关键信息
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基因名
VPA
- 应用
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别名
VPA；INO1；Inositol-3-phosphate synthase 1
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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
Q9NPH2
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表达区间
1-558aa
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氨基酸序列
MEAAAQFFVESPDVVYGPEAIEAQYEYRTTRVSREGGVLKVHPTSTRFTFRTARQVPRLGVMLVGWGGNNGSTLTAAVLANRLRLSWPTRSGRKEANYYGSLTQAGTVSLGLDAEGQEVFVPFSAVLPMVAPNDLVFDGWDISSLNLAEAMRRAKVLDWGLQEQLWPHMEALRPRPSVYIPEFIAANQSARADNLIPGSRAQQLEQIRRDIRDFRSSAGLDKVIVLWTANTERFCEVIPGLNDTAENLLRTIELGLEVSPSTLFAVASILEGCAFLNGSPQNTLVPGALELAWQHRVFVGGDDFKSGQTKVKSVLVDFLIGSGLKTMSIVSYNHLGNNDGENLSAPLQFRSKEVSKSNVVDDMVQSNPVLYTPGEEPDHCVVIKYVPYVGDSKRALDEYTSELMLGGTNTLVLHNTCEDSLLAAPIMLDLALLTELCQRVSFCTDMDPEPQTFHPVLSLLSFLFKAPLVPPGSPVVNALFRQRSCIENILRACVGLPPQNHMLLEHKMERPGPSLKRVGPVAATYPMLNKKGPVPAATNGCTGDANGHLQEEPPMPTT
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分子量
61 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.
质检流程
相关产品
背景信息
VPA (Valproic Acid) is a well-known pharmaceutical compound widely used as an anticonvulsant and mood-stabilizing drug. Recent studies have highlighted its role in influencing protein folding and expression, making it a significant factor in the field of protein research. The study of VPA-recombinant proteins has gained attention due to VPA's ability to enhance the yield and solubility of proteins expressed in various systems, such as bacterial or mammalian cells. By modulating cellular stress responses and protein homeostasis, VPA can facilitate the correct folding of complex proteins, thereby improving their functional properties. Researchers are particularly interested in VPA's potential to assist in the production of therapeutic proteins and enzymes that require precise structural integrity for proper function. Additionally, its application in understanding protein misfolding diseases has opened new avenues for therapeutic intervention. Given the increasing demand for recombinant proteins in biopharmaceutical development, VPA's role as a molecular chaperone offers a promising strategy to optimize protein expression and purification processes. Hence, ongoing research into VPA's molecular mechanisms and its interactions with target proteins not only enhances our understanding of protein biology but also contributes to the advancement of biotechnological applications.
