Analytical Data
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Gene name
PRR15
- Application
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Alternative Names
PRR15; Proline-rich protein 15
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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
Q8IV56
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Expression Region
1-129 aa
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AA Sequence
MADSGDAGSS GPWWKSLTNS RKKSKEAAVG VPPPAQPAPG EPTPPAPPSP DWTSSSRENQ HPNLLGGAGE PPKPDKLYGD KSGSSRRNLK ISRSGRFKEK RKVRATLLPE AGRSPEEAGF PGDPHEDKQ
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Molecular Weight
13.7 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
PRR15 (Proline-Rich Protein 15) is a member of the proline-rich protein family, which plays significant roles in various biological processes, including cell signaling, cytoskeletal organization, and cellular response to stress. Its expression is regulated in different tissues and is particularly relevant in the context of cancer and other diseases. Recent studies indicate that PRR15 interacts with key signaling pathways, thereby modulating the behavior of cancer cells and influencing their proliferation, migration, and invasion. Given the importance of understanding the molecular mechanisms underlying tumorigenesis, researchers have focused on characterizing PRR15's structure and function, as well as its potential as a biomarker or therapeutic target. Furthermore, advancements in recombinant protein technology have enabled the production of PRR15 in sufficient quantities for in-depth studies. This research aims to elucidate the intricate role of PRR15 in cellular mechanisms, its impact on disease progression, and explore its potential utility in clinical settings. As such, understanding PRR15's functions could contribute to the development of novel therapeutic strategies and improve patient outcomes in various malignancies. The ongoing investigations into PRR15's biological significance underscore its potential as a crucial player in cancer biology and a promising avenue for future research.
