Analytical Data
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基因名
LYG1
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简介
LYG1, a classical secretory protein, belongs to the lysozyme G family. LYG1 inhibits tumor growth by promoting the activation, proliferation, and function of CD4+ T cells. LYG1 also has a hydrolase activity and is involved in the degradation of peptidoglycans from bacterial membranes[1][2]. LYG1 Protein, Human (sf9, His) is the recombinant human-derived LYG1 protein, expressed by Sf9 insect cells , with C-His labeled tag.
- Application
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别名
Lysozyme g-like protein 1; LYG1
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种属
Human
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表达系统
Baculovirus
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标签
C-His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q8N1E2
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表达区间
S20-F194
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蛋白长度
Full Length of Mature Protein
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分子量
22 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
LYG1, also known as Lysozyme G1, is a protein that has garnered increasing attention for its potential applications in biotechnology and medicine. It plays a crucial role in various biological processes, particularly in the innate immune response, where it exhibits antimicrobial properties. The significance of LYG1 lies in its ability to hydrolyze bacterial cell walls, thus contributing to pathogen clearance. Research into LYG1 has expanded in recent years, focusing on its structure, function, and mechanism of action. Scientists have been exploring methods for recombinant expression of LYG1 to produce large quantities of the protein for further studies and potential therapeutic uses. By utilizing recombinant DNA technology, researchers aim to enhance the yield and activity of LYG1, allowing for detailed investigations into its enzyme kinetics and interactions with other biomolecules. Additionally, understanding the molecular basis of LYG1's antimicrobial activity could pave the way for developing new anti-infective agents, especially in the face of rising antibiotic resistance. Overall, the study of LYG1 not only contributes to our understanding of immune defense mechanisms but also opens up opportunities for innovative approaches in drug development and therapeutic interventions against infectious diseases.
