Analytical Data
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Gene name
PRELP
- Application
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Alternative Names
PRELP；SLRR2A；Prolargin
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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
P51888
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Expression Region
21-382aa
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AA Sequence
QPTRRPRPGT GPGRRPRPRP RPTPSFPQPD EPAEPTDLPP PLPPGPPSIF PDCPRECYCP PDFPSALYCD SRNLRKVPVI PPRIHYLYLQ NNFITELPVE SFQNATGLRW INLDNNRIRK IDQRVLEKLP GLVFLYMEKN QLEEVPSALP RNLEQLRLSQ NHISRIPPGV FSKLENLLLL DLQHNRLSDG VFKPDTFHGL KNLMQLNLAH NILRKMPPRV PTAIHQLYLD SNKIETIPNG YFKSFPNLAF IRLNYNKLTD RGLPKNSFNI SNLLVLHLSH NRISSVPAIN NRLEHLYLNN NSIEKINGTQ ICPNDLVAFH DFSSDLENVP HLRYLRLDGN YLKPPIPLDL MMCFRLLQSV VI
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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
PRELP (Proline-Arginine Rich End Leucine-Peptide) is a protein that has garnered increasing interest in the field of biomedical research due to its unique structure and potential implications in various physiological and pathological processes. Initially discovered as a component of the extracellular matrix, PRELP is characterized by its high proline and arginine content, which contributes to its role in tissue remodeling and cellular interactions. Studies have demonstrated that PRELP is involved in processes such as wound healing, inflammation, and scar formation, highlighting its importance in both normal physiology and disease contexts. Given its potential role as a biomarker for certain pathological conditions, including cancer and fibrotic diseases, researchers have focused on elucidating the mechanisms by which PRELP influences cellular behavior and tissue dynamics. Furthermore, recombinant forms of PRELP are being explored for their therapeutic potential, particularly in regenerative medicine and tissue engineering applications. The ongoing research aims not only to clarify the biological functions of PRELP but also to leverage its properties for innovative treatment strategies. As such, continued investigation into PRELP and its applications could pave the way for novel interventions in various health conditions, making it a significant focus within the realms of molecular biology and therapeutic development.
