs. This detection level allowed the measurement of FSH levels in serum of hypophysectomized (HYPEX) rats at 0.18 ng/ml. In serum of cycling rats, the FSH levels of the IFMA were 2-fold lower than those of the FIA, while in ovariectomized (OVX) rats the IFMA levels were comparable. A peak level of FSH was found during proestrus of Day 2 and gestation with both RIA and FIA, but with IFMAs at gestation only. An IFMA for rLH was set up with mMAb (hCG77A) reacting with rLHbeta as capture and rabbit PAb to rec rLHalpha (R95-2712) as signal antibody. Rat LH standard could be assessed between 0.001 and 10 ng/ml with a detection limit of 0.012 and 0.1 ng/ml in buffer and serum, respectively, which was 8-fold lower than that in RIA/FIA. In serum of HYPEX rats, LH was undetectable (< 0.04 ng/ml), whereas a high background level of 2.5 ng/ml was measured in the FIA. In serum of cycling rats, only a very low LH level of 0.14 ng/ml was measured, which strongly deviated from the level of 3.46 ng/ml with an FIA. The load of LH in serum of OVX rats was 2.91 ng/ml, which was 12-fold lower than that for the FIA. The peak level of LH was detected on proestrus Day 2 with RIA, FIA, and IFMA. In conclusion, two IFMAs for rFSH and one for rLH have been developed with high sensitivity and specificity for intact gonadotropins. The LH pattern during the estrous cycle was comparable between IFMA, RIA, and FIA, although the overall level in the IFMA was much lower, as were HYPEX levels. The FSH pattern differed only on proestrus Day 2 in the IFMA from that of RIA/FIA, showing a peak level with RIA/FIA and a basal level with the IFMA. This implies that in RIA/FIA measurements, proteins other than intact FSH and LH interfere with the analysis at proestrus Day 2 for FSH and in HYPEX, cycling, and OVX rats for LH.

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Rat follicle-stimulating Rat Thyroid Stimulating H GLP 1 ELISA Kit, Rat Gluc Follicle Stimulating Horm Mouse Anti-Human Follicle Mouse Anti-Follicle Stimu Rabbit Anti-Follicle Stim Luteinizing Hormone Relea MOUSE ANTI HUMAN LUTEINIZ Rat adrencocorticotropic Rat growth hormone releas Glucagon ELISA KIT, Rat G

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#9286275   1997/09/15 Save this To Up

Expression of major histocompatibility complex molecules in rodent retina. Immunohistochemical study.

In Lewis rats, S-antigen-induced intraocular inflammation, which occurs initially in the retina, is mediated by T cells requiring major histocompatibility complex (MHC)-restricted antigen presentation. In such organ-specific inflammation, antigen presentation may take place at the site of the initial inflammatory response. In the present study an attempt was made to determine the presence of the putative antigen-presenting cells in the retina of rats.

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Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon DNA (cytosine 5) methyltr Mouse Anti-Major Histocom Mouse Anti-Major Histocom Mouse Anti-Major Histocom Mouse Anti-Major Histocom Mouse Anti-Major Histocom Mouse Anti-Major Histocom Mouse Anti-Major Histocom

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#8726217   1996/10/09 Save this To Up

Immunoperoxidase staining of tumors by an antibody to Xenopus pNiXa.

pNiXa, a serpin from oocytes and embryos of Xenopus laevis, was tested as a tumor marker in human and rodent tissues. A peptide corresponding to the histidine-rich domain of pNiXa was conjugated and administered to rabbits to produce a polyclonal antibody, which was purified by antigen-affinity and used for immunoperoxidase staining of formalin-fixed, paraffin-embedded tissue sections. Staining with pNiXa-antibody was positive in 23/187 human tumors (12 percent) and negative in 119 specimens of normal human tissues. Positive reactions were more frequent in liver (38 percent) and colon (34 percent) tumors than breast (18 percent), prostate (9 percent), mesothelioma (20 percent) or lung (0 percent) tumors. Staining was negative in human tumors from other sites. Rodent tumors and preneoplastic foci induced by chemical carcinogens were surveyed for staining with pNiXa-antibody. Staining was positive in 10/10 hepatic lesions (hepatocellular foci, adenomas, carcinomas) induced in hybrid D2B6F1 mice by diethylnitrosamine and phenobarbital, whereas murine mammary tumors and thyroid, pituitary, renal, and colon tumors of F-344/CNr rats were negative. Thus, immunostaining with pNiXa-antibody identifies a subset of human and murine tumors; further studies are needed to determine if reactivity of pNiXa-antibody has diagnostic or prognostic significance.

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Shiga Toxin 1 antibody, M Shiga Toxin 2 antibody, M Cholera toxin antibody, M Clostridium botulinum D T Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Diphtheria toxin antibody

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