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           Search results for: Rabbit Anti-GAPDH(3E12)-Loading Control Polyclonal Antibody, HRP Conjugated   

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#23539949   2013/03/29 Save this To Up

Induction of prominent Th1 response in C57Bl/6 mice immunized with an E. coli-expressed multi T-cell epitope EgA31 antigen against Echinococcus granulosus.

First step in developing an epitope-based vaccine is to predict peptide binding to the major histocompatibility complex (MHC) molecules. We performed computational analysis of unique available EgA31 sequence to locate appropriate antigenic propensity positions. T-cell epitopes with best binding affinity values of < 50% inhibitory concentration were selected using different available servers (Propred and IEDB). Peptides with 100% population coverage were selected. A DNA fragment corresponding to the furin linker enriched in Golgi apparatus was inserted sequentially between each epitope sequences in a synthetic DNA in order to cleave the chimeric protein into four separated peptides. Subsequently, the synthetic DNA was cloned into the pGEX4T-1 and pEGFP-N1 vectors and GST-ChEgA31 was expressed in E. coli strain BL21-DE3. The recombinant protein was detected by western blotting using an HRP-conjugated polyclonal anti-GST antibody. Fusion protein purified by affinity chromatography was used to raise antisera in rabbits. Results in agar gel immunodiffusion assay indicated induction of specific antibodies against multiepitope antigen in the tested rabbits. Cytokine assay was carried out in C57Bl/6 mice and the levels of cytokines were analyzed by sandwich ELISA. Interestingly, production of specific IFN-gamma was prominently higher in mice immunized with GST-ChEgA31 and pEGFP-ChEgA31 (650-1300 pg/ml) compared to control groups. No difference was observed in the level of IL-10 and IL-4 in immunized and GST control group. Challenge study with 500 live protoscolices of Echinococcus granulosus on immunized mice demonstrated protectivity level (50-60%). Based on our results, it appeared that the chimeric protein in the study was able to stimulate T-helper cell-1 (Th1) development and high level of cell mediated immunity in mice.

2416 related Products with: Induction of prominent Th1 response in C57Bl/6 mice immunized with an E. coli-expressed multi T-cell epitope EgA31 antigen against Echinococcus granulosus.

Cell cycle antibody array Rabbit Anti-Cell death in Dog Receptor-binding canc Mouse Anti P.aeruginosa s Oral squamous cell cancer Ki-67 Antigen Ki-67 Antigen Ki-67 Antigen HBV surface recombinant a HEV (Birma) ORF2 recombin HCV core 2 119aa recombin HCV NS3 1192 1456aa recom

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#22304298   2012/02/06 Save this To Up

Development of ELISA for the detection of transgenic vegetative insecticidal protein in GM crops/produce.

In the process of the development of insect-resistant genetically modified (GM) crops and also to evaluate the consistency in the expression of toxin under field conditions, immunological assays are commonly being used. An immunoassay was developed to support the labelling of vegetative insecticidal protein (Vip3A)-based GM produce. The developed ELISA for the measurement of Vip3A is a triple antibody sandwich procedure utilising a polyclonal capture antibody (mouse anti-Vip3A) and a polyclonal detection antibody (rabbit anti-Vip3A) followed by use of a third HRP-conjugated anti-species antibody (goat anti-rabbit IgG). The limit of detection limit of the ELISA assay was 16 ng ml(-1) with a linear quantification range from approximately 31 to 500 ng ml(-1) of Vip3A protein. Furthermore, the assay was in-house validated with GM brinjal samples. The assay was specific, sensitive and reproducible, which can be helpful to detect and track down the spread of unapproved and intentionally/unintentionally released GM produce harbouring Vip protein.

1857 related Products with: Development of ELISA for the detection of transgenic vegetative insecticidal protein in GM crops/produce.

Rabbit Anti-TNIP2 ABIN2 T Rat intestinal fatty acid Chicken craniofacial deve Bovine prolactin-induced Rat Inactive rhomboid pro Casein ELISA Kit Milk ca Protein Phosphatase 1 sub Protein Phosphatase 1 sub Protein Phosphatase 1 sub Protein Phosphatase 1 sub Protein Phosphatase 1 sub Protein Phosphatase 1 sub

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#22808420   2012/07/18 Save this To Up

Production and Purification of Anti-Rhombomys opimus Immunoglobulins.

Zoonotic cutaneous leishmaniasis (ZCL) is an increasing public health problem in some endemic regions. Horseradish peroxidase (HRP) conjugated rabbit anti-Rhombomys opimus (R. opimus) Ig is needed for immunoblotting and ELISA tests used to explore the immune response of the rodents against the sand fly saliva. In this study, the production of HRP conjugated rabbit anti-R. opimus Ig was conducted for the first time.

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Rabbit Anti-Human Androge Rabbit Anti-Human Androge Protein Purification Bea Protein Purification Bea Protein Purification Bea Protein Purification Bea Protein Purification Bea Protein Purification Bea Protein Purification Bea Protein Purification Bea Protein Purification Bea Protein Purification Bea

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#15941537   2005/06/08 Save this To Up

[Development and application of triple antibodies-based sandwich ELISA for detecting nucleocapsid protein of SARS-associated coronavirus].

To prepare and characterize monoclonal antibodies (mAb) and polyclonal antibodies against nucleocapsid (N) protein of severe acute respiratory syndrome (SARS)-associated coronavirus (SARS-CoV) and to establish antibodies-based sandwich ELISA for detecting N protein of SARS-CoV, which might apply to early diagnosis of patients with SARS-CoV infection.

1272 related Products with: [Development and application of triple antibodies-based sandwich ELISA for detecting nucleocapsid protein of SARS-associated coronavirus].

Rabbit Anti-SARS Virus Nu Rabbit Anti-SARS-Associat Rabbit Anti-SARS-Associat Mouse Anti-SARS-Associate Mouse Anti-SARS-Associate Mouse Anti-SARS Nucleocap Anti-SARS Nucleocapsid Pr Recombinant Viral antige Recombinant Viral antige Rabbit Anti-SARS-Associat Rabbit Anti-SARS-Associat Rabbit Anti-SARS-Associat

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#14695487   2003/12/25 Save this To Up

[Binding between alpha 1A-adrenergic receptor and segment of bone morphogenetic protein-1 in human embryonic cell 293].

Using matchmaker yeast two-hybrid system, it has been demonstrated that there exists an interaction between the cellular C terminal of alpha(1A)-adrenergic receptor (alpha(1A)-AR) and a segment of bone morphogenetic protein-1 (BMP-1). In the present study binding between the two proteins was further determined in human embryonic cell 293 (HEK293), a mammalian expression system. Mammalian expression vector PCP3HA was constructed by PCR and consisted of segments of BMP-1 cDNA, and vector PDT-alpha(1A) consisted of the full-length cDNA of human alpha(1A)-AR. They were transfected to HEK293 cells and examined by Western blot. alpha(1A)-AR and the segment of BMP-1 could be detected in the lysis of transfected cells. Then binding between alpha(1A)-AR and the segment of BMP-1 in HEK293 cell was determined by enzyme-linked immunosorbent assays (ELISA) and co-immunoprecipitation. In ELISA experiment, the ELISA microwell plate was first coated with anti-FLAG M2 antibody, which recognizes the FLAG-tagged alpha(1A)-AR, then the cell lysis, anti-HA rabbit polyclonal antibody and HRP conjugated anti-rabbit antibody were added in turn. The OD(490) values among the control group, PDT-alpha(1A) transfection group and PCP3HA transfection group, exhibited no significant difference (0.034+/-0.027, 0.042+/-0.019, 0.030+/-0.0096), but the OD(490) values of PDT-alpha(1A) and PCP3HA co-transfection group (0.57+/-0.12) were significantly higher than those of the other groups (P<0.001, respectively). In co-immunoprecipitation experiments, HEK293 cells expressing alpha(1A)-AR or/and segment of BMP-1 were lysed and incubated with anti-FLAG M2 antibody, then the immunoprecipitation pellet was immunoblotted with either the HRP conjugated anti-FLAG antibody or the anti-HA antibody, which recognizes the HA-tagged segment of BMP-1. Segment of BMP-1 was present in the pellet immunoprecipitation of PDT-alpha(1A) and PCP3HA co-transfected group. In conclusion, the results indicate that alpha(1A)-AR and the segment of BMP-1 are present in the same complex in HEK293 cells.

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Alpha-1A adrenergic recep Bone Morphogenetic Protei Bone Morphogenetic Protei interferon-alpha receptor Rabbit Anti-Cell death in Rabbit Anti-Cell death in Goat Anti-Human Vitamin D Mouse anti human INF alph Rabbit Anti-Human B-cell ELISA Human , Interleukin Anti-BMPR1A(Bone morphoge Anti-BMPR1B(Bone morphoge

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#11094520   2001/02/15 Save this To Up

[Cytokine-induced nitric oxide production of joint cartilage cells in continuous passive movement. Anti-inflammatory effect of continuous passive movement on chondrocytes: in vitro study].

The temporomandibular joint is a place of motion where release of proinflammatory cytokines like interleukin-1 beta (IL-1 beta) induces cartilage destruction via production of nitric oxide (NO). The purpose of this study was to evaluate the effects of continuous passive motion in the form of cyclic stretch on the synthesis of inducible nitric oxide synthase (iNOS).

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Rabbit Anti-Nitric Oxide Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon anti HSV (II) gB IgG1 (mo anti HCMV IE pp65 IgG1 (m anti HCMV gB IgG1 (monocl Macrophage Colony Stimula Macrophage Colony Stimula Rabbit Anti-FGF3 Oncogene Rat inducible nitric oxid

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