Poly- and Monoclonal Antibodies Against Recombinant Rat Brain Calbindin D-28K Were Produced to Map Its Selective Distribution in the Central Nervous System
Abstract: Many processes in the CNS depend on calcium. The calcium signal is transduced into an intracellular response via Ca2+-binding proteins, including calbindin D-28K. In many laboratories, polyclonal antibodies against chicken in testinal calbindin D-28K have been used to study its localizatio...
Ausführliche Beschreibung
Autor*in: |
Pinol, M. Rosa [verfasserIn] Kägi, Urs [verfasserIn] Heizmann, Claus W. [verfasserIn] |
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E-Artikel |
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Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1990 |
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Online-Ressource |
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2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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In: Journal of neurochemistry - Oxford : Wiley-Blackwell, 1956, 54(1990), 6, Seite 0 |
Übergeordnetes Werk: |
volume:54 ; year:1990 ; number:6 ; pages:0 |
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DOI / URN: |
10.1111/j.1471-4159.1990.tb04879.x |
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10.1111/j.1471-4159.1990.tb04879.x doi (DE-627)NLEJ240269055 DE-627 ger DE-627 rakwb Pinol, M. Rosa verfasserin aut Poly- and Monoclonal Antibodies Against Recombinant Rat Brain Calbindin D-28K Were Produced to Map Its Selective Distribution in the Central Nervous System Oxford, UK Blackwell Publishing Ltd 1990 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Many processes in the CNS depend on calcium. The calcium signal is transduced into an intracellular response via Ca2+-binding proteins, including calbindin D-28K. In many laboratories, polyclonal antibodies against chicken in testinal calbindin D-28K have been used to study its localization in the brain (normal and degenerated) of various species, including humans, but some of these antisera cross-reacted with other proteins, including calretinin. We purified recombinant rat brain calbindin D-28K to raise antisera in rabbits and purified a recombinant rat–chicken calbindin D28K hybrid protein to immunize mice for the generation of monoclonal antibodies. These antisera were highly specific for calbindin D-28K, as demonstrated by two-dimensional Western blotting analysis. Immunohistochemical analyses combined with in situ hybridization studies demonstrated that calbindin D-28K in the Purkinje cells of the cerebellum is independent of vitamin D. The antibodies described here will be important tools for studying the regulation of expression of calbindin D-28K and its biological function in the brain and in the PNS. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Calbindin D-28K Kägi, Urs verfasserin aut Heizmann, Claus W. verfasserin aut Vogel, Brigitte oth Séquier, Jean-Marc oth Haas, Werner oth Hunziker, Willi oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 54(1990), 6, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:54 year:1990 number:6 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1990.tb04879.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 54 1990 6 0 |
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10.1111/j.1471-4159.1990.tb04879.x doi (DE-627)NLEJ240269055 DE-627 ger DE-627 rakwb Pinol, M. Rosa verfasserin aut Poly- and Monoclonal Antibodies Against Recombinant Rat Brain Calbindin D-28K Were Produced to Map Its Selective Distribution in the Central Nervous System Oxford, UK Blackwell Publishing Ltd 1990 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Many processes in the CNS depend on calcium. The calcium signal is transduced into an intracellular response via Ca2+-binding proteins, including calbindin D-28K. In many laboratories, polyclonal antibodies against chicken in testinal calbindin D-28K have been used to study its localization in the brain (normal and degenerated) of various species, including humans, but some of these antisera cross-reacted with other proteins, including calretinin. We purified recombinant rat brain calbindin D-28K to raise antisera in rabbits and purified a recombinant rat–chicken calbindin D28K hybrid protein to immunize mice for the generation of monoclonal antibodies. These antisera were highly specific for calbindin D-28K, as demonstrated by two-dimensional Western blotting analysis. Immunohistochemical analyses combined with in situ hybridization studies demonstrated that calbindin D-28K in the Purkinje cells of the cerebellum is independent of vitamin D. The antibodies described here will be important tools for studying the regulation of expression of calbindin D-28K and its biological function in the brain and in the PNS. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Calbindin D-28K Kägi, Urs verfasserin aut Heizmann, Claus W. verfasserin aut Vogel, Brigitte oth Séquier, Jean-Marc oth Haas, Werner oth Hunziker, Willi oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 54(1990), 6, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:54 year:1990 number:6 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1990.tb04879.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 54 1990 6 0 |
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10.1111/j.1471-4159.1990.tb04879.x doi (DE-627)NLEJ240269055 DE-627 ger DE-627 rakwb Pinol, M. Rosa verfasserin aut Poly- and Monoclonal Antibodies Against Recombinant Rat Brain Calbindin D-28K Were Produced to Map Its Selective Distribution in the Central Nervous System Oxford, UK Blackwell Publishing Ltd 1990 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Many processes in the CNS depend on calcium. The calcium signal is transduced into an intracellular response via Ca2+-binding proteins, including calbindin D-28K. In many laboratories, polyclonal antibodies against chicken in testinal calbindin D-28K have been used to study its localization in the brain (normal and degenerated) of various species, including humans, but some of these antisera cross-reacted with other proteins, including calretinin. We purified recombinant rat brain calbindin D-28K to raise antisera in rabbits and purified a recombinant rat–chicken calbindin D28K hybrid protein to immunize mice for the generation of monoclonal antibodies. These antisera were highly specific for calbindin D-28K, as demonstrated by two-dimensional Western blotting analysis. Immunohistochemical analyses combined with in situ hybridization studies demonstrated that calbindin D-28K in the Purkinje cells of the cerebellum is independent of vitamin D. The antibodies described here will be important tools for studying the regulation of expression of calbindin D-28K and its biological function in the brain and in the PNS. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Calbindin D-28K Kägi, Urs verfasserin aut Heizmann, Claus W. verfasserin aut Vogel, Brigitte oth Séquier, Jean-Marc oth Haas, Werner oth Hunziker, Willi oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 54(1990), 6, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:54 year:1990 number:6 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1990.tb04879.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 54 1990 6 0 |
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10.1111/j.1471-4159.1990.tb04879.x doi (DE-627)NLEJ240269055 DE-627 ger DE-627 rakwb Pinol, M. Rosa verfasserin aut Poly- and Monoclonal Antibodies Against Recombinant Rat Brain Calbindin D-28K Were Produced to Map Its Selective Distribution in the Central Nervous System Oxford, UK Blackwell Publishing Ltd 1990 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Many processes in the CNS depend on calcium. The calcium signal is transduced into an intracellular response via Ca2+-binding proteins, including calbindin D-28K. In many laboratories, polyclonal antibodies against chicken in testinal calbindin D-28K have been used to study its localization in the brain (normal and degenerated) of various species, including humans, but some of these antisera cross-reacted with other proteins, including calretinin. We purified recombinant rat brain calbindin D-28K to raise antisera in rabbits and purified a recombinant rat–chicken calbindin D28K hybrid protein to immunize mice for the generation of monoclonal antibodies. These antisera were highly specific for calbindin D-28K, as demonstrated by two-dimensional Western blotting analysis. Immunohistochemical analyses combined with in situ hybridization studies demonstrated that calbindin D-28K in the Purkinje cells of the cerebellum is independent of vitamin D. The antibodies described here will be important tools for studying the regulation of expression of calbindin D-28K and its biological function in the brain and in the PNS. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Calbindin D-28K Kägi, Urs verfasserin aut Heizmann, Claus W. verfasserin aut Vogel, Brigitte oth Séquier, Jean-Marc oth Haas, Werner oth Hunziker, Willi oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 54(1990), 6, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:54 year:1990 number:6 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1990.tb04879.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 54 1990 6 0 |
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10.1111/j.1471-4159.1990.tb04879.x doi (DE-627)NLEJ240269055 DE-627 ger DE-627 rakwb Pinol, M. Rosa verfasserin aut Poly- and Monoclonal Antibodies Against Recombinant Rat Brain Calbindin D-28K Were Produced to Map Its Selective Distribution in the Central Nervous System Oxford, UK Blackwell Publishing Ltd 1990 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Many processes in the CNS depend on calcium. The calcium signal is transduced into an intracellular response via Ca2+-binding proteins, including calbindin D-28K. In many laboratories, polyclonal antibodies against chicken in testinal calbindin D-28K have been used to study its localization in the brain (normal and degenerated) of various species, including humans, but some of these antisera cross-reacted with other proteins, including calretinin. We purified recombinant rat brain calbindin D-28K to raise antisera in rabbits and purified a recombinant rat–chicken calbindin D28K hybrid protein to immunize mice for the generation of monoclonal antibodies. These antisera were highly specific for calbindin D-28K, as demonstrated by two-dimensional Western blotting analysis. Immunohistochemical analyses combined with in situ hybridization studies demonstrated that calbindin D-28K in the Purkinje cells of the cerebellum is independent of vitamin D. The antibodies described here will be important tools for studying the regulation of expression of calbindin D-28K and its biological function in the brain and in the PNS. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Calbindin D-28K Kägi, Urs verfasserin aut Heizmann, Claus W. verfasserin aut Vogel, Brigitte oth Séquier, Jean-Marc oth Haas, Werner oth Hunziker, Willi oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 54(1990), 6, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:54 year:1990 number:6 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1990.tb04879.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 54 1990 6 0 |
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Poly- and Monoclonal Antibodies Against Recombinant Rat Brain Calbindin D-28K Were Produced to Map Its Selective Distribution in the Central Nervous System |
abstract |
Abstract: Many processes in the CNS depend on calcium. The calcium signal is transduced into an intracellular response via Ca2+-binding proteins, including calbindin D-28K. In many laboratories, polyclonal antibodies against chicken in testinal calbindin D-28K have been used to study its localization in the brain (normal and degenerated) of various species, including humans, but some of these antisera cross-reacted with other proteins, including calretinin. We purified recombinant rat brain calbindin D-28K to raise antisera in rabbits and purified a recombinant rat–chicken calbindin D28K hybrid protein to immunize mice for the generation of monoclonal antibodies. These antisera were highly specific for calbindin D-28K, as demonstrated by two-dimensional Western blotting analysis. Immunohistochemical analyses combined with in situ hybridization studies demonstrated that calbindin D-28K in the Purkinje cells of the cerebellum is independent of vitamin D. The antibodies described here will be important tools for studying the regulation of expression of calbindin D-28K and its biological function in the brain and in the PNS. |
abstractGer |
Abstract: Many processes in the CNS depend on calcium. The calcium signal is transduced into an intracellular response via Ca2+-binding proteins, including calbindin D-28K. In many laboratories, polyclonal antibodies against chicken in testinal calbindin D-28K have been used to study its localization in the brain (normal and degenerated) of various species, including humans, but some of these antisera cross-reacted with other proteins, including calretinin. We purified recombinant rat brain calbindin D-28K to raise antisera in rabbits and purified a recombinant rat–chicken calbindin D28K hybrid protein to immunize mice for the generation of monoclonal antibodies. These antisera were highly specific for calbindin D-28K, as demonstrated by two-dimensional Western blotting analysis. Immunohistochemical analyses combined with in situ hybridization studies demonstrated that calbindin D-28K in the Purkinje cells of the cerebellum is independent of vitamin D. The antibodies described here will be important tools for studying the regulation of expression of calbindin D-28K and its biological function in the brain and in the PNS. |
abstract_unstemmed |
Abstract: Many processes in the CNS depend on calcium. The calcium signal is transduced into an intracellular response via Ca2+-binding proteins, including calbindin D-28K. In many laboratories, polyclonal antibodies against chicken in testinal calbindin D-28K have been used to study its localization in the brain (normal and degenerated) of various species, including humans, but some of these antisera cross-reacted with other proteins, including calretinin. We purified recombinant rat brain calbindin D-28K to raise antisera in rabbits and purified a recombinant rat–chicken calbindin D28K hybrid protein to immunize mice for the generation of monoclonal antibodies. These antisera were highly specific for calbindin D-28K, as demonstrated by two-dimensional Western blotting analysis. Immunohistochemical analyses combined with in situ hybridization studies demonstrated that calbindin D-28K in the Purkinje cells of the cerebellum is independent of vitamin D. The antibodies described here will be important tools for studying the regulation of expression of calbindin D-28K and its biological function in the brain and in the PNS. |
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Poly- and Monoclonal Antibodies Against Recombinant Rat Brain Calbindin D-28K Were Produced to Map Its Selective Distribution in the Central Nervous System |
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http://dx.doi.org/10.1111/j.1471-4159.1990.tb04879.x |
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Kägi, Urs Heizmann, Claus W. Vogel, Brigitte Séquier, Jean-Marc Haas, Werner Hunziker, Willi |
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10.1111/j.1471-4159.1990.tb04879.x |
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