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Merck
CN
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主要文件

C4163

Sigma-Aldrich

α-晶体 来源于牛眼晶状体

lyophilized powder

别名:

alpha-Crystallin

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About This Item

CAS号:
MDL编号:
UNSPSC代码:
12352202
NACRES:
NA.61

生物来源

bovine eye (lens)

质量水平

方案

≥70% (biuret)

表单

lyophilized powder

技术

cell culture | mammalian: suitable

UniProt登记号

储存温度

−20°C

基因信息

应用

α-晶状体蛋白是一种晶状体蛋白,含有两个同源亚基:αA- 和 αB-晶状体蛋白。α-晶状体蛋白表现出类似伴侣的活性,并在保持镜片透明度方面发挥重要作用。已经注意到,在大鼠的糖尿病条件下,α-晶状体蛋白的伴侣活性下降。研究表明,膳食抗氧化剂姜黄素可以防止这种分子伴侣活性的丢失。

生化/生理作用

α-晶状体蛋白是一种小型热休克蛋白,具有类似伴侣的活性,可防止蛋白质在体外聚集。α-晶状体蛋白基因中的点突变被认为是导致遗传性白内障发展的原因。

储存分类代码

11 - Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)


历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Binding of Alpha-Crystallin to Cortical and Nuclear Lens Lipid Membranes Derived from a Single Lens.
Timsina, et al.
International Journal of Molecular Sciences, 23 (2023)
Laxman Mainali et al.
Current eye research, 46(2), 185-194 (2020-06-23)
Purpose/Aim: The amount of membrane-bound α-crystallin increases significantly with age and cataract formation, accompanied by a corresponding decline in the level of α-crystallin in the lens cytoplasm. The purpose of this research is to evaluate the binding affinity of α-crystallin
Axel Leppert et al.
Protein science : a publication of the Protein Society, 31(8), e4378-e4378 (2022-07-29)
Molecular chaperones are essential to maintain proteostasis. While the functions of intracellular molecular chaperones that oversee protein synthesis, folding and aggregation, are established, those specialized to work in the extracellular environment are less understood. Extracellular proteins reside in a considerably
Raju Timsina et al.
Experimental eye research, 202, 108337-108337 (2020-11-01)
It is well-studied that the significant factor in cataract formation is the association of α-crystallin, a major eye lens protein, with the fiber cell plasma membrane of the eye lens. The fiber cell plasma membrane of the eye lens consists
Jakob Bunkenborg et al.
Proteomics, 16(4), 545-553 (2015-12-09)
Proteomic identifications hinge on the measurement of both parent and fragment masses and matching these to amino acid sequences via database search engines. The correctness of the identifications is assessed by statistical means. Here we present an experimental approach to

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