Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Microarrays antibody

Kusnezow W., Hoheisel J.D., Antibody microarrays promises and problems, Biotechniques 2002 33 14-23. [Pg.499]

Angenendt P., Gloekler J., Murphy D., Lehrach H., Cahill D.J., Toward optimized antibody microarrays a comparison of current microarray support materials, Anal Biochem. 2002 309 253-260. [Pg.500]

Ko I-K, Kato K, Iwata H (2005) Parallel analysis of multiple surface markers expressed on rat neural stem cells using antibody microarrays. Biomaterials 26 4882 -891... [Pg.196]

Wang, X. Zhao, M. Nolte, D. D., Area scaling of interferometric and fluoresecnt detection of protein on antibody microarrays, Biosen. Bioelectron. 2008... [Pg.316]

In 1991, Roger Ekins convinced Boehringer-Marmheim to pursue commercial development of his Microspot technology (Ekins, 1998). Antibody microarrays were constructed on single-well polystyrene carriers by ink-jet printing. Unfortunately, no product was commercialized. [Pg.70]

Substrates for the creation of protein microarrays were initially selected from those used for DNA arrays, for example, PLL glass slides. At first, these substrates proved to be sufficient for antibody microarray studies. However, not all proteins will behave well or similarly on a particular substrate material. New solid phases applicable for protein microarrays need to be found. [Pg.89]

Angenendt, R, Glokler, J., Sobek, J., Lehrach, H., and Cahill, D.J., Next generation of protein microarray support materials Chromatography A 1009 97-104, 2003. evaluation for protein and antibody microarray applications. [Pg.89]

Angenendt et al. (2003) evaluated several slide surface chemistries for use as protein and antibody microarrays. They reasoned that because proteins vary greatly in their surface charge and relative hydrophobicity, a careful selection of surface chemistry may be important for obtaining optimal performance for a particular protein. Thus, several commercially available slide surface chemistries were evaluated for performance in model arrays... [Pg.141]

Usui-Aoki, K., K. Shimada, and H. Koga (2007) A novel antibody microarray format using non-covalent antibody immobilization with chemiluminescent detection. Mol Biosyst. 3, 36 2. [Pg.213]

Belov L, de la Vega O, dos Remedios CG, Mulligan SP, Christopherson RI. Immunophenotyping of leukemias using a cluster of differentiation antibody microarray. Cance Res 2001 61(ll) 4483-4489. [Pg.184]

Because protein microarrays (antibody microarrays) have been successfully used for a variety of applications, such as antibody response profiling, identification and detection of bacterial and protein analytes, as well as disease proteomics with a clear focus toward oncoproteomics, it can be assumed that they will also prove to be a useful tool in studies on allergens (Wingren and Borrebaeck, 2007). [Pg.106]

Borrebaeck, C.A.K. and Wingren, C. 2007. High-throughput proteomics using antibody microarrays An update. Expert Rev Mol Diagn 7 673-686. [Pg.108]

Ellmark, P, Woolfson, A, Belov, L., and Christopherson, R.I. 2008. The applicability of a cluster of differentiation monoclonal antibody microarrays to the diagnosis of human disease. In Genomic Protocols, 2nd ed., M. Starkey and R. Elaswarapu, Eds., Humana Press, Totowa, NJ Meth Mol Biol 439 199-209. [Pg.109]

Miller JC, Zhou H, Kwekel J, Cavallo R, Burke J, Butler EB, Teh BS, Haab BB, Antibody microarray profiling of human prostate cancer sera Antibody screening and identification of potential biomarkers, Proteomics, 3 56-63, 2003. [Pg.537]

Haab BB. Methods and applications of antibody microarrays in cancer research. Proteomics 2003 3(11) 2116-2122. Review. [Pg.135]

Antibody arrays immobilized on glass surfaces mimic DNA microarrays in format and spot size. The biggest challenge in protein profiling using antibody microarrays is selection of validated antibodies that are useful in the desired sample environment. Many of the initial reports used antibody arrays assayed for cytokines because serum presents a relatively simple sample assay environment compared to tissue and also because there are numerous validated antibodies available for this clinically important set of proteins. Tissue and cell lysates present more complex assay environments with more opportunities for antibody cross-reactivity and other interferences which erode the biological meaningfulness of the data. [Pg.62]

Figure 4.12 describes two popular antibody microarrays formats that are constructed for antigen capture in small sample volumes with detection by either sandwich immunoassay or antigen labeling. In sandwich immunoassay, capture antibodies are arrayed and immobilized to select specific proteins which are then found by a second labeled detection antibody. In protein target labeling, all proteins in the sample are prelabeled (i.e., fluorescent dyes) prior to capture by immobilized antibody arrays. In direct assay systems, sample proteins are directly immobilized onto... [Pg.62]

The capabilities of antibody microarray technology are similar to those for DNA array methods selectivity of immunoreagents in complex protein lysates rapid, massively parallel analysis of proteins small sample volume requirement and automation and compatibility with DNA microarray technologies (in hardware, software, and bioinformatics) also, native proteins are analyzed, which affords information on specific structure and protein-protein interactions. Limitations of this... [Pg.63]

The performance of protein or antibody microarrays is dependent on various factors. One of these is the use of an appropriate microarray surface for the immobilization of the protein or antibody samples. Most conventional microarray surfaces have been adapted from DNA chip technology. DNA can easily be immobilized by electrostatic interactions of the phosphate backbone onto a positively charged surface. In contrast to DNA, as already mentioned, proteins are chemically and structurally much more complex and show variable charges, which may influence the efficiency of protein attachment. Additionally, proteins lose their structure and biochemical activity easily. For example, globular proteins consist of a hydrophilic exterior and a hydrophobic interior. When immobilized on a hydrophobic surface, the inside of the protein turns out, which may destabilize the structure and, simultaneously, the activity of the protein. These considerations demonstrate the complex requirements for protein immobilization. [Pg.139]

Protein Microan ay Peptide Microarray Antibody Microarray... [Pg.144]

Next generation of protein microarray support materials evaluation for protein and antibody microarray applications. [Pg.151]


See other pages where Microarrays antibody is mentioned: [Pg.274]    [Pg.283]    [Pg.88]    [Pg.21]    [Pg.21]    [Pg.68]    [Pg.71]    [Pg.141]    [Pg.205]    [Pg.222]    [Pg.203]    [Pg.205]    [Pg.135]    [Pg.404]    [Pg.424]    [Pg.11]    [Pg.104]    [Pg.126]    [Pg.104]    [Pg.113]    [Pg.63]   
See also in sourсe #XX -- [ Pg.113 ]

See also in sourсe #XX -- [ Pg.4 , Pg.600 ]

See also in sourсe #XX -- [ Pg.600 ]




SEARCH



Microarray

Microarrays

© 2024 chempedia.info