日本同仁化学Hampton蛋白结晶试剂盒NDSB-256/HR2-705- DOJINDO

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Products > Optimize Reagents > Optimize – Solubilizing Agents (NDSB) > NDSB-256

NDSB-256

Hampton蛋白结晶试剂盒NDSB-256/HR2-705

CAT NO

HR2-705

NAME

NDSB-256

DESCRIPTION

5 grams

PRICE

$57.00

支持材料

Hampton蛋白结晶试剂盒NDSB-256/HR2-705 HR2-705 NDSB-256 User GuideHampton蛋白结晶试剂盒NDSB-256/HR2-705 HR2-705 NDSB-256 SDS

应用

  • Crystallization grade NDSB-256 for formulating screens or for optimization
  • 结晶级 NDSB-256 用于配制筛选或优化

特征

  • Efficiently solubilizes proteins at non-denaturing concentrations
  • Useful in preventing protein aggregation
  • Non detergent sulfobetaines (NDSB) are used for protein folding, renaturation and crystallization
  • Protein specific additive for solubility and stability
  • 在非变性浓度下有效溶解蛋白质
    可用于防止蛋白质聚集
    非洗涤剂磺基甜菜碱 (NDSB) 用于蛋白质折叠、复性和结晶
    用于溶解性和稳定性的蛋白质特定添加剂

描述

The NDSB are a group of zwitterionic compounds that can reduce aggregation and aid in refolding proteins found in inclusion bodies and bacterial expression systems.

Non detergent sulfobetaines have a sulfobetaine hydrophilic group and a short hydrophobic group that cannot aggregate to form micelles, therefore NDSB’s are not considered detergents. NDSB increase the extraction yield (up to 30%) of membrane, nuclear and cyto-skeletal associated proteins. The short hydrophobic groups combined with the charge neutralization of the sulfobetaine group results in higher yields of membrane proteins. NDSB have been used in refolding and renaturation of chemically and thermally denatured proteins.

NDSB 是一组两性离子化合物，可以减少聚集并帮助重新折叠包含体和细菌表达系统中发现的蛋白质。

非洗涤剂磺基甜菜碱有一个磺基甜菜碱亲水基团和一个不能聚集形成胶束的短疏水基团，因此 NDSB 不被视为洗涤剂。 NDSB 可提高膜、核和细胞骨架相关蛋白的提取率（高达 30%）。 短疏水基团与磺基甜菜碱基团的电荷中和相结合，导致膜蛋白产量更高。 NDSB 已用于化学和热变性蛋白质的重折叠和复性。

Typical useful NDSB concentration in protein sample is 0.5-1.0 M.

NDSB-256
Synonyms: Dimethylbenzylammonium propane sulfonate
C12H19NO3S
Mr 257.37
Purity: ≥99% by TLC
Hygroscopic
Store at room temperature (+20 degrees Celsius)

HR2-705

参考

1. Vuillard, L., et al, J. Biochem., 305, 337 (1995).

2. A nondetergent sulfobetaine prevents protein aggregation in microcalorimetric studies. Collins et al, Notes & Tips / Anal. Biochem. 352 (2006) 299-301.