Analytical Data
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基因名
hph
- Application
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别名
hph；Prolyl hydroxylase EGLN3
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种属
E.coli
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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
P00557
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表达区间
1-341aa
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氨基酸序列
MKKPELTATSVEKFLIEKFDSVSDLMQLSEGEESRAFSFDVGGRGYVLRVNSCADGFYKDRYVYRHFASAALPIPEVLDIGEFSESLTYCISRRAQGVTLQDLPETELPAVLQPVAEAMDAIAAADLSQTSGFGPFGPQGIGQYTTWRDFICAIADPHVYHWQTVMDDTVSASVAQALDELMLWAEDCPEVRHLVHADFGSNNVLTDNGRITAVIDWSEAMFGDSQYEVANIFFWRPWLACMEQQTRYFERRHPELAGSPRLRAYMLRIGLDQLYQSLVDGNFDDAAWAQGRCDAIVRSGAGTVGRTQIARRSAAVWTDGCVEVLADSGNRRPSTRPRAKE
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分子量
54.0 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 study of Hph recombinant proteins has gained significant attention in recent years due to their potential applications in various biotechnological and medical fields. Hph, or hapten-protein conjugates, are molecular structures that combine a small hapten with a carrier protein, often leading to enhanced immune responses in vaccination and diagnostics. This research is particularly important for developing effective vaccines against pathogens, as well as for creating targeted therapies for diseases, particularly cancers. The challenge in Hph recombinant protein research lies in the need for precise engineering to ensure that the immunogenic properties are optimized while minimizing adverse effects. Advances in recombinant DNA technology and protein expression systems have facilitated the production of Hph proteins with high purity and bioactivity, making it possible to study their mechanisms of action in detail. Furthermore, the ability to customize haptens and carrier proteins allows for the exploration of novel formulations that can better elicit desired immune responses. Ongoing research continues to unveil the complex interactions between Hph proteins and the immune system, with the hope of translating findings into practical applications that can improve human health outcomes.
