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Human Calsequestrin-1 / CASQ1 Protein

CASQ1, CASQ

Catalog Number P13805-HNAE
Organism Species Human
Host E. coli
Synonyms CASQ1, CASQ
Molecular Weight The recombinant human CASQ1 consists of 363 amino acids and predicts a molecular mass of 41.8 KDa. It migrates as an approximately 52 KDa band in SDS-PAGE under reducing conditions.
predicted N Met
SDS-PAGE
Purity > 90 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the mature form of human CASQ1 (P31415) (Gln35-Asp396) was expressed with a N-terminal Met.
Bio-activity
Research Area Neuroscience |Cell Type Marker in Neurodevelopment |Neuronal Cell Markers |Synapse & Synaptic Proteins |Calcium Signaling |Calcium Binding Proteins |
Formulation Lyophilized from sterile 50mM Tris, 10% glycerol, pH 7.5.
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Calsequestrin-1 is an isoform of calsequestrin. Calsequestrin is a calcium-binding protein of the sarcoplasmic reticulum. It helps hold calcium in the cisterna of the sarcoplasmic reticulum after a muscle contraction, even though the concentration of calcium in the sarcoplasmic reticulum is much higher than in the cytosol. Two forms of calsequestrin have been identified: Calsequestrin-2 and Calsequestrin-1. Calsequestrin-1 is found in fast skeletal muscle. The release of calsequestrin-bound calcium (through a calcium release channel) triggers muscle contraction. The active protein is not highly structured, more than 50% of it adopting a random coil conformation. When calcium binds there is a structural change whereby the alpha-helical content of the protein increases from 3 to 11%. Both forms of calsequestrin are phosphorylated by casein kinase 2, but the cardiac form is phosphorylated more rapidly and to a higher degree. Calsequestrin-1 is also secreted in the gut where it deprives bacteria of calcium ions.
Reference
  • Slupsky JR, et al. (1987) Characterization of cardiac calsequestrin. Biochemistry. 26(20): 6539-44.
  • Cala SE, et al. (1991) Phosphorylation of cardiac and skeletal muscle calsequestrin isoforms by casein kinase II. Demonstration of a cluster of unique rapidly phosphorylated sites in cardiac calsequestrin. J Biol Chem. 266(1):391-8.
  • Wang S, et al. (1998) Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum. Nat Struct Biol. 5(6):476-83.