Analytical Data
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Gene name
LRRC15
- Application
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Alternative Names
LIB; LRRC15
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Species
Rat
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Source
HEK293
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Tag
C-Avi;C-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8R5M3
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Expression Region
Y22-G535
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Molecular Weight
70-90 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
Related Products
Protein Description
LRRC15 (Leucine-Rich Repeat Containing 15) is a protein that has garnered attention in recent years due to its potential role in various biological processes and diseases. Initially discovered for its involvement in extracellular matrix interactions, LRRC15 has been implicated in pathophysiological conditions, particularly in cancers and fibrosis. Studies suggest that LRRC15 may play a critical role in tumor microenvironment regulation, influencing factors like cell adhesion, migration, and immune response. Its expression is often upregulated in tumors, making it a potential biomarker for cancer diagnosis and prognosis. Furthermore, the protein's function in fibrogenesis highlights its relevance in chronic inflammatory diseases. Researchers are increasingly interested in generating recombinant LRRC15 protein for the purpose of elucidating its structural and functional characteristics, which could pave the way for novel therapeutic strategies. Understanding the molecular mechanisms by which LRRC15 participates in disease pathways could offer insights into targeted treatments, particularly in conditions where current therapeutic options are limited. The development of LRRC15-based assays may also enhance our understanding of its biological significance in health and disease. Overall, the study of LRRC15 and its recombinant forms is crucial for unraveling its potential as a therapeutic target and for advancing our comprehension of its role in complex biological systems.
