GRADE & PURITYCarrier Free?Carrier-free — supplied without added carrier protein/stabilizer. Use when carriers (e.g. BSA) would interfere with conjugation or sensitive assays.≥90%(SDS-PAGE)expressed in E. coli; See COA
Carrier Free, ≥90%(SDS-PAGE), expressed in E. coli; See COA Carrier Free for sensitive chromatographic and analytical workflows requiring minimal baseline interference.
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Storage & shipping
Store at -20°C,Avoid repeated freezing and thawing Ships Ice chest + Ice pads Check lot-specific COA for exact specifications.
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Quality documents
SDS, COA, datasheet, and spec sheet available for download. Lot-specific COA accessible via lot number lookup.
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Literature proof
Cited in 0 peer-reviewed publications across chromatography, organic synthesis, and cross-coupling reactions.
Specifications
Product Name
Recombinant Human CASQ2 Protein
Grade
Carrier Free
Specifications & Purity
Carrier Free, ≥90%(SDS-PAGE), expressed in E. coli; See COA
Biochemical and Physiological Mechanisms
CASQ2 belongs to the calsequestrin family and is localized to the sarcoplasmic reticulum in cardiac and slow skeletal muscle cells. CASQ2 is a calcium binding protein that stores calcium for muscle function. The discharge of calcium bound to CASQ2 through
45.0 kDa, under reducing conditions; 45.0 & 90.0 kDa, under non-reducing conditions.
Molecule Type
Protein
Storage and Shipping
Concentration
expressed in E. coli; See COA
Storage
Store at -20°C,Avoid repeated freezing and thawing
Shipped In
Ice chest + Ice pads
Stability And Storage
Store at -20℃ long term (12 months). Upon receipt, it is recommended to aliquot. Avoid freeze/thaw cycle.
Images
Recombinant Human CASQ2 Protein (rp340391) - SDS-PAGE
3 μg/lane of Recombinant Human CASQ2 Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing the bands at 45.0 kDa under reducing conditions and 45.0 & 90.0 kDa under non-reducing conditions.
The observation of protein as both dimers and monomers under non-reducing (NR) conditions suggests that a portion of the protein forms dimers. This dimerization may be mediated by (or stabilized by) disulfide bonds (O14958).
Documentation
📋 Safety Data Sheet (SDS)
Comprehensive hazard, handling, storage, and regulatory compliance document.
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