Analytical Data
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Gene name
LRRC15
- Application
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Alternative Names
LRRC15；LIB；Leucine-rich repeat-containing Protein 15
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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
Q8TF66
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Expression Region
22-538aa
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AA Sequence
YHGCPSECTCSRASQVECTGARIVAVPTPLPWNAMSLQILNTHITELNESPFLNISALIALRIEKNELSRITPGAFRNLGSLRYLSLANNKLQVLPIGLFQGLDSLESLLLSSNQLLQIQPAHFSQCSNLKELQLHGNHLEYIPDGAFDHLVGLTKLNLGKNSLTHISPRVFQHLGNLQVLRLYENRLTDIPMGTFDGLVNLQELALQQNQIGLLSPGLFHNNHNLQRLYLSNNHISQLPPSVFMQLPQLNRLTLFGNSLKELSPGIFGPMPNLRELWLYDNHISSLPDNVFSNLRQLQVLILSRNQISFISPGAFNGLTELRELSLHTNALQDLDGNVFRMLANLQNISLQNNRLRQLPGNIFANVNGLMAIQLQNNQLENLPLGIFDHLGKLCELRLYDNPWRCDSDILPLRNWLLLNQPRLGTDTVPVCFSPANVRGQSLIIINVNVAVPSVHVPEVPSYPETPWYPDTPSYPDTTSVSSTTELTSPVEDYTDLTTIQVTDDRSVWGMTQAQSG
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Molecular Weight
60.5 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) has emerged as an important focus in biomedical research due to its potential roles in various physiological and pathological processes. This protein, characterized by its leucine-rich repeat domains, is involved in cellular adhesion, migration, and signaling pathways, making it a significant contributor to tissue homeostasis and immune responses. Recent studies have indicated that LRRC15 expression is upregulated in certain cancers, suggesting it may play a role in tumor progression and metastasis. Consequently, investigating LRRC15 as a biomarker for cancer diagnosis and prognosis has gained traction. Moreover, its involvement in the regulation of the extracellular matrix and collagen organization links it to fibrosis and tissue remodeling disorders. As researchers pursue the characterization of LRRC15 and its signaling mechanisms, the development of recombinant LRRC15 protein has become essential for studying its biological functions and potential therapeutic applications. This recombinant protein can facilitate high-throughput assays, structural biology studies, and the examination of LRRC15 interactions with other cellular molecules. Overall, the exploration of LRRC15 through recombinant protein technology holds promise for uncovering new insights into its role in health and disease, paving the way for innovative strategies in cancer therapy and regenerative medicine.
