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           Search results for: Rabbit Anti-JIP1_MAPK8IP1 Polyclonal Antibody   

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Immunohistochemical expression of polo-like kinase 1 in oral squamous cell carcinoma and oral submucous fibrosis.

Polo-like kinase 1 (PLK1) is a critical molecule in the proliferation of several human cancers. Overexpression of PLK1 has been correlated with cancer cell proliferation and lower overall survival rates. Although PLK1 has been studied in various tumors, information regarding its expression in oral cancer and precancer is limited. Aims: This study is aimed at evaluating the expression of PLK1 in a potentially malignant and malignant disorder of the oral cavity, namely, oral submucous fibrosis (OSMF) and oral squamous cell carcinoma (OSCC), respectively, using the immunohistochemistry technique. It also intended to evaluate the association of the various histological grades of OSCC with the intensity of PLK1 expression.

1699 related Products with: Immunohistochemical expression of polo-like kinase 1 in oral squamous cell carcinoma and oral submucous fibrosis.

Oral cavity squamous cell Lung squamous cell carcin Cervix squamous cell carc Esophagus squamous cell c Esophagus squamous cell c Esophageal squamous cell Oral squamous cell cancer Esophagus squamous cell c Esophagus squamous cell c Kidney clear cell carcino Kidney clear cell carcino Esophagus squamous cell c

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Development of a serum neutralization assay to detect Pteropine Orthoreovirus Indonesia/2010 neutralizing antibodies.

Pteropine Orthoreoviruses (PRVs) are fusogenic bat-borne orthoreoviruses that cause flu-like upper respiratory tract infections in humans. The presence of this group of viruses in bats and humans has been well documented in areas where their biological reservoirs - fruit bats (family Pteropodidae) - live densely. In the present study, a serum neutralization (SN) assay to detect neutralizing antibodies against PRV Indonesia/2010 isolate was set up and used to assess the seroprevalence of this virus in Italian domestic animals. The new developed assay was able of detecting PRV neutralizing antibodies in the hyper-immune polyclonal serum produced in rabbits (titer of 1:160). The negative serum was negative at all tested dilutions. No cross-reactions have been evidenced neither against reference MRVs nor against their respective hyper-immune sera. Eight hundred and fifty-three serum samples collected from 524 bovines, 271 small ruminants, and 58 horses (all used as sentinel animals in the Bluetongue and West Nile disease National surveillance program) were also tested with the new developed SN assay. According to the results of this survey, neither PRV nor PRV cross- reacting viruses antibodies have been demonstrated in Italian domestic animals. However, the new developed SN assay could be a very valuable diagnostic tool to detect infection in animals and humans.

1088 related Products with: Development of a serum neutralization assay to detect Pteropine Orthoreovirus Indonesia/2010 neutralizing antibodies.

 EpiQuik Total Histone H  EpiQuik Total Histone H  EpiQuik Total Histone H  EpiQuik Total Histone H Shiga Toxin 1 antibody, M Shiga Toxin 2 antibody, M Human Serum Albumin antib Human Serum Albumin antib Cholera toxin antibody, M Clostridium botulinum D T Clostridum difficile toxi Clostridum difficile toxi

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Distribution of mannose receptor in blunt snout bream (Megalobrama amblycephala) during the embryonic development and its immune response to the challenge of Aeromonas hydrophila.

The mannose receptor (MR) is a type I transmembrane protein. Its ectodomain has eight C-type lectin-like domains, which are able to recognize and mediate the phagocytosis of a wide range of pathogens. Comprehensive studies have revealed that mammalian MR is widely distributed in the mononuclear phagocyte system (MPS, previously known as the reticuloendothelial system) and play a key role both in the physiological clearance and cell activation. Hitherto, neither the MR distribution, nor the function of clearance and cell activation has been investigated in fish. In the previous study, we have reported the full-length cDNA of blunt snout bream MR, analyzed its structure and relative mRNA expression during embryogenesis and in the liver, head kidney, spleen and intestine of fish after stimulation with killed Aeromonas hydrophila. In the present study, we developed a rabbit polyclonal antibody against MR and undertook a systematic survey of the expression of MR at the protein level by immunohistochemistry. To get more information about MR function, the mRNA expression of MR, pro-inflammatory factor TNF-α and anti-inflammatory factor ARG2 genes was measured by qRT-PCR in the liver, head kidney, and spleen after A. hydrophila challenge. We first observed MR expression in the yolk sac at the fertilized egg stage and possibly MR was expressed by early macrophages. We also showed the MR distribution in head kidney, body kidney, spleen, liver, intestine, muscle, brain, heart, and gills. Following A. hydrophila challenge the MR immunoreactive cells became more widespread in head kidney and spleen, which are the major reticuloendothelial systems of fish. The quantitative studies at mRNA levels showed that there exists a high correlation between MR expression and immune cytokine expressions after bacteria challenge.

2289 related Products with: Distribution of mannose receptor in blunt snout bream (Megalobrama amblycephala) during the embryonic development and its immune response to the challenge of Aeromonas hydrophila.

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Immunodetection of the toxic portion of Vip3A reveals differential temporal regulation of its secretion among Bacillus thuringiensis strains.

Devise a protocol for heterologous expression and purification of a partial toxic portion of the Bacillus thuringiensis (Bt) vegetative insecticidal protein Vip3A, using it as antigen for anti-Vip3A polyclonal antibody development. Evaluate the regulation of Vip3A secretion into culture supernatants of different Bt strains based on this antibody.

2881 related Products with: Immunodetection of the toxic portion of Vip3A reveals differential temporal regulation of its secretion among Bacillus thuringiensis strains.

Ofloxacin CAS Number [824 Epidermal Growth Factor ( Epidermal Growth Factor ( BACTERIOLOGY BACTEROIDES BACILLUS CEREUS Z091, tit DNA (cytosine 5) methyltr Bacillus anthracis (Anthr Bacillus anthracis (Anthr Bacillus anthracis (Anthr Bacillus anthracis (Anthr Bacillus anthracis (Anthr REASTAIN® Quick Diff Kit

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Temporospatial study of hexose transporters and mucin in the epithelial cells of chicken (Gallus gallus domesticus) small intestine.

The temporospatial patterns in the localization of hexose transporters as well as in the quantitative and qualitative differences of glycoprotein mucin produced by the goblet cells of broiler chicken (Gallus gallus domesticus) small intestine during their first postnatal month were studied. The integral membrane proteins glucose transporter-2 and -5 (GLUT-2 and GLUT-5) that facilitate the transport of hexoses across epithelial cell layers that separate distinct compartments in organism were detected in the chicken intestinal epithelial cells using immunohistochemical labeling with polyclonal primary antibodies Rabbit anti-GLUT-2 and Rabbit anti-GLUT-5 (IHC kit, Abcam, UK). The chemical composition of mucin (neutral, acid) was carried out by applying the histochemical reactions by Alcian-Blue and periodic acid-Schiff methods. The results revealed presence of the hexose transporters GLUT-2 and -5, immunolocalized in the enterocytes of broiler's small intestine and the temporospatial pattern of the density of goblet cells of intestinal mucosa as well as the chemical composition of mucin produced by the goblet cells in chicken immediately after hatching and in 30-days-old chicken's. Simultanously, when goblet cells remained unstained with both antibodies in intestinal epithelium in chicken of both ages or some moderate staining was noticed in 30-days-old chickens' ileal epithelium, the increase of neutral and acid mucin- containing cells per area unit in both segments of the small intestine was detected from the first day after hatching to 30 day of life and the densilty of goblet cells was found to be higher in ileal than in duodenal region.

1409 related Products with: Temporospatial study of hexose transporters and mucin in the epithelial cells of chicken (Gallus gallus domesticus) small intestine.

Human Small Intestine Mic Alkaline Phospatase (ALP) Human Large Intestine Mic ELISA kit Calcyclin,Chick GI cancer (esophageal, ga Multiple organ stromal tu Small intestine cancer, m Small intestine disease ( Small intestine adenocarc Small intestine adenocarc Small intestine carcinoma Small intestine disease s

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Immunohistochemical Expression of FXR1 in Canine Normal Tissues and Melanomas.

Fragile X mental retardation-related protein 1 (FXR1) is a cytoplasmic RNA-binding protein highly conserved among vertebrates. It has been studied for its role in muscle development, inflammation, and tumorigenesis, being related, for example, to metastasizing behavior in human and canine uveal melanoma. Anti-FXR1 antibodies have never been validated in the canine species. To investigate FXR1 expression in canine melanocytic tumors, the present study tested two commercially available polyclonal anti-human FXR1 antibodies, raised in goat and rabbit, respectively. The cross-reactivity of the anti-FXR1 antibodies was assessed by Western blot analysis, and the protein was localized by IHC in a set of normal canine tissues and in canine melanocytic tumors (10 uveal and 10 oral). Western blot results demonstrated that the antibody raised in rabbit specifically recognized the canine FXR1, while the antibody raised in goat did not cross-react with this canine protein. FXR1 protein was immunodetected using rabbit anti-FXR1 antibody, in canine normal tissues with different levels of intensity and distribution. It was also detected in 10/10 uveal and 9/10 oral melanocytic tumors. The present study validated for the first time the use of anti-FXR1 antibody in dogs and highlighted different FXR1 protein expression in canine melanocytic tumors, the significance of which is undergoing further investigations.

1993 related Products with: Immunohistochemical Expression of FXR1 in Canine Normal Tissues and Melanomas.

High density breast invas Breast cancer tissue arra Multiple breast cancer ti Colon cancer tissue array High density cervix cance High density cervical can Esophageal cancer tissue Esophageal cancer tissue Mouse Anti-Human Fibronec High density kidney cance Kidney cancer tissue arra High density Lung cancer

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Electrophoretic Detection and Confocal Microscopic Imaging of Tyrosine Nitrated Proteins in Plant Tissue.

Tyrosine nitrated proteins can be detected in plant cells electrophoretically and their distribution can be monitored by confocal laser scanning microscopy (CLSM) imaging. One-dimensional polyacrylamide gel electrophoresis (1D PAGE) followed by Western blotting using polyclonal antibody against 3-nitrotyrosine residues enables detection of tyrosine nitrated proteins in plant cells. Here we describe detection of tyrosine nitrated proteins in the homogenates derived from sunflower (Helianthus annuus L.) seedling cotyledons. Total soluble proteins obtained from tissue homogenates are resolved using vertical gel electrophoresis followed by their electrophoretic transfer on to a microporous membrane support for immunodetection. Spatial distribution of tyrosine nitrated proteins can be visualized using an antibody against 3-nitrotyrosine residues. Immunofluorescent localization is performed by cutting 7 μm thick wax sections of tissue followed by incubation in primary anti-nitrotyrosine antibody (dilution 1:200) and secondary Cy-3 labeled anti-rabbit IgG antibody (dilution 1:1500). Confocal laser scanning microscopy analysis is undertaken using argon lasers (ex: 530-550 nm and em: 570 nm) at pinhole 1. Modulation in the abundance and spatial localization of tyrosine nitrated proteins in plant tissues can be monitored using these techniques.

1245 related Products with: Electrophoretic Detection and Confocal Microscopic Imaging of Tyrosine Nitrated Proteins in Plant Tissue.

Incu Tissue(square vessel Incu Tissue(square vessel Incu Tissue(square vessel MarkerGeneTM in vivo lacZ Native Influenza HA (A Br Native Influenza HA (A Br Native Influenza HA (A Br Native Influenza HA (A Ca Native Influenza HA (A Ca Native Influenza HA (A Ca Recombinant Influenza HA Recombinant Influenza HA

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Development of Polyclonal Antibody against Clenbuterol for Immunoassay Application.

Development of an immunoassay for clenbuterol (CLB) detection required an anti-CLB antibody as an important bioreceptor. In this study, we report our work on production and purification of a rabbit-derived polyclonal anti-CLB antibody. The antibody was then purified by nProtein A Sepharose affinity column and the antibody purity was confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis. The activities of purified antibody were evaluated based on high antibody titer determined from enzyme-linked immunosorbent assay (ELISA). The sensitivity and selectivity of this antibody was evaluated and exhibits negligible cross-reactivity to antibiotics other than β-agonist families. Evaluation of the antibody as bioreceptor in immunoassay was performed using direct competitive ELISA and exhibited linear calibration plot (R² = 0.9484). The antibody was used to detect the content of CLB in spiked milk samples and the recovery of more than 92% indicating significant performance as bioreceptor for the development of a rapid and simple immunoassay.

1812 related Products with: Development of Polyclonal Antibody against Clenbuterol for Immunoassay Application.

succinate-CoA ligase, GDP formin-like 1 antibody So succinate-CoA ligase, ADP RABBIT ANTI GSK3 BETA (pS Rabbit Anti-OPN Polyclona Rabbit Anti-OPN Polyclona Rabbit Anti-AD7c-NTP Poly Rabbit Anti-AACT-Alpha1 A Rabbit Anti-beta-Amyloid( Mouse Anti-beta-Amyloid(1 Rabbit Anti-Nogo R Polycl Rabbit Anti-Nogo R Polycl

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Development of Polyclonal Antibodies for Detection of Diosbulbin B-Derived cis-Enedial Protein Adducts.

Diosbulbin B (DSB), a major component of herbal medicine Dioscorea bulbifera L. (DB), can be metabolized to an electrophilic intermediate, DSB-derived cis-enedial (DDE). DDE was suggested to contribute to the hepatotoxicity observed in experimental animals and humans after their exposure to DSB. Our previous work found that DDE reacted with primary amino and/or sulfhydryl groups of hepatic protein. The objective of the study was to develop polyclonal antibodies that can recognize DDE-derived protein adducts. Immunogens synthesized from DDE and keyhole limpet hemocyanin were employed to raise polyclonal antibodies in rabbits. An enzyme-linked immunosorbent assay (ELISA) demonstrated high titers of antisera obtained from immunized rabbits. Immunoblot analysis showed that DDE-modified bovine serum albumin (BSA) was recognized by the obtained polyclonal antibodies in a concentration-dependent manner and without cross-reaction to native BSA. Competitive ELISA and competitive immunoblot analyses defined the specificity of the antibodies to recognize BSA modified by DDE. Immunoblot analysis also detected a multitude of chemiluminescent bands with a variety of molecular weights in liver homogenates that were harvested from mice treated with DSB. In summary, we have successfully raised polyclonal antibodies to detect protein adducts derived from DDE.

2493 related Products with: Development of Polyclonal Antibodies for Detection of Diosbulbin B-Derived cis-Enedial Protein Adducts.

S100 Protein antibody, Po Rat monoclonal anti mouse C Reactive Protein antibo Anti C-Reactive Protein A Anti VGLUT-1 Rat, polyclo Bone Morphogenetic Protei S6 Ribosomal Protein (Pho Mouse Anti-RSV 33kDa & 19 Rabbit Anti-SARS Virus Nu Alpha-soluble NSF attachm VDAC1 - Rabbit polyclonal S100 alpha - Rabbit polyc

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Polyclonal antibody production against rGPC3 and their application in diagnosis of hepatocellular carcinoma.

Glypican-3 (GPC3) is an integral membrane proteoglycan, which contains a core protein anchored to the cytoplasmic membrane through a glycosylphosphatidylinositol linkage. The glypican-3 can regulate the signaling pathways, thereby enhances cell division, growth, and apoptosis in certain cell types. It is almost nonexistent on the surface of the human normal cell membrane and highly expresses on the membrane of hepatocellular carcinoma (HCC) cells. It has been well established that GPC3 provides a useful diagnostic marker. For generating the polyclonal antibody of GPC3, we expected that GPC3 N-terminal region (amino acid sequence 26-358) could be expressed in Escherichia coli system, however, no active expression was observed after IPTG induction. Interestingly, after deletion of six proline residues from position 26 to 31 in the N-terminus, expression of recombinant GPC3 was clearly detected. We further analyzed the expressed protein deprived of six prolines, to immunize the New Zealand male rabbits for production of active antibodies. The binding affinity of antibody was analyzed by immunofluorescence analysis, immunohistochemical detection, and western blotting. The functional GPC3 N-terminal protein recombinant development, expression, purification, and the polyclonal antibody have been generated provide the basis for the diagnosis of HCC in cancer therapy.

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Rabbit Anti-intestinal FA Rabbit Anti-IAA (Indole-3 Rabbit Anti-IAA (Indole-3 Rabbit Anti-Integrin alph Rabbit Anti-APIP Apaf1 In Rabbit Anti-APIP Apaf1 In Rabbit Anti-TNIP2 ABIN2 T Rabbit Anti-TNIP2 ABIN2 T Rabbit Anti-TNIP2 ABIN2 T Rabbit Anti-Cell death in Rabbit Anti-Cell death in Integrin â3 (Phospho Tyr

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