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The absence of the light chains and CH1 domain in Camelidae heavy chain antibodies (HCAbs) give them many special characteristics that are different and superior to conventional antibody. HCAbs have the capability to resist heat and extreme pH without losing their activity. These advantages of HCAbs render them eligible to be used for diagnostic and therapeutic purposes. Mouse monoclonal antibodies and camel polyclonal antibodies against Her2, CD31 and Bcl2 peptides were produced, and assessed using ELISA, immunoblot and immunohistochemistry (IHC). In IHC, newly prepared C2B7 MCA…mehr

Produktbeschreibung
The absence of the light chains and CH1 domain in Camelidae heavy chain antibodies (HCAbs) give them many special characteristics that are different and superior to conventional antibody. HCAbs have the capability to resist heat and extreme pH without losing their activity. These advantages of HCAbs render them eligible to be used for diagnostic and therapeutic purposes. Mouse monoclonal antibodies and camel polyclonal antibodies against Her2, CD31 and Bcl2 peptides were produced, and assessed using ELISA, immunoblot and immunohistochemistry (IHC). In IHC, newly prepared C2B7 MCA anti-CD31-peptide was found be to as reactive as the commercially available anti-CD31 MCA. In contast, Anti-Her2 and anti-Bcl2 peptides MCA showed nonspecific staining reaction when they were tested on breast cancer and follicular hyperplasia tissues, respectively. Purified camel polyclonal anti-CD31-peptide antibodies staining specifically the blood vessel endothelial cells and nonspecifically epithelial cells. Purified camel polyclonal anti-Her2 peptide antibodies showed cytoplamsic reactivity.
Autorenporträt
Abdel-Rahman Mohammad Rawashdeh - Licenciado en Ciencias Biológicas, Universidad de Yarmouk, Irbid, Jordania, 2008.