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Merck
CN

C4163

α-晶体 来源于牛眼晶状体

lyophilized powder

别名:

alpha-Crystallin

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关于此项目

化学文摘社编号:
UNSPSC Code:
12352202
NACRES:
NA.61
MDL number:
Form:
lyophilized powder
Assay:
≥70% (biuret)
Biological source:
bovine eye (lens)
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biological source

bovine eye (lens)

assay

≥70% (biuret)

form

lyophilized powder

technique(s)

cell culture | mammalian: suitable

UniProt accession no.

storage temp.

−20°C

Quality Level

Gene Information

Application

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。

Biochem/physiol Actions

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。

存储类别

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

法规信息

监管及禁止进口产品
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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
P Anil Kumar et al.
Molecular vision, 11, 561-568 (2005-08-10)
A decline in the chaperone-like activity of eye lens alpha-crystallin in diabetic conditions has been reported. In this study, we investigated whether curcumin, a dietary antioxidant, can manipulate the chaperone-like activity of alpha-crystallin in diabetic rat lens. A group of
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
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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