Analytical Data
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Gene name
VPA
- Application
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Alternative Names
VPA；INO1；Inositol-3-phosphate synthase 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NPH2
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Expression Region
1-558aa
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AA Sequence
MEAAAQFFVESPDVVYGPEAIEAQYEYRTTRVSREGGVLKVHPTSTRFTFRTARQVPRLGVMLVGWGGNNGSTLTAAVLANRLRLSWPTRSGRKEANYYGSLTQAGTVSLGLDAEGQEVFVPFSAVLPMVAPNDLVFDGWDISSLNLAEAMRRAKVLDWGLQEQLWPHMEALRPRPSVYIPEFIAANQSARADNLIPGSRAQQLEQIRRDIRDFRSSAGLDKVIVLWTANTERFCEVIPGLNDTAENLLRTIELGLEVSPSTLFAVASILEGCAFLNGSPQNTLVPGALELAWQHRVFVGGDDFKSGQTKVKSVLVDFLIGSGLKTMSIVSYNHLGNNDGENLSAPLQFRSKEVSKSNVVDDMVQSNPVLYTPGEEPDHCVVIKYVPYVGDSKRALDEYTSELMLGGTNTLVLHNTCEDSLLAAPIMLDLALLTELCQRVSFCTDMDPEPQTFHPVLSLLSFLFKAPLVPPGSPVVNALFRQRSCIENILRACVGLPPQNHMLLEHKMERPGPSLKRVGPVAATYPMLNKKGPVPAATNGCTGDANGHLQEEPPMPTT
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Molecular Weight
61 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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
Related Products
Protein Description
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.
