Analytical Data
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Gene name
PIR
- Application
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Alternative Names
Iron Binding Nuclear Protein; Probable quercetin 2,3-dioxygenase PIR; Probable quercetinase
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Species
Human
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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
O00625
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Expression Region
Met1~Asn290
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Molecular Weight
36kDa
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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
PIR (Pathogen-Induced Resistance) proteins play a crucial role in plant immunity, particularly in the response to pathogen attacks. These proteins are involved in various defense mechanisms, including the recognition of pathogen-associated molecular patterns (PAMPs) and the activation of signaling pathways that lead to enhanced resistance. Recent research has focused on the molecular mechanisms governing PIR protein function and their interactions with other components of the plant immune system. Studies suggest that PIR proteins can modulate the expression of defense-related genes, helping plants to adapt to biotic stresses from pathogens such as fungi, bacteria, and viruses. Furthermore, advancements in genomics and proteomics have allowed scientists to better understand the diversity and evolution of PIR proteins across different plant species. This knowledge is critical for breeding programs aimed at developing disease-resistant crops, which are essential for ensuring food security in the face of increasing global challenges such as climate change and emerging pathogens. Overall, the study of PIR proteins not only enhances our understanding of plant-microbe interactions but also holds promise for improving agricultural practices and fortifying crops against diseases.
