Analytical Data
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Gene name
PIB5PA
- Application
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Alternative Names
INPP5J; PIB5PA; PIPP; Phosphatidylinositol 4.5-bisphosphate 5-phosphatase A; EC 3.1.3.56; Inositol polyphosphate 5-phosphatase J
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q15735
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Expression Region
361-470 aa
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AA Sequence
FLLQFAFRDDMPLVRLEVADEWVRPEQAVVRYRMETVFARSSWDWIGLYRVGFRHCKDYVAYVWAKHEDVDGNTYQVTFSEESLPKGHGDFILGYYSHNHSILIGITEPF
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Molecular Weight
37.84 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
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Protein Description
PIB5PA, a protein implicated in various cellular processes, has garnered significant attention in recent years due to its potential roles in cell signaling, growth, and response to stress. Research into PIB5PA has expanded as scientists seek to understand its function in different biological contexts, including its involvement in cancer biology and neurodegenerative disorders. The protein is known to interact with various signaling pathways, suggesting a critical role in modulating cellular responses to external stimuli. Investigating the structural and functional properties of PIB5PA can provide insights into its mechanisms of action and its relevance in pathological conditions. Moreover, the development of recombinant PIB5PA has enabled detailed studies of its properties, facilitating the exploration of its potential as a therapeutic target. Recent advances in protein engineering techniques have allowed researchers to create more stable and active forms of PIB5PA, thus paving the way for innovative applications in biotechnology and medicine. As a result, understanding PIB5PA not only enhances our knowledge of fundamental biological processes but also opens doors for new therapeutic strategies in treating diseases where this protein plays a pivotal role.
