Analytical Data
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基因名
ZNF398
- Application
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别名
ZNF398; KIAA1339; ZER6; Zinc finger Protein 398; Zinc finger DNA-binding Protein p52/p71
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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
Q8TD17
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表达区间
1-642 aa
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氨基酸序列
MAEAAPAPTSEWDSECLTSLQPLPLPTPPAANEAHLQTAAISLWTVVAAVQAIERKVEIH SRRLLHLEGRTGTAEKKLASCEKTVTELGNQLEGKWAVLGTLLQEYGLLQRRLENLENLL RNRNFWILRLPPGIKGDIPKVPVAFDDVSIYFSTPEWEKLEEWQKELYKNIMKGNYESLI SMDYAINQPDVLSQIQPEGEHNTEDQAGPEESEIPTDPSEEPGISTSDILSWIKQEEEPQ VGAPPESKESDVYKSTYADEELVIKAEGLARSSLCPEVPVPFSSPPAAAKDAFSDVAFKS QQSTSMTPFGRPATDLPEASEGQVTFTQLGSYPLPPPVGEQVFSCHHCGKNLSQDMLLTH QCSHATEHPLPCAQCPKHFTPQADLSSTSQDHASETPPTCPHCARTFTHPSRLTYHLRVH NSTERPFPCPDCPKRFADQARLTSHRRAHASERPFRCAQCGRSFSLKISLLLHQRGHAQE RPFSCPQCGIDFNGHSALIRHQMIHTGERPYPCTDCSKSFMRKEHLLNHRRLHTGERPFS CPHCGKSFIRKHHLMKHQRIHTGERPYPCSYCGRSFRYKQTLKDHLRSGHNGGCGGDSDP SGQPPNPPGPLITGLETSGLGVNTEGLETNQWYGEGSGGGVL
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分子量
71.3 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
ZNF398, a member of the zinc finger protein family, has garnered significant attention in recent years due to its potential role in gene regulation and cellular processes. Zinc finger proteins are characterized by their ability to bind DNA, RNA, or proteins, and they play crucial roles in transcriptional regulation, development, and cellular signaling. Research indicates that ZNF398 is involved in various biological functions, including cell growth, differentiation, and apoptosis. Furthermore, its dysregulation has been implicated in several diseases, including cancer, suggesting that understanding ZNF398's mechanisms could provide insights into therapeutic targets. The study of recombinant ZNF398 protein enables researchers to investigate its structure-function relationships, binding affinities, and interaction with other cellular molecules. By producing ZNF398 in an exogenous system, scientists can conduct biochemical assays, structural analyses, and functional assays to elucidate its role in cellular pathways. Additionally, understanding the post-translational modifications and interactions of ZNF398 could be pivotal in comprehending its involvement in disease pathology. Overall, the ongoing research on ZNF398 recombinant protein holds promise not only for advancing our understanding of zinc finger proteins in general but also for paving the way toward novel therapeutic strategies targeting related disorders.
