Analytical Data
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基因名
Luciferin 4
- Application
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种属
Luciola cruciata
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P13129
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表达区间
1-548aa
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氨基酸序列
MENMENDENIVVGPKPFYPIEEGSAGTQLRKYMERYAKLGAIAFTNAVTGVDYSYAEYLEKSCCLGKALQNYGLVVDGRIALCSENCEEFFIPVIAGLFIGVGVAPTNEIYTLRELVHSLGISKPTIVFSSKKGLDKVITVQKTVTTIKTIVILDSKVDYRGYQCLDTFIKRNTPPGFQASSFKTVEVDRKEQVALIMNSSGSTGLPKGVQLTHENTVTRFSHARDPIYGNQVSPGTAVLTVVPFHHGFGMFTTLGYLICGFRVVMLTKFDEETFLKTLQDYKCTSVILVPTLFAILNKSELLNKYDLSNLVEIASGGAPLSKEVGEAVARRFNLPGVRQGYGLTETTSAIIITPEGDDKPGASGKVVPLFKAKVIDLDTKKSLGPNRRGEVCVKGPMLMKGYVNNPEATKELIDEEGWLHTGDIGYYDEEKHFFIVDRLKSLIKYKGYQVPPAELESVLLQHPSIFDAGVAGVPDPVAGELPGAVVVLESGKNMTEKEVMDYVASQVSNAKRLRGGVRFVDEVPKGLTGKIDGRAIREILKKPVAKM
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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
Luciferin is a bioluminescent compound that plays a crucial role in the light-emitting reactions observed in various organisms, including fireflies and certain marine species. The study of luciferin and its related proteins, particularly luciferase enzymes, has garnered significant attention in biochemical and biotechnological research due to their potential applications in bioluminescent imaging, biosensors, and reporter gene assays. Recent advancements in molecular biology techniques have enabled the development of luciferin-based recombinant proteins that enhance the efficiency and brightness of luminescent signals. These recombinant proteins may also exhibit improved stability and reduced background noise compared to their natural counterparts. Furthermore, by engineering luciferin in conjunction with luciferase, researchers can explore innovative applications ranging from in vivo imaging in medical research to monitoring cellular processes in real-time. The ongoing research aims not only to understand the underlying mechanisms of bioluminescence but also to harness these proteins for practical applications in various fields, including diagnostics, environmental monitoring, and drug development, making the study of luciferin and its recombinant variants a promising avenue for future exploration.
