DOCSLIB.ORG

GFP Antibody NB600-308

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
GFP Antibody NB600-308 Product Datasheet GFP Antibody NB600-308 Unit Size: 0.1 mg Store at -20C. Avoid freeze-thaw cycles. Reviews: 18 Publications: 201 Protocols, Publications, Related Products, Reviews, Research Tools and Images at: www.novusbio.com/NB600-308 Updated 7/13/2021 v.20.1 Earn rewards for product reviews and publications. Submit a publication at www.novusbio.com/publications Submit a review at www.novusbio.com/reviews/destination/NB600-308 Page 1 of 6 v.20.1 Updated 7/13/2021 NB600-308 GFP Antibody Product Information Unit Size 0.1 mg Concentration Please see the vial label for concentration. If unlisted please contact technical services. Storage Store at -20C. Avoid freeze-thaw cycles. Clonality Polyclonal Preservative 0.01% Sodium Azide Isotype IgG Purity Immunogen affinity purified Buffer 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 Target Molecular Weight 27 kDa Product Description Host Rabbit Species Non-species specific Reactivity Notes No reaction was observed against Human, Mouse serum proteins. Suitable for detecting fusion proteins containing the GFP sequence expressed in Human, Mouse, Rat, C. elegans, Drosophila and in vitro transcription/translation systems and transgenic animals. GFP Transgenic Rat reactivity reported in scientific literature (PMID:25724725). Mouse reactivity reported in multiple pieces of scientific literature.Transgenic C. elegans reactivity reported in scientific literature (PMID: 27110099). Known cross reactivity with wt and all variants such as rGFP, eGFP, S65T-GFP, RS-GFP, YFP and EGFP. Use in Mouse reported in secitific publication PMID: 32765228 Plant reactivity reported in scientific literature (PMID:32896843) Specificity/Sensitivity Anti-GFP antibody was prepared from monospecific antiserum by immunoaffinity chromatography using Green Fluorescent Protein (Aequorea victoria) coupled to agarose beads followed by solid phase adsorption(s) to remove any unwanted reactivities. Assay by immunoelectrophoresis resulted in a single precipitin arc against anti-Rabbit Serum and purified and partially purified Green Fluorescent Protein (Aequorea victoria). Primate reactivity reported in scientific literature (PMID: 27723741). Immunogen The immunogen is a Green Fluorescent Protein (GFP) fusion protein corresponding to the full length amino acid sequence (246aa) derived from the jellyfish Aequorea victoria. Notes This antibody was prepared from monospecific antiserum by immunoaffinity chromatography using Green Fluorescent Protein (Aequorea victoria) coupled to agarose beads followed by solid phase adsorption(s) to remove any unwanted reactivities. Assay by immunoelectrophoresis resulted in a single precipitin arc against anti-Rabbit Serum and purified and partially purified Green Fluorescent Protein (Aequorea victoria) Store this antibody at -20C prior to opening. Aliquot contents and freeze at -20C or below for extended storage. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. GFP antibody is stable for several weeks at 4C as an undiluted liquid. Dilute only prior to immediate use. Product Application Details Page 2 of 6 v.20.1 Updated 7/13/2021 Applications Western Blot, ELISA, Electron Microscopy, Flow Cytometry, Immunocytochemistry/Immunofluorescence, Immunohistochemistry, Immunohistochemistry-Frozen, Immunohistochemistry-Paraffin, Immunoprecipitation, Immunohistochemistry Free-Floating, Immunohistochemistry Whole-Mount, Knockdown Validated Recommended Dilutions Western Blot 1:500-1:5000, Flow Cytometry 1:10-1:1000, ELISA 1:20000- 1:120000, Immunohistochemistry 1:200-1:3000, Immunocytochemistry/Immunofluorescence 1:500-1:5000, Immunoprecipitation 1:10-1:500, Immunohistochemistry-Paraffin 1:10-1:500, Immunohistochemistry- Frozen 1:50-1:250, Electron Microscopy 1:10-1:500, Immunohistochemistry Free-Floating, Immunohistochemistry Whole-Mount, Knockdown Validated Application Notes This antibody is designed to detect GFP and its variants. GFP antibody can be used to detect GFP by ELISA (sandwich or capture) for the direct binding of antigen and recognizes wild type, recombinant and enhanced forms of GFP. This Biotin conjugated polyclonal anti-GFP used in a sandwich ELISA is well suited to titrate GFP in solution using this antibody in combination with monoclonal anti- GFP using either form of the antibody as the capture or detection antibodies. However, use the monoclonal form only for the detection of wild type or recombinant GFP as this form does not sufficiently detect 'enhanced' GFP. The detection antibody is typically conjugated to biotin and subsequently reacted with streptavidin conjugated HRP. This antibody can be used to detect GFP by immunofluorescence microscopy in prokaryotic (E.coli) and eukaryotic (CHO cells) expression systems and can detect GFP containing inserts. Significant amplification of signal is achieved using fluorochrome conjugated polyclonal anti- GFP relative to the fluorescence of GFP alone. For immunoblotting use either alkaline phosphatase or peroxidase conjugated polyclonal anti-GFP to detect GFP or GFP containing proteins on western blots. Optimal titers for applications should be determined by the researcher. Use in Knockdown Validated reported in scientific literature (PMID: 32905777). Images Western Blot: GFP Antibody [NB600-308] - Wild type GFP (0.1 ug) was used to spike HeLa whole cell lysate. Load: 30 ug per lane. Primary antibody: GFP antibody at 1:1000 for overnight at 4C. Secondary antibody: IR Dye800 Goat-anti-Rabbit IgG [H&L] MX10 at 1:10,000 for 45 min at RT. Block: 5% BLOTTO in PBS overnight at 4C. Predicted/Observed size: 27 kDa for epitope tag GFP. Other band(s): none. Immunocytochemistry/Immunofluorescence: GFP Antibody [NB600-308] - Analysis of GFP in transgenic mouse pancreas in OCT. The blue region in the center is an islet which does not express GFP and is negative. Image from verified customer review. Page 3 of 6 v.20.1 Updated 7/13/2021 Western Blot: GFP Antibody [NB600-308] - analysis of GFP tagged PKA subunits over-expressed in HEK293T cells using GFP antibody. Image from verified customer review. Immunohistochemistry: GFP Antibody [NB600-308] - Analysis of GFP in mouse retinal cells. Image courtesy of anonymous customer review. Immunohistochemistry-Paraffin: GFP Antibody [NB600-308] - Staining of GFP+ hepatocytes (brown) transplanted into the liver of a recipient animal using anti-GFP antibody. Cyclin D1 double staining in blue. Image from verified customer review. Immunohistochemistry-Frozen: GFP Antibody [NB600-308] - Adult mouse brain tissue. This image was submitted via customer review. Page 4 of 6 v.20.1 Updated 7/13/2021 Immunoprecipitation: GFP Antibody [NB600-308] - IP analysis of GFP in S2 Cells (Drosophila). Image from verified customer review. Immunoprecipitation: GFP Antibody [NB600-308] - Immunoprecipiation experiments showing that GFP-MISP binds endogenous IQGAP1 (upper panel) and MISP binds to IQGAP1 endogenously using specific antibodies (lower panel) in mitotically arrested (taxol and nocodazole, respectively) HeLa cell lysates. Image collected and cropped by CiteAb from the following publication (nature.com/articles/s41598-018-24682-8), licensed under a CC-BY licence. Page 5 of 6 v.20.1 Updated 7/13/2021 Publications Bourgeois Js, Wang L, Rabino Af Et Al. ARHGEF26 enhances Salmonella invasion and inflammation in cells and mice PLoS pathogens Jul 1 2021 12:00AM [PMID: 34242364] (DB) Girish N, Liu CY, Gadeock S et al. Persistence of Lgr5+ colonic epithelial stem cells in mouse models of inflammatory bowel disease American journal of physiology. Gastrointestinal and liver physiology Jul 14 2021 12:00AM [PMID: 34260310] (IHC-P) Singh B, Khattab F, Chae H et al. KATP channel blockers control glucagon secretion by distinct mechanisms: The direct stimulation of alpha-cells involving a [Ca2+]c rise and an indirect inhibition mediated by somatostatin Molecular metabolism Jun 9 2021 12:00AM [PMID: 34118477] (IHC) Xu PF, Borges RM, Fillatre J et al. Construction of a mammalian embryo model from stem cells organized by a morphogen signalling centre Nature communications Jun 2 2021 12:00AM [PMID: 34078907] (IHC) Green EL Nicotinamide, neural cells, and Parkinsons disease: exploring nicotinamides effects on proliferation, neuronal differentiation, and neuroprotection within in vitro models Thesis Jan 1 2021 12:00AM McElvain LE, Chen Y, Moore JD et al. Specific populations of basal ganglia output neurons target distinct brain stem areas while collateralizing throughout the diencephalon Neuron Apr 1 2021 12:00AM [PMID: 33823137] Bota-Rabassedas N, Banerjee P, Niu Y et al. Contextual cues from cancer cells govern cancer-associated fibroblast heterogeneity Cell reports Apr 20 2021 12:00AM [PMID: 33882319] Oikawa K, Imai T, Thagun C et al. Mitochondrial movement during its association with chloroplasts in Arabidopsis thaliana Communications biology Mar 5 2021 12:00AM [PMID: 33674706] (WB) Yu D, G Febbo I, J Maroteaux M et al. The Transcription Factor Shox2 Shapes Neuron Firing Properties and Suppresses Seizures by Regulation of Key Ion Channels in Thalamocortical Neurons Cerebral cortex (New York, N.Y. : 1991) Mar 2 2021 12:00AM [PMID: 33675359] (IHC, WB) Tang C, Han J, Dalvi S et al. A human model of Batten disease shows role of CLN3 in phagocytosis at the photoreceptor-RPE interface Communications biology Feb 5 2021 12:00AM [PMID: 33547385] (WB, Human, Mouse) Taniguchi T, Zanetti-Yabur A, Wang P et al. Interindividual Diversity in Expression of Organic Anion Uptake
Load more

Recommended publications
  • Mcb 407-Immunology and Immunochemistry-Lecture Note
    MCB 407-IMMUNOLOGY AND IMMUNOCHEMISTRY-LECTURE NOTE DR. D. A. OJO BRIEF HISTORICAL REVIEW OF IMMUNOLOGY The mechanism by which antibody are formed has been debated for years. It was proposed that the specificity of an antibody molecule was determined both by its amino acid sequence but by the molding of the peptide chain around the antigenic determinant. This theory lost favour when it became apparent that antibody-forming cells were devoid of antigen and that antibody specificity was a function of amino acid sequence. At present, the CLONAL (proposed by Burnete) SELECTION THEORY is widely accepted. It holds that an immunologically responsive cell can respond to only one antigen or a closely related group of antigens and that this property is inherent in the cell before the antigen is encountered. According to the clonal selection theory, each individual is endowed with a very large pool of lymphocytes, each of which is capable of responding to a different antigen. When the antigen enters the body, it selects the lymphocyte which has the best “fit” by virtue of a surface receptor. The antigen binds to this antibody-like receptor, and the cell is stimulated to proliferate and form a clone of cells. Thus, selected cells quickly differentiate into plasma cells and secrete antibody which is specific for the antigen which served as the original selecting agent (or a closely related group of antigens). The History of Blood Transfusion Man’s centuries-long desire to perform blood transfusion as a therapeutic procedure forms the cornerstone of the modern science of immunohematology. At present time, the use of whole blood is a well-accepted and commonly employed measure without which many modern surgical procedures could not be carried out.
    [Show full text]
  • TITAN IV Immunoelectrophoresis Procedure
    TITAN IV Immunoelectrophoresis Procedure Cat. No. 9050 and 9061 Helena Laboratories Titan IV Immunoelectrophoresis (IEP) is intended for barbital-sodium barbital buffer with 0.1% sodium azide added semiquantitative determinations by immunoelectrophoresis. as a preservative. WARNING: FOR IN-VITRO DIAGNOSTIC USE ONLY. This SUMMARY product contains sodium azide. Refer to the sodium azide Immunoelectrophoresis (IEP) combines two techniques, warning. electrophoresis and immunodiffusion. In this two-part procedure, Preparation for Use: The plates are ready for use as proteins in a serum or urine sample are first separated packaged. according to charge by electrophoresis. Then, antisera Storage and Stability: Plates should be stored flat, in the complimentary to the proteins under study are applied to the protective packaging, at 2°C to 8°C and are stable until the plate and allowed to diffuse. When a favorable antigen to expiration date indicated on the label. DO NOT FREEZE antibody ratio exists, a precipitin arc will form on the plate. PLATES OR EXPOSE THEM TO EXCESSIVE HEAT. IEP is used for the diagnosis and differential diagnosis of Signs of Deterioration: The plates should have a smooth, monoclonal gammopathies when using serum or urine clear agarose surface. Discard the plates if they appear 1-4 specimens. The method is also used for a number of other cloudy, show bacterial growth, or if they have been exposed to purposes, including screening for circulating immune freezing (a cracked or bubbled surface) or excessive heat (a complexes, characterization of cryoglobulinemia and dried, thin surface). pyroglobulinemia, recognition and characterization of antibody 2. Antisera for Assay of Immunoglobulins syndromes, and recognition and characterization of the various Antiserum to Human IgG, Cat.
    [Show full text]
  • IMMUNOELECTROPHORESIS TEST Dr
    [Type text] IMMUNOELECTROPHORESIS TEST Dr. Daljeet Chhabra Department of Veterinary Microbiology College of Veterinary Science and A.H., Mhow NDVSU, Jabalpur The term “immunoelectrophoresis” was first coined by Grabar and Williams in 1953. Immunoelectrophoresis refers to precipitation in agar under an electric field. It is a process of a combination of immuno-diffusion and electrophoresis. An antigen mixture is first separated into its component parts by electrophoresis and then tested by double immuno-diffusion. Antigens are placed into wells cut in a gel (without antibody) and electrophoresed. A trough is then cut in the gel into which antibodies are placed. The antibodies diffuse to meet diffusing antigens, and lattice formation and precipitation occur permitting determination of the nature of the antigens. Principle: When an electric current is applied to a slide layered with gel, the antigen mixture placed in wells is separated into individual antigen components according to their charge and size. Following electrophoresis, the separated antigens are reacted with specific antisera placed in troughs parallel to the electrophoretic migration and diffusion is allowed to occur. Antiserum present in the trough moves toward the antigen components resulting in the formation of separate precipitin lines in 18-24 hrs, each indicating reaction between individual proteins with its antibody. Materials required: Agarose gel, slides, well cutters, Immunoelectrophoresis machine, buffer, etc. Procedure: 1. Agarose gel is prepared on a glass slide put in a horizontal position. 2. After well cutting, sample is added in well. 3. The gel is placed into the electrophoresis chamber with the samples on the cathodic side, and electrophoresis runs for 20 mins/ 100 volts.
    [Show full text]
  • The Power and Limitations of Influenza Virus Hemagglutinin Assays
    ISSN 00062979, Biochemistry (Moscow), 2017, Vol. 82, No. 11, pp. 12341248. © Pleiades Publishing, Ltd., 2017. Original Russian Text © N. B. Ustinov, E. G. Zavyalova, I. G. Smirnova, A. M. Kopylov, 2017, published in Biokhimiya, 2017, Vol. 82, No. 11, pp. 15771592. REVIEW The Power and Limitations of Influenza Virus Hemagglutinin Assays N. B. Ustinov, E. G. Zavyalova*, I. G. Smirnova, and A. M. Kopylov Lomonosov Moscow State University, Faculty of Chemistry, 119991 Moscow, Russia; Email: [email protected] Received May 12, 2017 Revision received August 8, 2017 Abstract—Influenza virus hemagglutinins (HAs) are surface proteins that bind to sialic acid residues at the host cell surface and ensure further virus internalization. Development of methods for the inhibition of these processes drives progress in the design of new antiviral drugs. The state of the isolated HA (i.e. combining tertiary structure and extent of oligomerization) is defined by multiple factors, like the HA source and purification method, posttranslational modifications, pH, etc. The HA state affects HA functional activity and significantly impacts the results of numerous HA assays. In this review, we ana lyze the power and limitations of currently used HA assays regarding the state of HA. DOI: 10.1134/S0006297917110025 Keywords: influenza virus, surface antigens, influenza hemagglutinin, inhibitors of hemagglutination, monoclonal antibod ies, ELISA Influenza is one of the most common infectious dis endosome with subsequent nucleoprotein release from eases: 510% of adults and 2030% children are infected the endosome (HA and M2 protein), and detachment of with influenza each year. Influenza infection itself lasts the newly synthesized virus particles from the host cell only for several days, but the high risk for human health surface (neuraminidase, NA) [35].
    [Show full text]
  • Immunoelectrophoresis: a Possible Source of Error
    J Clin Pathol: first published as 10.1136/jcp.33.5.500 on 1 May 1980. Downloaded from J Clin Pathol 1980; 33: 500-504 Detection of monoclonal immunoglobulins by immunoelectrophoresis: a possible source of error AM SMITH, RA THOMPSON, AND MR HAENEY From the Supra Regional Protein Reference Unit, Department ofImmunology, East Birmingham Hospital, Bordesley Green East, Birmingham, B9 5ST, UK SUMMARY The technique of immunoelectrophoresis (IEP) is widely employed in the qualitative analysis of serum immunoglobulins. The most commonly used support media are agarose or agar gels, but the mobility of immunoglobulins is different in these two media. The presence of a small amount of a cathodal monoclonal immunoglobulin G may not be detected on IEP in agar if it is masked by larger amounts of polyclonal immunoglobulin of the same class. In these circum- stances the use of agarose imparts to the monoclonal protein a different mobility from that of the bulk of the serum IgG and allows its positive identification. Since its introduction' immunoelectrophoresis (IEP) phoresis may then be interpreted as an artefact. has proved a valuable tool in the qualitative investi- This paper reports five cases in which the presence gation of proteins, particularly human serum of a monoclonal protein could not be shown immunoglobulins. Classically, the technique involves convincingly on IEP in agar, although all were the separation of proteins by electrophoresis in a clearly visible after IEP in agarose. gel support medium, followed by visualisation of the separated proteins using specific antisera. Initial Material and methods separation of the proteins depends on the charge carried by each protein.
    [Show full text]
  • Hemagglutinin from Acrididae (Grasshopper)
    Hemagglutinin from Acrididae (Grasshopper) : preparation and properties by Mark Richard Stebbins A thesis submitted in partial fulfillment of the requirements for the degree of Master of Science in Biochemistry Montana State University © Copyright by Mark Richard Stebbins (1984) Abstract: The proteinaceous hemagglutinin (lectin) present in the hemolymph of Melanoplus sanguinipes (F.), was isolated and biochemically characterized. The protein was purified to homogeneity by affinity chromatography on a column of Sepharose-galactose. The hemagglutinin showed broad specificity and agglutinated several erythrocyte types. Gel filtration and electrophoresis showed that grasshopper hemagglutinin was a high molecular weight (600-700 K dalton) non-covalent aggregate of 70 K dalton subunits. The 70 K dalton subunits contained two disulfide-linked polypeptide chains of molecular weight 40,000 and 28,000 respectively. The purified hemagglutinin contained a preponderance of acidic and polar amino acid residues and a small amount of glucosamine. Hemagglutination activity toward human asialo erythrocytes was destroyed by treatment of the hemagglutinin with trypsin, heat or EDTA. Hemagglutination inhibition studies showed that low concentrations (<5 mM) of both galactosidic and glucosidic carbohydrates are bound by the hemagglutinin and cause inhibition of erythrocyte agglutination. The strongest inhibitors of hemagglutination were the alpha anomers of D-galactose. Hemolymphatic hemagglutinin isolated from Melanoplus differentiaIis yielded identical physicochemical results as did hemagglutinin from Melanoplus sanguinipes. It was concluded that a single hemagglutinin protein was the substance responsible for all hemagglu-tinating activity present in the hemolymph of either species. Research directed toward the elucidation of the possible roles that grasshopper hemagglutinin plays in grasshopper immune/defense mechanisms was initiated by producing antibodies to purified hemagglutinin in rabbits and mice.
    [Show full text]
  • Inmunoelectrophoresis
    INMUNOELECTROPHORESIS This protocol is based on the EDVOTEK® protocol “Radial Immunodiffusion”. 10 groups of students 1. EXPERIMENT OBJECTIVE In this experiment, students are introduced to the use of immunoelectrophoresis to separate and characterize a mixture of proteins and examine the specificity of the antigen-antibody interaction. 2. EXPERIMENT COMPONENTS for 10 groups of students COMPONENTS STORE A IgG 4-8ºC B Whole serum 4-8ºC C Albumin 4-8ºC D Antibody to whole serum 4-8ºC E Antibody to Ig 4-8ºC F UltraSpec-Agarosa™ 4-8ºC G Electrophoresis (25x concentrate) 4-8ºC Microtest tubes 10 ml pipettes Filter paper Well cutters Petri plates (60 mm) NOTE: Store all components at the indicated temperatures upon receipt. NOTE: No human material is used in this practice. NOTE: All components are intended for educational research only. They are not to be used for diagnostic or drug purposes, nor administered to or consumed by humans or animals. 2.1 Requirements Horizontal Electrophoresis Apparatus Power Supply Automatic Micropipet and Tips (5-50 μl) Waterbath Microscope Slides (1" x 3") Distilled Water 400 to 600 ml Beaker 1000 ml Graduated Cylinder Bunsen Burner, Heat Plate, or Microwave Container with Lid (large enough to hold electrophoresis trays) Paper Toweling Plastic Wrap or Foil 37°C Incubation Oven NOTE: Make sure glassware is clean, dry, and free of soap residue. For convenience, you can buy additional disposable transfer pipettes to the steps of extraction and washing liquids. 3. BACKGROUND INFORMATION Immunoelectrophoresis Immunoelectrophoresis is used in both clinical and research laboratories for separating and identifying proteins on the basis of their electrophoretic behavior and their immunological properties.
    [Show full text]
  • The Application of Labeled Antibody Technics in Studying Cell Antigens1
    [CANCER RESEARCH 28, 1372-1381,July 1968] The Application of Labeled Antibody Technics in Studying Cell Antigens1 Robert C. Mellors The Hospital for Special Surgery, Affiliated with The New York Hospital, Cornell University Medical College, and the Department of Pathology, Cornell University Medical College, New York, New York INTRODUCTION by the direct (one-step, one-layer) procedure (12), that is, direct staining with fluorescent antibody, or by the indirect The underlying principles of the immunofluorescence method, (multiple step, "sandwich") procedure (100), in which un originated and developed by A. H. Coons and his associates (10- labeled antibody reacts with antigen and is followed by, and 12), are these: in turn stained by fluorescent antibody against the deposited (a) Antibodies can be conjugated with chemical compounds y-globulins. Antibody (Chart lò) is usually localized by the (32), including colored dyes (57), without destroying the ca indirect procedure (13), using a layer of antigen followed by pacity of the antibody to react specifically with its antigen. fluorescent antibody against this antigen. However, labeled (6) Antibodies can be conjugated with fluorescent dyes antigens of high molecular weight and labeled antigen-excess (fluorescent antibodies) and used as immunospecific stains for soluble immune complexes (preformed "sandwich") can be the histochemical detection of antigens (11, 12). used for the detection of antibody by the direct procedure (63- (c) Antigens used indirectly as unlabeled intermediaries 65). A provisional or presumptive identification of antigen- (followed by fluorescent antibodies) or directly when labeled antibody complex (Chart le) and/or denatured or aggregated (fluorescent antigens) serve as immunospecific reagents for the •y-globulinismade by the indirect procedure using a layer of histochemical detection of antibodies (13).
    [Show full text]
  • Detection of Porcine Rotavirus by Em, Elisa and Ciet·
    Acta vet. scand. 1981,22, 32-38. From the Department of Veterinary Virology and Immunology, Hoyal Veterinary and Agricultural University, Copenhagen, Denmark. DETECTION OF PORCINE ROTAVIRUS BY EM, ELISA AND CIET· By Jon Askaa and Bucliardt Bloch ASKAA, JON and BUCHARDT BLOCH: Detection of porcine rota virus by EM, ELISA and CIET. Acta vet. scand. 1981, 22, 32-38. ­ Feces samples from swine-herds with severe problems of neonatal diarrhoea, 3 weeks scours or early weaning diarrhoea were examined for porcine rotavirus using three techniques: E:\1, ELISA and CIET. Infection with rotavirus was found in about one third of the feces samples, representing more than half of the examined swine-herds. EM and ELISA revealed nearly all the samples found to be positive, while CIET as used here detected only half of them. p 0 r ci n e rot a vir us; EM; C lET; ELI SA; d i a r rho e a. Rotavirus has been detected in pig feces since 1975 (Rodger et al. 1975) and considered to be the cause of, or to be a contri­ butory agent for, certain forms of neonatal diarrhoea, 3 weeks scours and early weaning diarrhoea (Rodger et al., Leece et al, H)76, McNulty et al. 1976, Woode et al. 19i6, Clwsey & Lucas 19i7, Bohl et al. 1978, 'I'zipori & Williams 1978, Debouck & Pen saert 1979) . Further the diarrhoea complex has been reproduced experimentally-by inoculation of field isolates and of in vitro cultured virus on colostrum-deprived piglets (Leece et al., McNulty et al., Woode et al., Theil et al.
    [Show full text]
  • A Tumor-Associated Antigen in Human Nephroblastomas (Wilms' Tumor/Virus/Immunoelectrophoresis/Immunofluorescence) P
    Proc. Nat. Acad. Sci. USA Vol. 70, No. 7, pp. 2051-2054, July 1973 A Tumor-Associated Antigen in Human Nephroblastomas (Wilms' tumor/virus/immunoelectrophoresis/immunofluorescence) P. BURTIN AND M. C. GENDRON Laboratorie d'Immunochimie, Institut de Recherches Scientifiques sur le Cancer, 94800 Villejuif, France Communicated by Andre LIwoff, April19, 1978 ABSTRACT Antisera prepared against extracts of diseases (tuberculosis, pyelonephritis, and polykystic disease), human nephroblastomas (Wilms' tumors) allowed the characterization in these extracts, and in a few extracts three were obtained at necropsy from patients who died from of tumors of other organs, of a tumor-associated antigen. different diseases, cancerous or not. A pool of 18 kidneys of This antigen is different from all previously described anti- children who died from congenital cardiopathies was studied. gens, and was named W antigen (W for Wilms). It does not Other noncancerous organs obtained at necropsy were: livers, seem to be a carcinoembryonic antigen, and hence it adrenals, lung, heart, thymus, and epididymis. Those ob- could be of viral origin. tained after surgery were: colonic and gastric mucosae, Immunochemical studies have led to the discovery of several spleen, and urinary bladder. Different kinds of mucus secre- tumor-associated antigens, all of fetal origin. Two of them have tion were: gastric mucus, jejunal juice, and pools of saliva. been isolated, and their usefulness in diagnosis and surveil- Fetal Organs were generally obtained from the third to the lance of some carcinomas has been well documented: they are sixth month of gestation: kidney, liver, lung, adrenals, muscle, the a fetoprotein (1, 2) and the carcinoembryonic antigen of epididymis, urinary bladder, skin, stomach, and colon.
    [Show full text]
  • Comparison of Apolipoprotein D Determination Methods in Breast Cancer
    ANTICANCER RESEARCH 28 : 1151-1160 (2008) Comparison of Apolipoprotein D Determination Methods in Breast Cancer H VARD S ILAND 1,2 , IVAR SKALAND 3, EMIEL A.M. JANSSEN 3, EINAR GUDLAUGSSON 3, HARÅTWIG K ØRNER 1,2 , JAN ERIK VARHAUG 2,4 , JON ARNE S REIDE 1,2 and JAN P.A. BAAK 3,5,6 Ö Ø Departments of 1Surgery and 3Pathology, Stavanger University Hospital, Stavanger; 4Section for Endocrine and Breast Surgery, Haukeland University Hospital, Bergen; 2Department of Surgical Sciences, and the 5Gade Institute, University of Bergen, Norway; 6Free University, Amsterdam, The Netherlands Abstract. Background: Apolipoprotein D (ApoD) is a hypothesised that ApoD is a marker for steroid signalling in promising prognostic and predictive factor in breast cancer, but breast cancer (7, 8), and its high affinity to arachidonic acid the analysis methods and results vary. Patients and Methods: (9), progesterone and tamoxifen (10) makes it a very Determination of ApoD content by immunoelectrophoresis in interesting putative prognostic and predictive marker in tumour cytosol (EPC), immunohistochemistry (IHC) in whole breast cancer. sections (WS) and tissue micro arrays (TMA) were compared In breast cancer research, two different methods have in 283 breast carcinomas. Results: With EPC, 45% and with been used for ApoD determination, in tumour cytosol with IHC, 71% of the tumours were ApoD-positive. Correlation fresh frozen material by means of a precipitating antibody between the degree s of ApoD positivity by ECP and IHC was used in immunoelectrophoresis (EPC) (11) and by an poor (R 2=0.04), caused by higher sensitivity of the IHC immunohistochemical (IHC) method on paraffin- (resulting in many ECP negative carcinomas being IHC embedded tumour material (12).
    [Show full text]
  • Immunology and Serology
    LECTURE NOTES For Medical Laboratory Technology Students Immunology and Serology Selamawit Debebe Alemaya University In collaboration with the Ethiopia Public Health Training Initiative, The Carter Center, the Ethiopia Ministry of Health, and the Ethiopia Ministry of Education 2004 Funded under USAID Cooperative Agreement No. 663-A-00-00-0358-00. Produced in collaboration with the Ethiopia Public Health Training Initiative, The Carter Center, the Ethiopia Ministry of Health, and the Ethiopia Ministry of Education. Important Guidelines for Printing and Photocopying Limited permission is granted free of charge to print or photocopy all pages of this publication for educational, not-for-profit use by health care workers, students or faculty. All copies must retain all author credits and copyright notices included in the original document. Under no circumstances is it permissible to sell or distribute on a commercial basis, or to claim authorship of, copies of material reproduced from this publication. ©2004 by Selamawit Debebe All rights reserved. Except as expressly provided above, no part of this publication may be reproduced or transmitted in any form or by any means, electronic or mechanical, including photocopying, recording, or by any information storage and retrieval system, without written permission of the author or authors. This material is intended for educational use only by practicing health care workers or students and faculty in a health care field. Immunology and Serology Preface Immunology and serology is an advanced science dealing with how the human immune system organized, function and the different types of serological techniques. It is a very vast subject covering a wide area of technology.
    [Show full text]