Analytical Data
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基因名
ZA20D1
- Application
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别名
Zinc finger A20 domain containing Protein 1; Zinc finger A20 domain-containing Protein 1; Zinc finger Protein Cezanne
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q6GQQ9
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表达区间
1-427 aa
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氨基酸序列
MTLDMDAVLSDFVRSTGAEPGLARDLLEGKNWDVNAALSDFEQLRQVHAGNLPPSFSEGSGGSRTPEKGFSDREPTRPPRPILQRQDDIVQEKRLSRGISHASSSIVSLARSHVSSNGGGGGSNEHPLEMPICAFQLPDLTVYNEDFRSFIERDLIEQSMLVALEQAGRLNWWVSVDPTSQRLLPLATTGDGNCLLHAASLGMWGFHDRDLMLRKALYALMEKGVEKEALKRRWRWQQTQQNEESGLVYTEDEWQKEWNELIKLASSEPRMHLGTNGANCGGVESSEEPVYESLEEFHVFVLAHVLRRPIVVVADTMLRDSGGEAFAPIPFGGIYLPLEVPASQCHRSPLVLAYDQAHFSALVSMEQKENTKEQAVIPLTDSEYKLLPLHFAVDPGKGWEWGKDDSDNVRLASVILSLEVRLHLLHS
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分子量
74 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
The ZA20D1 recombinant protein is derived from specific genomic sequences encoded in the DNA of certain organisms, offering a unique opportunity for scientific investigation. Research into ZA20D1 has garnered attention due to its potential applications in biotechnology and medicine, particularly in the study of protein function, interaction, and expression. Initial studies have suggested that ZA20D1 may play a significant role in various biological pathways, yet its precise mechanism of action remains poorly understood. The recombinant approach allows for the large-scale production and purification of the ZA20D1 protein, enabling detailed biochemical and biophysical analyses. This research is critical for elucidating the structure-function relationship of ZA20D1, which may pave the way for innovative therapeutic strategies. As researchers continue to explore the implications of ZA20D1 in cellular processes, its relevance in drug development, disease treatment, and novel biotechnological applications becomes increasingly apparent. Understanding this protein could also facilitate advancements in synthetic biology, where engineered proteins can be designed for specific functions, addressing complex biological challenges. Overall, the study of ZA20D1 not only enriches our knowledge of protein dynamics but also holds promise for practical applications across multiple scientific fields.
