Analytical Data
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Gene name
LRP5
- Application
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Alternative Names
LRP5；LR3；LRP7；Low-density lipoProtein receptor-related Protein 5
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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
O75197
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Expression Region
41-130aa
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AA Sequence
RDVRLVDAGGVKLESTIVVSGLEDAAAVDFQFSKGAVYWTDVSEEAIKQT YLNQTGAAVQNVVISGLVSPDGLACDWVGKKLYWTDSETN
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Molecular Weight
36 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
LRP5 (Low-Density Lipoprotein Receptor-related Protein 5) is a crucial co-receptor involved in the Wnt signaling pathway, which plays a significant role in cell proliferation, differentiation, and survival. Dysregulation of LRP5 has been implicated in various pathological conditions, including cancer and osteoporosis, making it a target of interest for therapeutic interventions. Research on recombinant LRP5 proteins aims to elucidate their structure, function, and interactions within cellular signaling networks. By expressing and purifying LRP5 in a recombinant form, scientists can study its biochemical properties, investigate its ligand-binding capabilities, and assess how mutations may affect its role in cellular processes. Understanding LRP5's mechanism can provide insights into the modulation of Wnt signaling, offering potential avenues for developing drug candidates that could restore normal signaling in diseases associated with LRP5 dysfunction. Furthermore, the ability to generate large amounts of recombinant LRP5 protein enables high-throughput screening of small molecules or peptides that may enhance or inhibit its activity, thereby facilitating the discovery of novel therapeutic strategies. Overall, research on LRP5 recombinant proteins contributes to a deeper understanding of its biological significance and lays the groundwork for innovative treatments targeting LRP5-associated disorders.
