Analytical Data
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Gene name
PRR4
- Application
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Alternative Names
LPRP; PROL4; Lacrimal proline-rich protein; Nasopharyngeal carcinoma-associated proline-rich protein 4
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q16378
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Expression Region
Gln17~Trp134
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Molecular Weight
41kDa
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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
PRR4 (Proline-Rich Protein 4) is a member of the proline-rich protein family, which has garnered attention due to its potential roles in cellular processes, particularly in the context of cancer and inflammation. Research indicates that PRR4 is significantly upregulated in various types of cancers, suggesting a potential link between its expression and tumor progression. Understanding the molecular mechanisms underlying PRR4's function can provide insights into its role in the tumor microenvironment and cell signaling pathways. Moreover, PRR4 is thought to play a role in modulating immune responses, reinforcing its significance in both oncological and inflammatory diseases. The study of recombinant PRR4 proteins enables researchers to explore their structure-function relationships and interactions with other biomolecules, paving the way for the development of therapeutic strategies targeting PRR4-related pathways. Furthermore, advances in protein engineering techniques offer opportunities to create modified forms of PRR4 that may enhance its therapeutic efficacy or act as biomarkers for disease progression. Overall, PRR4 presents a promising avenue for research focused on understanding complex disease mechanisms and developing novel interventions in the fields of cancer biology and immunology.
