PA1-913 detects calsequestrin from canine, human, mouse, rat and sheep tissues. This antibody recognizes both cardiac and skeletal muscle calsequestrin.
PA1-913 has been successfully used in Western blot, immunofluorescence, immunocytochemistry, immunohistochemistry (paraffin) and immunoprecipitation procedures. By Western blot, this antibody detects an ~55 kDa protein representing calsequestrin from canine cardiac extract. Additional bands at 97 kDa may be observed and have been reported to be calsequestrin-like proteins.
PA1-913 antigen is purified canine cardiac calsequestrin.
The sarcoplasmic reticulum (SR) is in part responsible for maintaining the level of intracellular calcium in cardiac and skeletal muscle by storing and releasing calcium. Several intralumenal SR calcium binding proteins have been identified, the most prominent of these is calsequestrin. Calsequestrin is a calcium binding protein known to sequester calcium accumulated in the sarcoplasmic reticulum of muscle cells during relaxation and is found discretely localized to the junctional and corbular (terminal cisternae) SR. Calsequestrin functions to localize calcium near the junctional face of the terminal cisternae from which calcium can be released into the cytosol via the ryanodine receptor. This protein is highly acidic and has a large capacity and moderate to low affinity for calcium. Two mammalian isoforms of calequestrin exist, a cardiac and a skeletal muscle isoform, which are the products of different genes and are 63% identical.
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Protein Aliases: Aspartactin; calmitin; Calmitine; calsequestrin 1 (fast-twitch, skeletal muscle); Calsequestrin, skeletal muscle isoform; Calsequestrin-1; Casq1; Csq; Laminin-binding protein
Gene Aliases: CASQ; CASQ1; CSQ; CSQ-1; CSQ1; PDIB1; sCSQ; VMCQA