Analytical Data
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基因名
DNALI1
- Application
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别名
DNALI1;Axonemal dynein light intermediate polypeptide 1
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种属
Human
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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
O14645
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表达区间
1-280aa
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氨基酸序列
MGSSHHHHHH SSGLVPRGSH MGSMVTANKA HTGQGSCWVA TLASAMIPPA DSLLKYDTPV LVSRNTEKRS PKARLLKVSP QQPGPSGSAP QPPKTKLPST PCVPDPTKQA EEILNAILPP REWVEDTQLW IQQVSSTPST RMDVVHLQEQ LDLKLQQRQA RETGICPVRR ELYSQCFDEL IREVTINCAE RGLLLLRVRD EIRMTIAAYQ TLYESSVAFG MRKALQAEQG KSDMERKIAE LETEKRDLER QVNEQKAKCE ATEKRESERR QVEEKKHNEE IQFLKRTNQQ LKAQLEGIIA PKK
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分子量
34 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
DNALI1 (Dynein, Axonemal, Light Intermediate Chain 1) is a protein that plays a crucial role in the motility of cilia and flagella, which are essential for various biological processes, including respiratory function and reproductive health. Research on DNALI1 has garnered significant interest due to its implications in ciliopathies, a group of disorders arising from dysfunction in cilia. Given that these disorders can lead to severe clinical manifestations affecting multiple organ systems, understanding the structure and function of DNALI1 is vital. Recent studies have focused on the recombinant expression of DNALI1 to investigate its biochemical properties and interactions with other dynein complex components. Techniques such as site-directed mutagenesis and protein purification have been utilized to create functional assays that elucidate the mechanistic role of DNALI1 in dynein-driven motility. Furthermore, characterizing the protein's dynamics and its influence on ciliary assembly may help identify therapeutic targets for treating related disorders. As such, the ongoing research on DNALI1 not only enhances our understanding of its fundamental biological roles but also potentially opens new avenues for clinical applications in regenerative medicine and gene therapy for ciliopathies.
