Only in Titles

           Search results for: Polyclonal antibody Anti-IP3 Receptor-FITC   

paperclip

#29474159   // Save this To Up

Detecting Receptor Tyrosine Kinase ROR1 Using a Developed Anti-ROR1 Polyclonal Antibody.

Receptor tyrosine kinase ROR1 has been introduced as an interesting prognostic cancer marker in histopathology. The aim of this study was to produce a polyclonal antibody (PAb) against recombinant human ROR1 protein to be used as a tool for investigation of ROR1 expression in human cancer tissue blocks. The extracellular part of human ROR1 recombinant protein was expressed using pET-28b(+) plasmid in Escherichia coli Bl21(DE3) host. The recombinant ROR1, as a candidate immunogen, was purified and injected to a New Zealand rabbit. Followed by raising the titration of antibody, polyclonal anti-ROR1 antibody was purified through affinity chromatography column. After determining the purity of PAb anti-ROR1, its specific reactivity was assessed through various assessments. Flow cytometry analysis showed that PAb anti-ROR1 specifically recognizes ROR1 molecule in a number of positive and negative cell lines. Results obtained from detection of ROR1 in paraffin-embedded breast adenocarcinoma tissue blocks (n = 11) also demonstrated that PAb anti-ROR1 can effectively be used in immunohistochemistry. In conclusion, the developed anti-ROR1 PAb can be used as a tool for determining the prognostic value of ROR1 in histopathology of cancer tissues.

2602 related Products with: Detecting Receptor Tyrosine Kinase ROR1 Using a Developed Anti-ROR1 Polyclonal Antibody.

Anti RAGE (Receptor for A Anti RAGE (Receptor for A Anti RAGE (Receptor for A Rabbit Anti-Tyrosine Hydr Rabbit Anti-Tyrosine Hydr Rabbit Anti-Tyrosine Hydr Rabbit Anti-Tyrosine Hydr Rabbit Anti-Tyrosine Hydr Rabbit Anti-Tyrosine Hydr Rabbit Anti-Tyrosine Hydr Rabbit Anti-Tyrosine Hydr Rabbit Anti-Tyrosine Hydr

Related Pathways

paperclip

#29469422   // Save this To Up

[Cloning, fusion expression and identification of thioredoxin encoding gene from].

To clone and express the thioredoxin (Trx) from RH strain tachyzoites of, establish the prokaryotic expression vector and purify the recombinant protein, then produce the polyclonal anti-Trx antibody in rabbits.

2231 related Products with: [Cloning, fusion expression and identification of thioredoxin encoding gene from].

pYLEX1 - Expression Vect DNA (cytosine 5) methyltr Gene Expression: Mouse N Gene Expression: Rat P45 Lentiviral Technology pCD pCdgCAT Mammalian CAT Exp pCAMBIA0305.1 Vector, (Gu pCAMBIA0305.2 Vector (Sec pCAMBIA0380 Vector (No Re pCAMBIA1105.1 (GusPlus™ pCAMBIA1105.1R Vecotr (Gu pCAMBIA1200 Vector (No Re

Related Pathways

paperclip

#29469158   // Save this To Up

A novel potentiometric immunoassay for carcinoma antigen 15-3 by coupling enzymatic biocatalytic precipitation with a nanogold labelling strategy.

Methods based on potentiometric measurement have been developed for immunoassays, but most exhibit low sensitivities and are unsuitable for early diagnosis of disease. Herein we design a new potentiometric immunosensing platform for the sensitive detection of carcinoma antigen 15-3 (CA 15-3) by coupling with enzymatic biocatalytic precipitation and a nanogold labeling technique. The sandwich-type immunoreaction is carried out on a monoclonal anti-CA 15-3 capture antibody-modified working electrode, using horseradish peroxidase (HRP) and polyclonal anti-CA 15-3 detection antibody-labeled gold nanoparticles. Upon the introduction of target CA 15-3, the carried HRP molecules with an immunocomplex catalyze the oxidation of 4-chloro-1-naphthol (4-CN) into the insoluble benzo-4-chlorohexadienone. The formed product coated on the surface of the modified electrode results in a change of the electrical potential. Under optimal conditions, the shift in the electrical potential relative to the background signal increases with the increasing target CA 15-3 concentration, and exhibits a good linear relationship within the dynamic range of 0.01-30 U mLat a detection limit of 7.8 mU mL. Good precision and reproducibility, and high specificity were acquired for the analysis of 15 human serum specimens, giving well matched results with those obtained from a human CA 15-3 ELISA kit.

2148 related Products with: A novel potentiometric immunoassay for carcinoma antigen 15-3 by coupling enzymatic biocatalytic precipitation with a nanogold labelling strategy.

HIV 1 tat recombinant ant HIV 1 gag p24 recombinant HIV 1 env gp41 recombinan HIV 2 env gp36 recombinan HBV surface recombinant a HCV core 2 119aa recombin HCV NS5 2212 2313aa recom HAV VP3 recombinant antig HIV 2 env gp36 recombinan HSV 1 gD recombinant anti Recombinant Viral antige Recombinant Viral antige

Related Pathways

paperclip

#29466428   // Save this To Up

Hemagglutinin-specific neutralization of subacute sclerosing panencephalitis viruses.

Subacute sclerosing panencephalitis (SSPE) is a progressive, lethal complication of measles caused by particular mutants of measles virus (MeV) that persist in the brain despite high levels of neutralizing antibodies. We addressed the hypothesis that antigenic drift is involved in the pathogenetic mechanism of SSPE by analyzing antigenic alterations in the MeV envelope hemagglutinin protein (MeV-H) found in patients with SSPE in relation to major circulating MeV genotypes. To this aim, we obtained cDNA for the MeV-H gene from tissue taken at brain autopsy from 3 deceased persons with SSPE who had short (3-4 months, SMa79), average (3.5 years, SMa84), and long (18 years, SMa94) disease courses. Recombinant MeVs with a substituted MeV-H gene were generated by a reverse genetic system. Virus neutralization assays with a panel of anti-MeV-H murine monoclonal antibodies (mAbs) or vaccine-immunized mouse anti-MeV-H polyclonal sera were performed to determine the antigenic relatedness. Functional and receptor-binding analysis of the SSPE MeV-H showed activity in a SLAM/nectin-4-dependent manner. Similar to our panel of wild-type viruses, our SSPE viruses showed an altered antigenic profile. Genotypes A, G3, and F (SSPE case SMa79) were the exception, with an intact antigenic structure. Genotypes D7 and F (SSPE SMa79) showed enhanced neutralization by mAbs targeting antigenic site IIa. Genotypes H1 and the recently reported D4.2 were the most antigenically altered genotypes. Epitope mapping of neutralizing mAbs BH015 and BH130 reveal a new antigenic site on MeV-H, which we designated Φ for its intermediate position between previously defined antigenic sites Ia and Ib. We conclude that SSPE-causing viruses show similar antigenic properties to currently circulating MeV genotypes. The absence of a direct correlation between antigenic changes and predisposition of a certain genotype to cause SSPE does not lend support to the proposed antigenic drift as a pathogenetic mechanism in SSPE.

1970 related Products with: Hemagglutinin-specific neutralization of subacute sclerosing panencephalitis viruses.

Actin, Muscle Specific; Actin, Muscle Specific; PSA (Prostate Specific A PSA (Prostate Specific A PSAP (Prostate Specific PSAP (Prostate Specific PSA (Prostate Specific A PSA (Prostate Specific A Actin, Muscle Specific; PSA (Prostate Specific A PSAP (Prostate Specific PSA (Prostate Specific A

Related Pathways

paperclip

#29464573   // Save this To Up

Intrinsic Inflammation Is a Potential Anti-Epileptogenic Target in the Organotypic Hippocampal Slice Model.

Understanding the mechanisms of epileptogenesis is essential to develop novel drugs that could prevent or modify the disease. Neuroinflammation has been proposed as a promising target for therapeutic interventions to inhibit the epileptogenic process that evolves from traumatic brain injury. However, it remains unclear whether cytokine-related pathways, particularly TNFα signaling, have a critical role in the development of epilepsy. In this study, we investigated the role of innate inflammation in an in vitro model of post-traumatic epileptogenesis. We combined organotypic hippocampal slice cultures, representing an in vitro model of post-traumatic epilepsy, with multi-electrode array recordings to directly monitor the development of epileptiform activity and to examine the concomitant changes in cytokine release, cell death, and glial cell activation. We report that synchronized ictal- and interictal-like activities spontaneously evolve in this culture. Dynamic changes in the release of the pro-inflammatory cytokines IL-1β, TNFα, and IL-6 were observed throughout the culture period (3 to 21 days in vitro) with persistent activation of microglia and astrocytes. We found that neutralizing TNFα with a polyclonal antibody significantly reduced ictal discharges, and this effect lasted for 1 week after antibody washout. Neither phenytoin nor an anti-IL-6 polyclonal antibody was efficacious in inhibiting the development of epileptiform activity. Our data show a sustained effect of the anti-TNFα antibody on the ictal progression in organotypic hippocampal slice cultures supporting the critical role of inflammatory mediators in epilepsy and establishing a proof-of-principle evidence for the utility of this preparation to test the therapeutic effects of anti-inflammatory treatments.

1194 related Products with: Intrinsic Inflammation Is a Potential Anti-Epileptogenic Target in the Organotypic Hippocampal Slice Model.

Mouse Anti P. aeruginosa Mouse Anti P.aeruginosa s Mouse Anti P.aeruginosa s Mouse Anti Salmonella typ Mouse Anti Shigella boydi Mouse Anti-Insulin-Like G Mouse Anti-Lipoprotein Li MOUSE ANTI BOVINE ROTAVIR Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon

Related Pathways

paperclip

#29462680   // Save this To Up

Thermal unfolding of human lysozyme induces aggregation: Recognition of the aggregates by antisera against the native protein.

Protein aggregates are formed due to the inappropriate folding of polypeptides. Human lysozyme (HLZ) plays an important role in the innate immune response of the body and has been used extensively as a model protein to study aggregation. In this study, we showed that HLZ undergoes unfolding induced aggregation when heated. We further showed that the aggregates were recognized by polyclonal antibodies against the native HLZ. The consequences of these observations are further co-related with mammalian physiology.

2778 related Products with: Thermal unfolding of human lysozyme induces aggregation: Recognition of the aggregates by antisera against the native protein.

anti FAS IgG1 (monoclonal TCP-1 theta antibody Sour Recombinant Human PKC the Recombinant Human PKC the Recombinant Human PKC the ELISA TEK™ MBM Thermal NATIVE HUMAN PROLACTIN, P NATIVE HUMAN PROLACTIN-PU MyGenie 32 Thermal Block MyGenie 96 Gradient Therm MyGenie 96 Gradient Therm Thermal Shaker with cooli

Related Pathways

paperclip

#29462667   // Save this To Up

A Proximity Extension Assay (PEA)-based method for quantification of bevacizumab.

Proximity Extension Assay (PEA) is a direct one-step protein quantification method using a pair of DNA oligonucleotides linked to antibodies against the target molecule. It requires polyclonal or two monoclonal antibodies (mAbs) that bind to target epitopes close enough to form a DNA duplex which is quantified by real-time PCR. Bevacizumab, an anti-cancer drug, is a mAb against vascular endothelial growth factor with common cardiovascular adverse effects. It is widely used off-label to treat neovascular eye disorders by intravitreal application of small doses. Even then, certain amount reaches systemic circulation which is considered relevant regarding safety. We aimed to set-up a PEA-based assay for bevacizumab in human plasma and to preliminary evaluate it in patients treated intravitreally.

2988 related Products with: A Proximity Extension Assay (PEA)-based method for quantification of bevacizumab.

QuantiChrom™ LDH Cytoto QuantiChrom™ Formaldehy MarkerGeneTM Fluorescent Creatinine Assay Creatini Glucose Assay With the La Cultrex In Vitro Angiogen Endothelial Tube Formatio QuantiChrom™ Nitric Oxi QuantiChrom™ Acetylchol QuantiChrom™ α-Amylase QuantiChrom™ Formaldehy QuantiChrom™ BCP Albumi

Related Pathways

paperclip

#29460549   // Save this To Up

IgM and IgA enriched polyclonal immunoglobulins reduce short term mortality in extremely low birth weight infants (ELBW) with sepsis: a retrospective cohort study.

Immunoglobulin supplementation is a debated strategy in fighting sepsis. We evaluated a polyclonal IgM and IgA enriched immunoglobulin (IgMeIVIG) preparation in reducing the short term mortality in extremely low birth weight neonates (ELBW) with proven infection.

2260 related Products with: IgM and IgA enriched polyclonal immunoglobulins reduce short term mortality in extremely low birth weight infants (ELBW) with sepsis: a retrospective cohort study.

Interleukin-34 IL34 (N-t Mouse anti IgA1 antibody, Integrin â3 (Phospho Tyr Androgen Receptor (Phosph Androgen Receptor (Phosph Integrin â3 (Phospho Tyr Goat Anti-Human HMGB3 HMG Goat Anti-Human F2R PAR1, Goat Anti-Mouse APOBEC1, anti H inh human blood an Integrin â3 (Ab 773) Ant Androgen Receptor (Ab 650

Related Pathways

paperclip

#29459849   // Save this To Up

Widely Used Commercial ELISA Does Not Detect Precursor of Haptoglobin2, but Recognizes Properdin as a Potential Second Member of the Zonulin Family.

There is increasing evidence for the role of impaired intestinal permeability in obesity and associated metabolic diseases. Zonulin is an established serum marker for intestinal permeability and identical to pre-haptoglobin2. Here, we aimed to investigate the relationship between circulating zonulin and metabolic traits related to obesity.

1197 related Products with: Widely Used Commercial ELISA Does Not Detect Precursor of Haptoglobin2, but Recognizes Properdin as a Potential Second Member of the Zonulin Family.

G protein-coupled recepto amyloid beta precursor pr RAP2C, member of RAS onco Beta Amyloid (40) ELISA K Beta Amyloid (1 42) ELISA Anti Galectin(Gal 3) Huma ReadiUse™ ABTS Solution Amplite™ Fluorimetric G Amplite™ Fluorimetric G Human Amyloid Beta Precur Cell Meter™ JC 10 Mitoc Cell Meter™ JC 10 Mitoc

Related Pathways

paperclip

#29458660   // Save this To Up

Identification of antigenic proteins from Mycobacterium avium subspecies paratuberculosis cell envelope by comparative proteomic analysis.

Johne's disease (JD) is a contagious, chronic granulomatous enteritis of ruminants caused by Mycobacterium avium subsp. paratuberculosis (MAP). The aim of this study was to identify antigenic proteins from the MAP cell envelope (i.e. cell wall and cytoplasmic membranes) by comparing MAP, M. avium subsp. hominissuis (MAH) and M. smegmatis (MS) cell envelope protein profiles using a proteomic approach. Composite two-dimensional (2D) difference gel electrophoresis images revealed 13 spots present only in the image of the MAP cell envelope proteins. Using serum from MAP-infected cattle, immunoblot analysis of 2D gels revealed that proteins in the 13 spots were antigenic. These proteins were identified by liquid chromatography tandem mass spectrometry as products of the following genes: sdhA, fadE25_2, mkl, citA, gapdh, fadE3_2, moxR1, mmp, purC, mdh, atpG, fbpB and desA2 as well as two proteins without gene names identified as transcriptional regulator (MAP0035) protein and hypothetical protein (MAP1233). Protein functions ranged from energy generation, cell wall biosynthesis, protein maturation, bacterial replication and invasion of epithelial cells, functions considered essential to MAP virulence and intracellular survival. Five MAP cell envelope proteins, i.e. SdhA, FadE25_2, FadE3_2, MAP0035 and DesA2 were recombinantly expressed, three of which, i.e. SdhA, FadE25_2 and DesA2, were of sufficient purity and yield to generate polyclonal antibodies. Immunoblot analysis revealed antibodies reacted specifically to the respective MAP cell envelope proteins with minimal cross-reactivity with MAH and MS cell envelope proteins. Identification and characterization of MAP-specific proteins and antibodies to those proteins may be useful in developing new diagnostic tests for JD diagnosis.

2977 related Products with: Identification of antigenic proteins from Mycobacterium avium subspecies paratuberculosis cell envelope by comparative proteomic analysis.

Recombinant Dengue Virus Recombinant Dengue Virus Recombinant Dengue Virus Recombinant Dengue Virus Recombinant Dengue Virus Recombinant Dengue Virus Recombinant Dengue Virus Recombinant Dengue Virus Recombinant Dengue Virus Recombinant Dengue Virus Recombinant Dengue Virus Recombinant HBsAg adr [fr

Related Pathways

  •  
  • No related Items