Analytical Data
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Gene name
PRELP
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简介
The PRELP protein may be an anchoring factor that plays a crucial role in connecting the basement membrane and connective tissue, contributing to structural integrity. Its interaction with the heparan sulfate proteoglycan perlecan and type I and type II collagen emphasizes its versatile binding ability. PRELP Protein, Human (HEK293, Fc) is the recombinant human-derived PRELP protein, expressed by HEK293 , with N-mFc labeled tag.
- Application
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Alternative Names
Prolargin; Proline-arginine-rich end leucine-rich repeat protein; PRELP; SLRR2A
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Species
Human
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Source
HEK293
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Tag
N-mFc
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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
Q21-I382
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Protein Length
Full Length of Mature Protein
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Molecular Weight
80-90 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
PRELP (Proline-arginine-rich end leucine-terminated peptide) is a small, secretory protein that has garnered attention in various fields of biological research due to its unique structural and functional properties. Originally identified in the context of bone metabolism, PRELP plays a crucial role in the regulation of osteogenesis and is thought to be involved in the organization of extracellular matrix components. Its proline- and arginine-rich structure suggests potential interactions with a variety of biomolecules, making it a candidate for investigations into cell signaling pathways and tissue regeneration. Recent studies have highlighted the implications of PRELP in inflammatory responses and its potential role as a biomarker for certain diseases, such as arthritis and cancer. Furthermore, the exploration of PRELP’s recombinant forms for therapeutic applications has opened new avenues in regenerative medicine and tissue engineering. Given its diverse biological effects and potential clinical relevance, the characterization of PRELP and its recombinant variants is essential for understanding its mechanisms of action and developing novel therapeutic strategies targeting relevant diseases.
