Analytical Data
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Gene name
PRAP1
- Application
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Alternative Names
PRAP1；UPA；Proline-rich acidic 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
Q96NZ9
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Expression Region
1-151aa
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AA Sequence
MRRLLLVTSL VVVLLWEAGA VPAPKVPIKM QVKHWPSEQD PEKAWGARVV EPPEKDDQLV VLFPVQKPK LLTTEEKPRG QGRGPILPGT KAWMETEDTL GHVLSPEPDH DSLYHPPPEE DQGEERPRL WVMPNHQVLL GPEEDQDHIY HPQ
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Molecular Weight
16 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
PRAP1 (Proline-Rich Acidic Protein 1) is a protein that has garnered significant attention in the field of molecular biology due to its potential roles in various cellular processes, including cell signaling, stress response, and disease mechanisms. Initially identified for its high proline and acidic amino acid content, PRAP1 is hypothesized to participate in the regulation of protein-protein interactions and cellular homeostasis. Research indicates that PRAP1 may play a crucial role in the development of certain cancers, cardiovascular diseases, and neurodegenerative disorders. The investigation of PRAP1 as a recombinant protein has become a focal point for understanding its structure-function relationships and cellular roles, which could lead to innovative therapeutic strategies. By producing PRAP1 in recombinant systems, researchers aim to obtain a sufficient quantity of the protein for biochemical characterization, functional assays, and potential drug development. Furthermore, the study of PRAP1's interactions with other cellular components could reveal insights into the molecular pathways it influences, ultimately contributing to our understanding of its involvement in health and disease. This makes PRAP1 not only a subject of fundamental research but also a promising candidate for targeted therapy in various pathological conditions.
