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CHAPS, >98%, Reagent Grade, 5G | BioShop CHA003

Fiyat Sorunuz

High-purity non-denaturating detergent for protein isolation and membrane protein analysis

  • Non-denaturing detergent preserving native protein structure
  • High purity grade (>98%) for sensitive applications
  • Suitable for protein isolation, purification, and electrophoresis
  • Ideal for cell membrane protein analysis
  • Stable at -20°C storage conditions

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2-3 Gün

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BioShop CHA003 CHAPS is a detergent widely used in protein isolation and purification workflows. Its non-denaturing properties enable dissolution of proteins without structural degradation, essential for biochemical research applications. With high purity (>98%), it delivers reliable results in sensitive biotechnology experiments. Particularly preferred for cell membrane protein studies and proteomics applications.

Technical Specifications

Molecular Formula C32H58N2O7S
Molecular Weight 614.89 g/mol
CAS Number 75621-03-3
Package Size 5G
Purity >98%
Grade Reagent Grade
Storage Temperature -20°C

Applications

  • Protein isolation and purification
  • Cell membrane protein analysis
  • Native PAGE and electrophoresis studies
  • Proteomics research
  • Membrane protein characterization

Frequently Asked Questions

What is the primary function of CHAPS in biochemical research?
CHAPS is a non-denaturing detergent that solubilizes cell membranes while preserving native protein structure and biological activity, making it ideal for isolating and analyzing membrane proteins.
Why is CHAPS purity important for research applications?
High purity (>98%) ensures minimal contamination that could interfere with sensitive biochemical assays, electrophoresis, and protein analysis, providing reliable and reproducible results.
What is the recommended storage condition?
Store at -20°C to maintain product stability and purity over extended periods.
Is CHAPS suitable for native protein studies?
Yes, its non-denaturing properties make it ideal for native protein extraction and analysis, preserving quaternary and tertiary protein structures.