Analytical Data
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基因名
ZNF397
- Application
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别名
ZNF397; ZNF47; ZSCAN15Zinc finger Protein 397; Zinc finger and SCAN domain-containing Protein 15; Zinc finger Protein 47
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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
Q8NF99
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表达区间
1-534 aa
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氨基酸序列
MAVESGVIST LIPQDPPEQE LILVKVEDNF SWDEKFKQNG STQSCQELFR QQFRKFCYQE TPGPREALSR LQELCYQWLM PELHTKEQIL ELLVLEQFLS ILPEELQIWV QQHNPESGEE AVTLLEDLER EFDDPGQQVP ASPQGPAVPW KDLTCLRASQ ESTDIHLQPL KTQLKSWKPC LSPKSDCENS ETATKEGISE EKSQGLPQEP SFRGISEHES NLVWKQGSAT GEKLRSPSQG GSFSQVIFTN KSLGKRDLYD EAERCLILTT DSIMCQKVPP EERPYRCDVC GHSFKQHSSL TQHQRIHTGE KPYKCNQCGK AFSLRSYLII HQRIHSGEKA YECSECGKAF NQSSALIRHR KIHTGEKACK CNECGKAFSQ SSYLIIHQRI HTGEKPYECN ECGKTFSQSS KLIRHQRIHT GERPYECNEC GKAFRQSSEL ITHQRIHSGE KPYECSECGK AFSLSSNLIR HQRIHSGEEP YQCNECGKTF KRSSALVQHQ RIHSGDEAYI CNECGKAFRH RSVLMRHQRV HTIK
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分子量
61.1 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
ZNF397, a member of the zinc finger protein family, has garnered attention in recent years due to its potential roles in various biological processes, including gene regulation and chromatin remodeling. Zinc finger proteins are characterized by their ability to bind DNA, RNA, and other proteins, thereby influencing transcriptional activity and cellular functions. Specifically, ZNF397 has been implicated in modulating gene expression associated with cell differentiation, proliferation, and apoptosis. Research has suggested that alterations in ZNF397 expression could be linked to several diseases, including cancer, emphasizing the importance of understanding its functional mechanisms. The production of recombinant ZNF397 protein enables researchers to investigate its structure, binding properties, and functional interactions in vitro, providing insights into how this protein contributes to cellular processes. Additionally, studying the recombinant protein can help elucidate the pathways through which ZNF397 exerts its effects, potentially identifying novel therapeutic targets for diseases where ZNF397 activity is disrupted. Given its significant biological implications, further exploration of ZNF397 through recombinant techniques is essential for advancing our understanding of its role in health and disease.
