Analytical Data
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基因名
NEIL3
- Application
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别名
NEIL3；Endonuclease 8-like 3
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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
Q8TAT5
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表达区间
2-605aa
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氨基酸序列
VEGPGCTLN GEKIRARVLP GQAVTGVRGS ALRSLQGRAL RLAASTVVVS PQAAALNNDS SQNVLSLFNG YVYSGVETLG KELFMYFGPK ALRIHFGMKG FIMINPLEYK YKNGASPVLE VQLTKDLICF FDSSVELRNS MESQQRIRMM KELDVCSPEF SFLRAESEVK KQKGRMLGDV LMDQNVLPGV GNIIKNEALF DSGLHPAVKV CQLTDEQIHH LMKMIRDFSI LFYRCRKAGL ALSKHYKVYK RPNCGQCHCR ITVCRFGDNN RMTYFCPHCQ KENPQHVDIC KLPTRNTIIS WTSSRVDHVM DSVARKSEEH WTCVVCTLIN KPSSKACDAC LTSRPIDSVL KSEENSTVFS HLMKYPCNTF GKPHTEVKIN RKTAFGTTTL VLTDFSNKSS TLERKTKQNQ ILDEEFQNSP PASVCLNDIQ HPSKKTTNDI TQPSSKVNIS PTISSESKLF SPAHKKPKTA QYSSPELKSC NPGYSNSELQ INMTDGPRTL NPDSPRCSKH NRLCILRVVG KDGENKGRQF YACPLPREAQ CGFFEWADLS FPFCNHGKRS TMKTVLKIGP NNGKNFFVCP LGKEKQCNFF QWAENGPGIK IIPGC
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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
NEIL3 (Nei endonuclease VIII-like 3) is a DNA glycosylase that plays a crucial role in the base excision repair (BER) pathway, which is essential for maintaining genomic stability. This enzyme is responsible for recognizing and excising oxidized or damaged bases in DNA, particularly those caused by oxidative stress or environmental factors. As a member of the NEIL family, NEIL3 has garnered interest due to its unique recognition and repair mechanisms, which differ from those of other DNA glycosylases. Research has shown that NEIL3 is predominantly expressed in the heart and brain, suggesting a protective role against DNA damage in these vital tissues. Furthermore, studies have linked NEIL3 to various diseases, including cancer and neurodegenerative disorders, underscoring its significance in health and disease. Investigating the functional properties of NEIL3, including its substrate specificity, activity regulation, and interaction with other repair proteins, is essential for understanding its potential therapeutic implications. The ongoing research aims to elucidate the molecular mechanisms underlying NEIL3's actions, its contributions to cellular responses to DNA damage, and the potential for targeting this enzyme in novel treatment strategies for DNA damage-related diseases. Overall, NEIL3 represents a promising area of study in the field of molecular biology, with implications for cancer research, aging, and the development of targeted therapies.
