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Merck
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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號碼:
分類程式碼代碼:
12352202
NACRES:
NA.61

生物源

bovine eye (lens)

品質等級

化驗

≥70% (biuret)

形狀

lyophilized powder

技術

cell culture | mammalian: suitable

UniProt登錄號

儲存溫度

−20°C

基因資訊

應用

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。

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)


历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Delay of diabetic cataract in rats by the antiglycating potential of cumin through modulation of α-crystallin chaperone activity.
Kumar PA., et al.
The Journal of Nutrition, 20, 553-562 (2009)
Raju Timsina et al.
Experimental eye research, 206, 108544-108544 (2021-03-22)
The concentration of α-crystallin decreases in the eye lens cytoplasm, with a corresponding increase in membrane-bound α-crystallin during cataract formation. The eye lens's fiber cell plasma membrane consists of extremely high cholesterol (Chol) content, forming cholesterol bilayer domains (CBDs) within
Pasupulati Anil Kumar et al.
IUBMB life, 61(5), 485-495 (2009-04-25)
Cataract, loss of eye lens transparency, is the leading cause of blindness worldwide. alpha-Crystallin, initially known as one of the major structural proteins of the eye lens, is composed of two homologous subunits alphaA- and alphaB-crystallins. It is convincingly established
Raju Timsina et al.
Current eye research, 47(6), 843-853 (2022-02-19)
This research aims to probe the interaction of α-crystallin with a model of human, porcine, and mouse lens-lipid membranes. Cholesterol/model of human lens-lipid (Chol/MHLL), cholesterol/model of porcine lens-lipid (Chol/MPLL), and cholesterol/model of mouse lens-lipid (Chol/MMLL) membranes with 0-60 mol% Chol were
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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