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Validated All-in-One™ qPCR Primer for CAST(NM_001042444.3) Search again
Powered by BiozBy default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
The protein encoded by this gene is an endogenous calpain (calcium-dependent cysteine protease) inhibitor. It consists of an N-terminal domain L and four repetitive calpain-inhibition domains (domains 1-4), and it is involved in the proteolysis of amyloid precursor protein. The calpain/calpastatin system is involved in numerous membrane fusion events, such as neural vesicle exocytosis and platelet and red-cell aggregation. The encoded protein is also thought to affect the expression levels of genes encoding structural or regulatory proteins. Several alternatively spliced transcript variants of this gene have been described, but the full-length natures of only some have been determined. [provided by RefSeq].
Gene References into function
- involved in the proteolysis of amyloid precursor protein, which is thought to be abnormal in patients with Alzheimer's disease
- Overexpression of calpastatin reduced muscle atrophy during 10 day unloading period. Overexpression completely prevented shift in myofibrillar myosin content from slow to fast isoforms, which normally occurs in muscle unloading.
- insights into how the calpain/calpastatin network is spatially and temporally regulated in cells binding to the extracellular matrix
- calpastatin and calpain-1 represent critical proximal elements in a cascade of pro-apoptotic events leading to Bax, mitochondria, and caspase-3 activation
- Calpastatin amino acid side chains at leucine-11 and isoleucine-18 interact with hydrophobic pockets in calpain, and each of these interactions is indispensable for effective inhibition of calpain.
- Overexpression of calpastatin in transgenic mice is associated with an increase in GLUT4 protein.
- A complete calpain-calpastatin system is expressed in the human oocyte and may play a role in the various calcium-mediated processes occurring during activation of human oocytes.
- CS(L) modulates Ca2+-channel activity through interacting with the calmodulin-binding site on the C-terminal tail of the Cav1.2 channel.
- The activity of calpain in human peripheral blood lymphocytes, was estimated by assessing the levels of limited proteolysis of calpastatin.
- Results suggest a regulation on the calpain-calpastatin expression response to muscle damaging eccentric exercise, but not concentric exercise.
- genetically determined IL-1alpha levels may modulate transcription of calpain and calpastatin
- NMR data of calapastin tripartite binding mode to capain induced by calcium were presented.
- performed a full NMR assignment of hCSD1 to characterize it in its solution state
- c-Myc regulates calpain activity through calpastatin; apoptosis induced by calpain inhibition is dependent on c-Myc, and calpastatin knockdown promotes transformation in c-Myc-negative cells
- Proof of concept that the calpastatin-based reagents may be useful to selectively detect the active conformation of calpain.
- Role of the calpain-calpastatin system in the density-dependent growth arrest.