Analytical Data
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Gene name
plc
- Application
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Alternative Names
Alpha-toxin (Hemolysin) (Lecithinase) (Phosphatidylcholine cholinephosphohydrolase)
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Species
Clostridium perfringens
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0C216
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Expression Region
29-398aa
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Molecular Weight
48.5 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
PLC (phospholipase C) is a crucial enzyme that plays a significant role in cell signaling pathways by hydrolyzing phosphatidylinositol 4,5-bisphosphate to generate inositol trisphosphate (IP3) and diacylglycerol (DAG). The study of PLC recombinant proteins has garnered attention due to their involvement in various physiological processes, including cell growth, differentiation, and apoptosis. Abnormal PLC activity has been implicated in a range of diseases, such as cancer, cardiovascular disorders, and neurological conditions. Consequently, understanding the structure and function of PLCs is pivotal for developing targeted therapies. Advances in recombinant DNA technology allow researchers to produce PLC proteins in heterologous systems, facilitating detailed biochemical studies and structural analyses. By studying PLC recombinant proteins, scientists aim to elucidate their mechanisms of action, regulatory pathways, and interactions with other cellular components. This research not only enhances our understanding of PLC biology but also opens new avenues for pharmaceutical interventions that could modulate PLC activity in disease contexts.
