Analytical Data
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基因名
CRYGD
- Application
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别名
Gamma-D-crystallin Gamma-crystallin 4
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种属
Human
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表达系统
E. coli
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标签
N- GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P07320
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表达区间
1-174aa
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分子量
47.6 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
CRYGD (Crystallin Gamma D) is a member of the crystallin family, primarily known for its role in maintaining transparency and refractive properties in the lens of the eye. Research into CRYGD has gained prominence due to its implications in lens development and the pathogenesis of cataracts, a leading cause of blindness worldwide. Mutations within the CRYGD gene can lead to structural malformations in the protein, disrupting its ability to function properly and contributing to lens opacification. Recent studies have focused on the recombinant expression of CRYGD to better understand its biochemical properties and the molecular mechanisms underlying its role in lens clarity. By producing CRYGD as a recombinant protein, researchers aim to investigate its interactions with other lens proteins, characterize its functional properties, and explore potential therapeutic strategies for cataract prevention and treatment. The study of recombinant CRYGD not only enhances our understanding of lens biology but may also pave the way for novel interventions in ocular disorders associated with crystallin dysfunction.
