Analytical Data
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Gene name
PRB1
- Application
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Alternative Names
PRB1；Retinoblastoma-like Protein 1
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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
P04280
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Expression Region
17-103aa
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AA Sequence
QNLNEDVSQEESPSLIAGNPQGPSPQGGNKPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGDKSRSPRSPPGKPQGPPPQ
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Molecular Weight
40.2 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
PRB1, or Proline-rich protein 1, is a significant protein involved in various physiological processes, particularly in the context of oral health and epithelial tissue functions. Research has indicated its pivotal role in the maintenance of oral mucosal integrity, wound healing, and immune responses. Given its proline-rich nature, PRB1 interacts with a variety of cellular components, influencing cell adhesion and signaling pathways. Studies have shown that abnormalities or dysregulation of PRB1 expression may contribute to oral diseases, including periodontitis and oral cancers. The investigation of PRB1 recombinant protein has garnered attention in recent years, as it may serve as a potential biomarker for disease states or be utilized in therapeutic applications. By studying PRB1 through recombinant technology, researchers aim to better understand its structural properties, functional mechanisms, and interactions with other biomolecules. The findings from these studies could pave the way for innovative strategies in disease prevention and treatment, highlighting the importance of PRB1 in both basic science and clinical applications. Consequently, the exploration of PRB1 recombinant protein not only enhances our understanding of its biological functions but also opens new avenues for therapeutic interventions in oral and systemic diseases.
