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Platelets kill bacteria by bridging innate and adaptive immunity via PF4 and FcγRIIA.

Activated platelets release the chemokine platelet factor 4 (PF4) stored in their granules. PF4 binds to polyanions (P) on bacteria, undergoes a conformational change and exposes neoepitopes. These neoepitopes induce production of anti-PF4/P antibodies. As PF4 binds to a variety of bacteria, anti-PF4/P IgG can bind and opsonize several bacterial species.

2869 related Products with: Platelets kill bacteria by bridging innate and adaptive immunity via PF4 and FcγRIIA.

Androgen Receptor (Phosph Androgen Receptor (Phosph Rabbit Anti-Human Androge Rabbit Anti-Human Androge Androgen Receptor (Ab 650 AZD-3514 Mechanisms: Andr 17β-Acetoxy-2α-bromo-5 (5α,16β)-N-Acetyl-16-[2 (5α,16β)-N-Acetyl-16-ac 5α-N-Acetyl-2'H-androst- 5α-N-Acetyl-2'H-androst- 3-O-Acetyl 5,14-Androstad

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Monoclonal antibody-based colloid gold immunochromatographic strip for the rapid detection of Tomato zonate spot tospovirus.

Tomato zonate spot virus (TZSV), a new species of genus Tospovirus, caused significant losses in yield and problems in quality of many important vegetables and ornamentals in Southwest China and posed a serious threat to important economic crops for the local farmers. A convenient and reliable method was urgently needed for rapid detection and surveillance of TZSV.

2629 related Products with: Monoclonal antibody-based colloid gold immunochromatographic strip for the rapid detection of Tomato zonate spot tospovirus.

MOUSE ANTI BOVINE ROTAVIR MOUSE ANTI BORRELIA BURGD Mouse Anti-Beta-2-MG(B2E5 Mouse Anti-BrdU(A7) Monoc FDA Standard Frozen Tissu FDA Standard Frozen Tissu MarkerGeneTM Fluorescent MOUSE ANTI CANINE DISTEMP MOUSE ANTI HUMAN CD15, Pr MOUSE ANTI HUMAN CD19 RPE MOUSE ANTI HUMAN CD15, Pr MOUSE ANTI APAAP COMPLEX,

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Molecular cloning and characterization of leucine aminopeptidase gene from Taenia pisiformis.

Leucine aminopeptidase (LAP, EC: 3.4.11.1) is an important metalloexopeptidase that catalyze the hydrolysis of amino-terminal leucine residues from polypeptides and proteins. In this study, a full length of cDNA encoding leucine aminopeptidase of Taenia pisiformis (TpLAP) was cloned by rapid amplification of cDNA-ends using the polymerase chain reaction (RACE-PCR) method. The full-length cDNA of the TpLAP gene is 1823 bp and contains a 1569 bp ORF encoding 533 amino acids with a putative mass of 56.4 kDa. TpLAP contains two characteristic motifs of the M17LAP family in the C-terminal sequence: the metal binding site 265-[VGKG]-271 and the catalytic domain motif 351-[NTDAEGRL]-357. The soluble GST-TpLAP protein was expressed in Escherichia coli Transetta (DE3) and four specific anti-TpLAP monoclonal antibodies (mAbs) were prepared. In enzymatic assays, the optimal activity was observed at pH 9.5 at 45 °C. GST-TpLAP displayed a hydrolyzing activity for the Leu-pNA substrate with a maximum activity of 46 U/ml. The enzymatic activity was significantly enhanced by Mn2+ and completely inhibited by 20 nM bestatin and 0.15 mM EDTA. The native TpLAP was detected specifically in ES components of adult T. pisiformis by western blotting using anti-TpLAP mAb as a probe. Quantitative real-time PCR revealed that the TpLAP gene was expressed at a high level in adult worm tissues, especially in the gravid proglottids (50.71-fold). Immunolocalization analysis showed that TpLAP was located primarily in the subtegumental parenchyma zone and the uterine wall of adult worms. Our results indicate that TpLAP is a new member of the M17LAP family and can be considered as a stage-differentially expressed protein. These findings might provide new insights into the study of the mechanisms of growth, development and survival of T. pisiformis in the final host and have potential value as an attractive target for drug therapy or vaccine intervention.

1725 related Products with: Molecular cloning and characterization of leucine aminopeptidase gene from Taenia pisiformis.

F box and leucine rich re pYLEX1 - Expression Vect MIC2 Gene Protein, CD99; MIC2 Gene Protein, CD99; Cytokeratin, High Molecu Cytokeratin, High Molecu Cytokeratin, High Molecu Cytokeratin, High Molecu MIC2 Gene Protein, CD99; Cytokeratin, High Molecu Cytokeratin, High Molecu T4 SSB (gene 32) protein

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Linear epitopes in African swine fever virus p72 recognized by monoclonal antibodies prepared against baculovirus-expressed antigen.

Protein p72 is the major capsid protein of African swine fever virus (ASFV) and is an important target for test and vaccine development. Monoclonal antibodies (mAbs) were prepared against a recombinant antigenic fragment, from amino acid (aa) 20-303, expressed in baculovirus. A total of 29 mAbs were recovered and tested by immunofluorescent antibody (IFA) staining on ASFV Lisbon-infected Vero cells. Six antibodies were IFA-positive and selected for further characterization. Epitope mapping was performed against overlapping polypeptides expressed in E. coli and oligopeptides. Based on oligopeptide recognition, the mAbs were divided into 4 groups: mAb 85 (aa 165-171); mAbs 65-3 and 6H9-1 (aa 265-280); mAbs 8F7-3 and 23 (aa 280-294); and mAb 4A4 (aa 290-303). All mAbs were located within a highly conserved region in p72. This panel of antibodies provides the opportunity to develop new assays for the detection of ASFV antibody and antigen.

1505 related Products with: Linear epitopes in African swine fever virus p72 recognized by monoclonal antibodies prepared against baculovirus-expressed antigen.

Viral antibodies, anti-R HIV1 integrase antibody, Measles Virus Nucleoprote Measles Virus nucleoprote Hepatitis C Virus antibod Feline Leukemia virus ant Feline Leukemia Virus p27 Feline Leukemia Virus gp7 Feline Leukemia Virus gp7 Hepatitis B Virus antibod Hepatitis B Virus antibod Hepatitis C Virus antibod

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Preparation of a Monoclonal Antibody Against gD Protein of Bovine Herpesvirus I.

The two DNA fragments encoding predicted main antigenic regions, aa 20-160 and aa 257-344 on gD protein of bovine herpesvirus-1 (BoHV-1) were tandem-cloned into the vector pET28a. The recombinant His-tagged Δ gD1-Δ gD2 was expressed in Escherichia coli BL21(DE3)pLysS by induction with 0.5 mM isopropyl-1-thio-β-D-galactoside (IPTG) and Western blot analysis demonstrated that the recombinant His-tagged Δ gD1-Δ gD2 reacted with the positive serum against BoHV-1. A monoclonal antibody (MAb), designated as 2B6, was prepared by fusion of SP2/0 myeloma cells with splenocytes from a female 8-week-old BALB/c mouse immunized with purified His-tagged Δ gD1-Δ gD2 protein with the addition of Freund's adjuvant. The titer of the ascitic fluid triggered by hybridoma cells secreting MAb 2B6 was 1:2.5 × 108 and the subtype of MAb 2B6 was IgG 2a/κ. MAb 2B6 positively recognized with BoHV-1 infected Madin-Darby bovine kidney cells by an indirect fluorescent antibody assay. Moreover, MAb 2B6 showed 1:160 viral neutralizing activity using 60% plaque reduction assay. Therefore, this work suggested that MAb 2B6 has potential in the diagnosis of bovine respiratory disease complex associated with BoHV-1 and function analysis.

2544 related Products with: Preparation of a Monoclonal Antibody Against gD Protein of Bovine Herpesvirus I.

Anti C Reactive Protein A MOUSE ANTI BOVINE ROTAVIR HSV1 gD antibody, Monoclo HSV2 gD antibody, Monoclo HSV2 gD antibody, Monoclo HSV2 gD antibody, Monoclo HSV2 gD antibody, Monoclo Anti CEL Monoclonal Antib Anti AGE 3 Monoclonal Ant anti GFP antibody, rat mo Proteinase 3 Antibody Mou Rabbit Anti-F1 protein (Y

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Development of Competitive Enzyme-Linked Immunosorbent Assays for Antibody Detection Based on Bluetongue Virus Monoclonal Antibodies.

Bluetongue is a ruminant infectious disease that is characterized by hyperpyrexia, leukocyte decrease and mucosal ulcerative inflammation changes. In this study, three segments of Bluetongue virus (BTV)-8 VP2 protein (BTV-8A, 8B, and 8C) were cloned into pET-28a (+) and pMAl-c5X vectors and expressed in Escherichia coli BL21 (DE3) as histidine (His)-tagged (His-8A/8B/8C) and maltose-binding protein (MBP)-tagged (MBP-8A/8B/8C) fusion proteins. After purification, His-8A/8B/8C were used to immunize BALB/mice and MBP-8A/8B/8C were used to screen for monoclonal antibody (mAb)-secreting hybridomas. Two mAbs (8B-5D4 and 8B-3G11) that could recognize BTV-8 were obtained. Two competitive enzyme-linked immunosorbent assays with good specificity and sensitivity using mAbs 8B-5D4 or 8B-3G11 as competitive antibody were established. With the joint reaction of these methods, serum samples containing anti-BTV-7 or anti-BTV-8 antibody could be screened out, suggesting that these methods would be useful for the diagnosis and epidemiological studies of BTV-8.

1359 related Products with: Development of Competitive Enzyme-Linked Immunosorbent Assays for Antibody Detection Based on Bluetongue Virus Monoclonal Antibodies.

Measles Virus Nucleoprote Measles Virus nucleoprote Hepatitis C Virus antibod Feline Leukemia virus ant Feline Leukemia Virus p27 Feline Leukemia Virus gp7 Feline Leukemia Virus gp7 Hepatitis B Virus antibod Hepatitis B Virus antibod Hepatitis C Virus antibod Hepatitis C Virus antibod Hepatitis C Virus antibod

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An ELISA method to estimate the mono ADP-ribosyltransferase activities: e.g in pertussis toxin and vaccines.

ADP-ribosyltransferase activities have been observed in many prokaryotic and eukaryotic species and viruses and are involved in many cellular processes, including cell signalling, DNA repair, gene regulation and apoptosis. In a number of bacterial toxins, mono ADP-ribosyltransferase is the main cause of host cell cytotoxicity. Several approaches have been used to analyse this biological system from measuring its enzyme products to its functions. By using a mono ADP-ribose binding protein we have now developed an ELISA method to estimate native pertussis toxin mono ADP-ribosyltransferase activity and its residual activities in pertussis vaccines as an example. This new approach is easy to perform and adaptable in most laboratories. In theory, this assay system is also very versatile and could measure the enzyme activity in other bacteria such as Cholera, Clostridium, E. coli, Diphtheria, Pertussis, Pseudomonas, Salmonella and Staphylococcus by just switching to their respective peptide substrates. Furthermore, this mono ADP-ribose binding protein could also be used for staining mono ADP-ribosyl products resolved on gels or membranes.

2526 related Products with: An ELISA method to estimate the mono ADP-ribosyltransferase activities: e.g in pertussis toxin and vaccines.

Toxoplasma gondii GRA8, r Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon anti HSV (II) gB IgG1 (mo anti HCMV gB IgG1 (monocl Shiga Toxin 1 antibody, M Shiga Toxin 2 antibody, M Cholera toxin antibody, M Clostridum difficile toxi Clostridum difficile toxi

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Development of CDV-specific monoclonal antibodies for differentiation of variable epitopes of nucleocapsid protein.

The highly contagious canine distemper viruses (CDVs) are still a major threat to a wide range of natural susceptible hosts. The nucleocapsid (N) protein plays various roles in the virus-induced immune response. But precise mapping of epitopes and antigenic variations in N protein of CDV are still scant. In this study, two monoclonal antibodies (MAbs), designated as F8N and G3N, against the N protein of CDV were generated and characterized. The epitopes recognized by the two MAbs were mapped by truncated N protein fragments expressed in E.coli based on western blotting. The 470ESRYDTQ476 and 385GITKEEAQL393 were identified as the minimal linear epitopes recognized by F8N and G3N, respectively. The amino acid residues of the epitope (385-393aa) were highly conserved in a variety of CDV strains from the databases as well as five CDV strains in this study, indicating that MAb G3N can detect various CDV strains. However, MAb F8N was found not to react with an older CDV 851 strain of the five CDV strains due to both of two amino substitution (S471P and Y473H) in the epitope, whereas either single mutant S471P or Y473H did not eliminate the binding of F8N. Further, the variable epitopes existed in the N protein of six CDV strains resembling CDV3 in phylogenic tree by alignment with sequences from the databases. This is the first record of a precise epitope affecting antigenity of N protein of CDV. These results may facilitate future investigations into the function of NP of CDV and diagnostic methods for CDV infection.

1478 related Products with: Development of CDV-specific monoclonal antibodies for differentiation of variable epitopes of nucleocapsid protein.

Rat monoclonal anti mouse MOUSE ANTI BOVINE ROTAVIR Rabbit Anti-SARS Virus Nu MOUSE ANTI BORRELIA BURGD NATIVE HUMAN PROLACTIN, P Mouse Anti-SARS Nucleocap Anti-SARS Nucleocapsid Pr Goat Anti- T-cell differe Mouse monoclonal anti-fla Ofloxacin CAS Number [824 Rat monoclonal anti mouse Rat monoclonal anti mouse

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Ecobody technology: rapid monoclonal antibody screening method from single B cells using cell-free protein synthesis for antigen-binding fragment formation.

We report a rapid and cost-effective monoclonal antibody screening method from single animal B cells using reverse transcription (RT)-PCR and Escherichia coli cell-free protein synthesis (CFPS), which allows evaluation of antibodies within 2 working days. This process is named "Ecobody technology". The method includes strategies to isolate B cells that specifically bind an antigen from the peripheral blood of immunised animals, and single-cell RT-PCR to generate DNA fragments of the VH and VL genes, followed by CFPS for production of fragments of antigen binding (Fab). In the CFPS step, we employed our techniques: 1) 'Zipbody' as a method for producing Fab, in which the association of heavy and light chains is facilitated by adhesive leucine zipper peptides fused at the C-termini of the Fab; and 2) an N-terminal SKIK peptide tag that can increase protein expression levels. Using Ecobody technology, we obtained highly-specific monoclonal antibodies for the antigens Vibrio parahaemolyticus and E. coli O26. The anti-V. parahaemolyticus Zipbody mAb was further produced in E. coli strain SHuffle T7 Express in inclusion bodies and refolded by a conventional method, resulting in significant antigen-binding activity (K D = 469 pM) and productivity of 8.5 mg purified antibody/L-culture.

2453 related Products with: Ecobody technology: rapid monoclonal antibody screening method from single B cells using cell-free protein synthesis for antigen-binding fragment formation.

Anti C Reactive Protein A MOUSE ANTI BORRELIA BURGD Anti-actin binding protei MOUSE ANTI BOVINE ROTAVIR E. coli SSB (Single Stran E. coli SSB (Single Stran E. coli SSB (Single Stran E. coli SSB (Single Stran Taq SSB (Single Stranded Taq SSB (Single Stranded ribosome binding protein ribosome binding protein

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Development of Monoclonal Antibodies Recognizing Linear Epitope: Illustration by Three Bacillus thuringiensis Crystal Proteins of Genetically Modified Cotton, Maize, and Tobacco.

Bacillus thuringiensis Cry1Ac, Cry1Ia1, and Cry1Ie are δ-endotoxin insecticidal proteins widely implemented in genetically modified organisms (GMO), such as cotton, maize, and potato. Western blot assay integrates electrophoresis separation power and antibody high specificity for monitoring specific exogenous proteins expressed in GMO. Procedures for evoking monoclonal antibody (mAb) for Western blot were poorly documented. In the present study, Cry1Ac partially denatured at 100 °C for 5 min was used as an immunogen to develop mAbs selectively recognizing a linear epitope of Cry1Ac for Western blot. mAb 5E9C6 and 3E6E2 selected with sandwich ELISA strongly recognized the heat semidenatured Cry1Ac. Particularly, 3E6E2 recognized both E. coli and cotton seed expressed Cry1Ac in Western blot. Such strategy of using partially denatured proteins as immunogens and using sandwich ELISA for mAb screening was also successfully demonstrated with production of mAbs against Cry1Ie for Western blot assay in maize.

2099 related Products with: Development of Monoclonal Antibodies Recognizing Linear Epitope: Illustration by Three Bacillus thuringiensis Crystal Proteins of Genetically Modified Cotton, Maize, and Tobacco.

Bacillus anthracis (Anthr Bacillus anthracis (Anthr Bacillus anthracis (Anthr Bacillus anthracis (Anthr Bacillus anthracis (Anthr Viral antibodies: anti-H Monoclonal Antibodies to Proteins and Antibodies H Proteins and Antibodies H Proteins and Antibodies H Proteins and Antibodies H Alpha B Crystallin Monocl

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