Analytical Data
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Gene name
plc
- Application
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Alternative Names
plc；KIAA1092；PLCE2；Inactive phospholipase C-like Protein 2
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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
P98160
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Expression Region
4197-4391aa
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AA Sequence
DAPGQYGAYFHDDGFLAFPGHVFSRSLPEVPETIELEVRTSTASGLLLWQGVEVGEAGQGKDFISLGLQDGHLVFRYQLGSGEARLVSEDPINDGEWHRVTALREGRRGSIQVDGEELVSGRSPGPNVAVNAKGSVYIGGAPDVATLTGGRFSSGITGCVKNLVLHSARPGAPPPQPLDLQHRAQAGANTRPCPS
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Molecular Weight
27.5 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
The study of phospholipase C (PLC) recombinant proteins is rooted in the understanding of their critical roles in cellular signaling pathways. PLC enzymes are pivotal in mediating the breakdown of phosphatidylinositol 4,5-bisphosphate (PIP2) into inositol trisphosphate (IP3) and diacylglycerol (DAG), which are essential secondary messengers in various physiological processes, including cell proliferation, differentiation, and apoptosis. The dysregulation of PLC activity has been implicated in numerous diseases, including cancer, cardiovascular disorders, and neurological conditions. Due to their significant biological functions, there is a growing interest in the production and characterization of recombinant PLC proteins, which can provide insights into their structure-function relationships and facilitate the development of targeted therapeutics. Advances in recombinant DNA technology have enabled the expression of PLC proteins in various systems, such as bacteria, yeast, and mammalian cells, allowing researchers to obtain sufficient quantities for detailed biochemical studies. Furthermore, the ability to engineer these proteins through site-directed mutagenesis or other protein engineering techniques enhances our understanding of their mechanisms and potential as drug targets. As the field progresses, the study of PLC recombinant proteins continues to unveil novel aspects of cellular signaling, paving the way for innovative therapeutic strategies that could mitigate the impact of PLC-related diseases.
