Analytical Data
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基因名
LRRC8A
- Application
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别名
AGM5; FLJ10337; FLJ41617; KIAA1437; Leucine rich repeat containing 8 family member A; Leucine rich repeat containing protein 8A; Leucine-rich repeat-containing protein 8A; LRC8A_HUMAN; LRRC8; Lrrc8a
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q8IWT6
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表达区间
711-810aa
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氨基酸序列
QNLAITANRIETLPPELFQCRKLRALHLGNNVLQSLPSRVGELTNLTQIELRGNRLECLPVELGECPLLKRSGLVVEEDLFNTLPPEVKERLWRADKEQA
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分子量
36.74 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
LRRC8A (Leucine-Rich Repeat Containing 8 A) is a crucial protein that functions as a component of the volume-regulated anion channel (VRAC), playing a significant role in maintaining cellular homeostasis and mediating osmoregulation. Its involvement in various physiological processes, including cell volume regulation, apoptosis, and the immune response, has drawn considerable research interest. Mutations and dysfunctions in LRRC8A have been linked to a number of pathological conditions, including neurological disorders and cancer, emphasizing the need for a deeper understanding of its functional mechanisms. Recent studies have focused on the structural and functional characterization of LRRC8A, exploring its oligomeric nature and regulatory pathways that modulate its activity. Additionally, recombinant LRRC8A proteins are being utilized to elucidate the biophysical properties of the channel and to develop pharmacological tools to target this channel in various diseases. Overall, the thorough investigation of LRRC8A as a model for studying ion channel biology is essential for advancing therapeutic strategies that exploit its potential role in health and disease.
