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Key Documents

E6527

Sigma-Aldrich

可溶性弹性蛋白 来源于牛颈部韧带

salt-free, lyophilized powder

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About This Item

CAS号:
EC號碼:
MDL號碼:
分類程式碼代碼:
12352202
NACRES:
NA.61

生物源

bovine neck ligament

品質等級

形狀

salt-free, lyophilized powder

技術

UV/Vis spectroscopy: suitable

UniProt登錄號

儲存溫度

2-8°C

InChI

1S/C27H48N6O6/c1-9-17(6)23(32-24(36)19(13-15(2)3)30-18(7)34)26(38)29-14-21(35)31-22(16(4)5)27(39)33-12-10-11-20(33)25(37)28-8/h15-17,19-20,22-23H,9-14H2,1-8H3,(H,28,37)(H,29,38)(H,30,34)(H,31,35)(H,32,36)/t17-,19-,20-,22-,23-/m0/s1

InChI 密鑰

DPUYCSDGMSDKKV-MKBYFEBXSA-N

基因資訊

cow ... ELN(280781)

一般說明

采用 Partrige 等的方法制备水溶性粉末。

應用

弹性蛋白是一种结构蛋白,已用于研究慢性阻塞性肺疾病(COPD)。它可以用来研究为什么COPD患者缺乏这些蛋白的修复。
由于其增溶的几种策略,目前发现高度稳定且具有血液相容性的蛋白质可用于构建生物材料。

生化/生理作用

负责许多组织弹性的蛋白质。它在血管中尤其重要,因为它占干组织重量的 50%。

注意

在 pH 5.0 和 37°C 条件下,形成凝聚层

適合性

如 Keller 和 Mandi 所述,适用于测定弹性蛋白溶解活性。

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves, type N95 (US)


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A novel fluorescence polarization assay based on the natural fluorophore epicocconone has been developed. This assay allows the rapid and accurate determination of enzyme kinetic parameters as well as inhibition constants through the measurement of fluorescence anisotropy on the actual
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Respiratory research, 9, 41-41 (2008-05-20)
COPD is characterised by loss of alveolar elastic fibers and by lack of effective repair. Elastic fibers are assembled at cell surfaces by elastin binding protein (EBP), a molecular chaperone whose function can be reversibility inhibited by chondroitin sulphate of
Pro-inflammatory phenotype of COPD fibroblasts not compatible with repair in COPD lung.
Zhang J., et al.
Journal of Cellular and Molecular Medicine (2011)
Zhongyuan Sun et al.
Journal of the American Chemical Society, 135(9), 3675-3679 (2013-02-07)
The chimeric proteins, silk-elastin-like protein polymers (SELPs), consist of repeating units of silk and elastin to retain the mechanical strength of silk, while incorporating the dynamic environmental sensitivity of elastin. A retinal-modified SELP was prepared, modified, and studied for photodynamic
A Panagopoulou et al.
Biochimica et biophysica acta, 1834(6), 977-988 (2013-03-27)
Dynamics of uncrystallized water and protein was studied in hydrated pellets of the fibrous protein elastin in a wide hydration range (0 to 23wt.%), by differential scanning calorimetry (DSC), thermally stimulated depolarization current technique (TSDC) and dielectric relaxation spectroscopy (DRS).

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