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           Search results for: Rabbit Anti-VEGFR3(mouse, rat) 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.

1715 related Products with: Facile Preparation of Stable Antibody-Gold Conjugates and Application to Affinity-Capture Self-Interaction Nanoparticle Spectroscopy.

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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#25070131   2014/09/26 Save this To Up

Epitope mapping of epidermal growth factor receptor (EGFR) monoclonal antibody and induction of growth-inhibitory polyclonal antibodies by vaccination with EGFR mimotope.

One of the proposed approaches in cancer therapy is to induce and direct the patient's own immune system against cancer cells. In this study, we determined the epitope mapping of the rat anti-human epidermal growth factor receptor (EGFR) monoclonal antibody ICR-62 using a phage display of random peptide library and identified a 12 amino acids peptide, which was recognized as a mimotope. The peptide was synthesized and conjugated to bovine serum albumin (BSA) as carrier protein (P-BSA). We have shown that ICR-62 can react specifically with P-BSA as well as native EGFR. Two rabbits were immunized either by BSA or P-BSA and the rabbits IgGs were purified and examined for binding to the antigens, mimotope and the EGFR protein purified from the EGFR overexpressing A431 cell line. We showed that the rabbit IgG generated against the mimotope is capable of inhibiting the growth of A431 cells by 15%, but does not have any effect on the growth of EGFR-negative MDA-MB-453 cell line in vitro. Our results support the need for further investigations on the potential of vaccination with either mimotope of the EGFR or epitope displayed on the surface of phage particles for use in active immunotherapy of cancer.

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#21605610   2011/07/15 Save this To Up

Determination of a new antibacterial peptide S-thanatin in rat plasma by an indirected-ELISA.

In this study, antimicrobial peptide S-thanatin (Ts) was chemically synthesized and linked to keyhole limpet hemocyanin (KLH) and bovine serum albumin (BSA) by carbodiimide reagent. Rabbits were immunized with Ts-KLH and polyclonal antibody against Ts was purified by fractional precipitation of ammonium sulfate, coupled with anion-exchange chromatography. The purified antibody specifically binding to Ts residues but not BSA molecules was observed by Western-Blot analysis. Ts-BSA was selected as immobilized antigen and reacted with the residual antibody after the excess of anti-Ts antibody was combined with Ts in the sample. The binding antibody was recognized by HRP-conjugated secondary antibody. Finally, the horseradish peroxidase in the complex could catalyze the TMB substrate, resulting in color development. The method was evaluated by analysis of linearity, precision and accuracy and successfully applied in determination of Ts in rat plasma. The data of the pharmacokinetic parameters were also obtained. The proposed ELISA has a great value in routine analysis of Ts for its therapeutic monitoring and pharmacokinetic studies.

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GLP 1 ELISA Kit, Rat Gluc Glucagon ELISA KIT, Rat G Human interleukin 2(IL-2) 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 Goat Anti-Rat MARCH10, (i Goat Anti-Mouse, Rat DLL1 Goat Anti-Human, Mouse, R Goat Anti-Human, Mouse, R

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#19177194   2009/01/29 Save this To Up

Preparation and Characterization of a Polyclonal Antibody against Brominated Protein.

(Di)bromotyrosine is formed by the specific reaction of eosinophil peroxidase and can be used as an eosinophil activation marker. In the present study, an antibody for (di)bromotyrosine in proteins was prepared to investigate the pathogenesis of eosinophil-related diseases such as allergic responses. A rabbit polyclonal antibody was raised against brominated keyhole limpet hemocyanin. The specificity of the antiserum was investigated with an enzyme-linked immunosorbent assay (ELISA). The antiserum recognized brominated bovine serum albumin (BSA) and dibromotyrosine-conjugated BSA. The antiserum also reacted with chlorinated BSA and di-iodotyrosine-conjugated BSA. Moreover, the specificity of the antiserum was investigated using competitive ELISA. Dibromotyrosine and di-iodotyrosine inhibited the recognition of brominated BSA by the antiserum. However, the recognition of brominated BSA by the antiserum was not inhibited by bromotyrosine, chlorotyrosine, iodotyrosine, nitrotyrosine, aminotyrosine, phosphotyrosine, or tyrosine. These results suggested that the epitope of the antiserum is dihalogenated tyrosine. Immunohistochemically, the antiserum stained brominated rat eosinophils but not chlorinated or nitrated eosinophils. In conclusion, an antiserum for dihalogenated protein was prepared. It is expected that the antiserum will be useful for the analysis of the pathogenesis of allergic diseases such as asthma and atopic dermatitis.

2541 related Products with: Preparation and Characterization of a Polyclonal Antibody against Brominated Protein.

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#18612319   2008/09/24 Save this To Up

L-Arginine decreases fluid-percussion injury-induced neuronal nitrotyrosine immunoreactivity in rats.

Peroxynitrite is a powerful oxidant capable of nitrating phenolic moieties, such as tyrosine or tyrosine residues in proteins and increases after traumatic brain injury (TBI). First, we tested the hypothesis that TBI increases nitrotyrosine (NT) immunoreactivity in the brain by measuring the number of NT-immunoreactive neurons in the cerebral cortex and hippocampus of rats subjected to parasagittal fluid-percussion TBI. Second, we tested the hypothesis that treatment with L-arginine, a substrate for nitric oxide synthase, further increases NT immunoreactivity over TBI alone. Rats were anesthetized with isoflurane and subjected to TBI, sham TBI, or TBI followed by treatment with L-arginine (100 mg/kg). Twelve, 24, or 72 h after TBI, brains were harvested. Coronal sections (10 microm) were incubated overnight with rabbit polyclonal anti-NT antibody, rinsed, and incubated with a biotinylated secondary antibody. The antigen-antibody complex was visualized using a peroxidase-conjugated system with diaminobenzidine as the chromagen. The number of NT-positive cortical and hippocampal neurons increased significantly in both ipsilateral and contralateral hemispheres up to 72 h after TBI compared with the sham-injured group. Remarkably, treatment with L-arginine reduced the number of NT-positive neurons after TBI in both cortex and hippocampus. Our results indicate that L-arginine actually prevents TBI-induced increases in NT immunoreactivity.

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Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Human Epstein-Barr Virus Jurkat Cell Extract (Indu Jurkat Cell Extract (Indu Jurkat Cell Extract (Indu Jurkat Cell Extract (Indu Mouse Epstein-Barr Virus TGF beta induced factor 2 Bovine prolactin-induced

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#18551996   2008/06/16 Save this To Up

Production and application of a polyclonal peptide antiserum for universal detection of StAR protein.

We report production of a polyclonal antibody against the StAR (steroidogenic acute regulatory) protein of steroidogenic cells and immunohistochemistry (IHC) staining of bovine adrenal gland tissue available in paraffin block. The epitope-specific polyclonal antibody was produced in a rabbit immunized against a synthetic 26 amino acid peptide (82AMQRALGILKDQEGWKKESRANGDE107) derived from the coding sequences reported for the bovine StAR gene (Gene Bank Accession No. Q28918). Western blots were developed using the StAR-specific peptide antiserum with an alkaline-phosphatase-conjugated anti-rabbit IgG second antibody chromogenic system. The antiserum was found to be highly specific for StAR, which exhibited an estimated molecular weight of about 30 KDa for all species analyzed. Finally, the peptide antiserum was successfully employed to localize StAR protein by immunohistochemical staining of thin sections prepared from bovine adrenal gland tissue. This study is the first to report a polyclonal peptide antiserum that apparently recognizes native StAR protein, regardless of the species of origin. The successful production of the antibody has provided a useful tool for studying regulation of StAR protein.

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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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#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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#17660589   2007/07/30 Save this To Up

Immunocytochemical localization of S100A1 in mitochondria on cryosections of the rat heart.

Immunocytochemical localization studies of S100A1 in muscle cells have so far yielded variable and conflicting results mainly due to different sample preparation techniques for immunoelectron microscopy. To minimize denaturation by fixation and embedding, cryofixation and cryosectioning followed by immunolabelling were used in the present study. Rat hearts were gently prefixed in a mixture of paraformaldehyde and glutaraldehyde. Samples from left and right ventricles and left and right atria were cryoprotected by sucrose and shock-frozen in liquid nitrogen. Ultrathin cryosections were labelled with rabbit polyclonal antiserum against S100A1. The sections were then incubated with secondary antibody conjugated to FITC (for fluorescence microscopy) or with protein A conjugated to 5 nm gold particles (for electron microscopy). The most prominent sites immunolabelled for S100A1 were mitochondria. In the fluorescence microscope the labelling of mitochondria was intense, suppressing the labelling in other compartments. In accordance with previous studies labelling of sarcoplasmic reticulum, Z-lines, actin and myosin filaments could also be detected in the electron microscope.

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