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4 edition of Development and characterization of a monoclonal antibody to calnexin, and ER marker protein found in the catalog.

Development and characterization of a monoclonal antibody to calnexin, and ER marker protein

Carmen Tang

Development and characterization of a monoclonal antibody to calnexin, and ER marker protein

by Carmen Tang

  • 350 Want to read
  • 23 Currently reading

Published by National Library of Canada in Ottawa .
Written in English


Edition Notes

Thesis (M.Sc.) -- University of Toronto, 1999.

SeriesCanadian theses = -- Thèses canadiennes
The Physical Object
FormatMicroform
Pagination2 microfiches : negative. --
ID Numbers
Open LibraryOL22344068M
ISBN 100612454169
OCLC/WorldCa49927257

marker Clean chip and add gel and marker Improving characterization of monoclonal antibodies Making a better biotherapeutic Novem Protein Characterization. 28 What is lab-on-a . Calreticulin and calnexin in the endoplasmic reticulum are important for phagocytosis to an antibody against an inherent ER marker protein, of the cell is most prominently labeled with the.

Consistent with this finding, FRAP/mTOR is cofractionated with calnexin, an ER marker protein. Biochemical characterization suggests that FRAP/mTOR is a peripheral ER/Golgi protein with tight.   Some monoclonal antibody drugs block protein-cell interactions necessary for the development of new blood vessels. Blocking immune system inhibitors. Certain proteins that bind to immune system cells are regulators that prevent overactivity of the system. Monoclonal antibodies that bind to these immune system cells give the cancer-fighting.

  Subcellular distribution of SLC35C1HEK cells were transfected with Flag‐tagged SLC35C1. 48 h later, immunofluorescence was performed with antibodies against Flag tag, GM (a marker for Golgi apparatus), calnexin (a marker for ER), Rab5 (a marker for early endosome), Rab7 (marker for late endosome), Lamp1 (a marker for lysosome) and TOM20 (a marker for mitochondria).   Our results show that ER did not contain recognizable GOS28, a Golgi marker protein, whereas Golgi was free from calnexin, an ER marker protein (Fig. 1 A). Both ER and Golgi membranes were found to be devoid of Rab11, an endosomal/lysosomal marker protein (data not shown).


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Development and characterization of a monoclonal antibody to calnexin, and ER marker protein by Carmen Tang Download PDF EPUB FB2

A monoclonal anti-calnexin antibody on the other hand would be more stable and available in indefinite supply, and is thus preferred.

In this thesis, 1 will concentrate on the development and characterization of a monoclonal antibody to calnexin cytoplasmic domain. I hypothesize that the use of thisAuthor: Carmen Tang. Rabbit polyclonal Calnexin antibody. Validated in WB, ICC/IF and tested in Mouse, Rat, Dog, Human, Pig, Chinese hamster.

Cited in 41 publication(s). Independently reviewed in 21 review(s). Immunogen 4/5(21). Calreticulin and calnexin are Ca 2+ ‐binding proteins with chaperone activity in the endoplasmic reticulum.

These proteins have been eliminated by gene replacement in Dictyostelium, the only microorganism known to harbor both proteins; family members in Dictyostelium are located at the base of phylogenetic trees.

A dramatic decline in the rate of phagocytosis was observed in double Cited by: Monoclonal Antibodies from mouse and rat. Custom monoclonal antibody development from mice or rats with any kind of antigen.

To receive the best results, four different antigen concentrations are used for the immunizations. This ensures an optimal immune response. The spleen from the mouse with the best titer will be used for the fusion. Monoclonal antibodies can cause side effects, which can differ from person to person.

The ones you may have and how they make you feel will depend on many factors, such as how healthy you are before treatment, your type of cancer, how advanced it is, the type of monoclonal antibody.

Calreticulin and calnexin are Ca 2+-binding proteins with chaperone activity in the endoplasmic proteins have been eliminated by gene replacement in Dictyostelium, the only microorganism known to harbor both proteins; family members in Dictyostelium are located at the base of phylogenetic trees.

A dramatic decline in the rate of phagocytosis was observed in double. Sato, K., Nishikawa, S. & Nakano, A. Membrane protein retrieval from the Golgi apparatus to the endoplasmic reticulum (ER): characterization of the RER1 gene product as a component involved in ER.

Characterization and application of monoclonal antibodies to bovine viral diarrhea virus nonstructural protein 5A. the distribution of the ER marker-protein calnexin. The. To visualize the ER of cells during PRRSV infection, we investigated ER morphology by immunofluorescence microscopy using an antibody against the ER marker protein, calnexin.

Highlights Monoclonal antibodies (mAbs) are essential drugs for treatment of various diseases. The heterogeneity of mAbs is significant and should be well characterized.

Reversed-phase liquid chromatography is a powerful strategy for mAbs analysis. Capillary-zone electrophoresis is a good option, because of its MS compatibility.

Adsorption of mAbs is a major concern with both. Erlin-1 and -2 localize to the ER. HeLa cells were transfected with full-length erlinGFP or erlinGFP as indicated.

Cells were counterstained using antibodies to the ER marker proteins (A) calnexin or (B) calreticulin (red) as indicated and visualized using wide-field microscopy.

Bars, 10 μm. Two monoclonal antibodies (MAbs) against CA IX were generated as specific immunological tools for clinical detection and therapy. Their diagnostic value has been confirmed by immunohistochemistry and radiolabeled monoclonal antibody imaging.

Recently, the importance of CA XII as a serodiagnostic marker for lung cancer has been demonstrated. mAbs that are sensitive to protein conformation can be helpful in studies of protein structure and function; in particular, mAb fragments are useful reagents in membrane protein crystallization.

We immunized mice with the rat 5HT2c serotonin receptor and derived clonal hybridoma cells, which we tested for specific antigen reactivity by using the complementarity of purified protein.

This is a Validated Antibody Database (VAD) review about human calnexin, based on published articles (read how Labome selects the articles), using calnexin antibody in all is aimed to help Labome visitors find the most suited calnexin antibody. Please note the number of articles fluctuates since newly identified citations are added and citations for discontinued catalog numbers.

T-cell protein tyrosine phosphatase gives rise to two splice isoforms: TC48, which is localized to the endoplasmic reticulum (ER) and TC45, a nuclear protein. The present study was undertaken to identify proteins that are involved in targeting TC48 to the ER.

We identified two TCinteracting proteins, p25 and p23, from a yeast two-hybrid screen. p23 and p25 are members of a family of. The largest group of these RF are those that express kappa light chains reactive with the monoclonal antibody 17–, which is a serological marker for the kv gene, in association with V H genes whose products are reactive with the monoclonal antibody G6, which is a serological marker for the DP and hv genes (see later).

Monoclonal antibodies (mAbs) are antigen-recognizing glycoproteins that are made by identical immune cells, all of which are clones of a unique parent cell. SinceFDA has approved at least five monoclonal antibodies per year, and this trend shows no signs of slowing.

B and C, immunocytochemical localization of PLD4 protein (green) and either calnexin, an ER marker (red) (B) or gol a trans -Golgi marker (red) (C), in HeLa cells transfected with pcDNA3-PLD4.

PLD4 is colocalized with calnexin in the ER and with golgin 97 in the Golgi complex. Scale bars = 10 um. HEK cells expressing GFP-tagged TLR9 were permeabilized and counterstained with a monoclonal antibody (mAb) to calnexin, an ER-resident protein.

A marker protein for the development of new. Calnexin, which is known as a marker protein of the ER (Cao et al., ), is a membrane-bound molecular chaperone protein. The structure of calnexin contains distinct regions of transmembrane domain, P-domain, calcium-binding region and lectin site, respectively.

ER stress response is regulated by Bax inhibitor-1 (BI-1), an anti-apoptotic protein capable of inhibiting Bax activation and translocation to the mitochondria. 12 Physiologically, BI-1 is linked to the dynamic Ca 2+ environment of the ER.

13, 14 Dynamic Ca 2+ status is linked to chaperones, such as calnexin and calreticulin. 15 Calnexin has an.Monoclonal antibodies are antibodies with a defined specificity derived from cloned cells or organisms. They can be obtained from immortalised B lymphocytes that are cloned and expanded as continuous cell lines (murine and human monoclonal antibodies) or from rDNA-engineered mammalian or bacterial cell lines (engineered monoclonal antibodies).

INTRODUCTION. The endoplasmic reticulum (ER) 1 is the largest endomembrane system within eukaryotic cells and performs a wide variety of functions including calcium uptake and release, lipid and protein synthesis, protein translocation, folding, glycosylation, concentration, and export to the Golgi complex (for review see Rose and Doms, ; Hurtley and Helenius, ; Sitia .