Analytical Data
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Gene name
Cathepsin L1
- Application
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Alternative Names
CTSL1; CATL; CTS-L; MEP; Cathepsin L1; Major excreted protein
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Species
Mouse
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P06797
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Expression Region
Thr18~Lys113
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Molecular Weight
40kDa
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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
Cathepsin L1 is a cysteine protease that plays a crucial role in various biological processes, including protein degradation, antigen processing, and apoptosis. It is widely expressed in different tissues and is particularly implicated in cancer progression, immune response, and various inflammatory conditions. Research has shown that Cathepsin L1 is involved in the remodeling of the extracellular matrix, which is vital for tumor metastasis and tissue repair. Due to its significant role in disease, Cathepsin L1 has emerged as a potential therapeutic target. The recombinant Cathepsin L1 protein offers a powerful tool for studying its biochemical properties and physiological functions in vitro and in vivo. By producing and characterizing this recombinant protein, researchers can dissect the enzymatic mechanisms underlying its activity and interactions with substrates. Moreover, understanding the structure-function relationship of Cathepsin L1 could lead to the development of novel inhibitors or therapies that could impede its activity in pathological conditions. Additionally, recombinant Cathepsin L1 provides an avenue for exploring its diagnostic potential as a biomarker for certain diseases. Overall, the study of recombinant Cathepsin L1 protein is pivotal in advancing our understanding of its biological significance and its implications in health and disease.
