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Results for "

zwitterionic structure

" in MedChemExpress (MCE) Product Catalog:

4

Inhibitors & Agonists

2

Biochemical Assay Reagents

1

Natural
Products

Cat. No. Product Name Target Research Areas Chemical Structure
  • HY-15435
    CHAPS
    4 Publications Verification

    Exosomes Biochemical Assay Reagents Others
    CHAPS is a cholic acid-derived, sulfobetaine-type zwitterionic detergent and micelle-forming agent. CHAPS exhibits properties of weak cationic or nonionic surfactants in different solution systems, undergoes micellization, and forms small, loose hydrophilic aggregates that are temperature-dependent. CHAPS stabilizes mononucleosomes under different ionic strengths, reduces nucleosome sequence specificity, promotes sliding of histone cores along DNA, solubilizes Tamm-Horsfall protein to reduce its interference with urinary exosome isolation, and maintains vesicle structure and the activity of related proteins at the same time. CHAPS is used to recover native folded fusion proteins, enhance the binding capacity of GST fusion proteins, and restore GST enzyme activity. However, CHAPS cannot refold proteins denatured by urea, guanidine hydrochloride or heat, nor can it construct the structure of intrinsically disordered proteins. CHAPS is commonly used in research on the separation and purification of membrane proteins .
    CHAPS
  • HY-126377

    Biochemical Assay Reagents Others
    Sulfobetaine 10, is a zwitterionic surfactant commonly used in biochemistry and biophysics. It is commonly used to dissolve membrane proteins and other hydrophobic molecules in aqueous solutions. Sulfobetaine 10 has both positively and negatively charged groups in its structure, which allows it to maintain a neutral charge in solution and reduces its tendency to denature proteins. It is considered a mild, non-denaturing surfactant and is widely used in protein research.
    Sulfobetaine 10
  • HY-15435A
    CHAPS hydrate
    4 Publications Verification

    Biochemical Assay Reagents Exosomes Others
    CHAPS hydrate is a cholic acid-derived, sulfobetaine-type zwitterionic detergent and micelle-forming agent. CHAPS hydrate exhibits properties of weak cationic or nonionic surfactants in different solution systems, undergoes micellization, and forms small, loose hydrophilic aggregates that are temperature-dependent. CHAPS hydrate stabilizes mononucleosomes under different ionic strengths, reduces nucleosome sequence specificity, promotes sliding of histone cores along DNA, solubilizes Tamm‑Horsfall protein to reduce its interference with urinary exosome isolation, and maintains vesicle structure and the activity of related proteins at the same time. CHAPS hydrate is used to recover native folded fusion proteins, enhance the binding capacity of GST fusion proteins, and restore GST enzyme activity. However, CHAPS hydrate cannot refold proteins denatured by urea, guanidine hydrochloride or heat, nor can it construct the structure of intrinsically disordered proteins. CHAPS hydrate is commonly used in research on the separation and purification of membrane proteins .
    CHAPS hydrate
  • HY-W012161

    L-Alanyl-L-phenylalanine; H-Ala-Phe-OH

    Endogenous Metabolite Drug Intermediate Others
    Alanylphenylalanine (L-Alanyl-L-phenylalanine) is a dipeptide. Alanylphenylalanine forms a mononuclear Au (III) complex through bidentate coordination via its carboxyl oxygen atom and deprotonated amide nitrogen atom .
    Alanylphenylalanine

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