Analytical Data
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Gene name
CTSL2
- Application
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Alternative Names
CAT L2; Cathepsin L2; Cathepsin U; Cathepsin V; CathepsinL2; CathepsinU; CathepsinV; CATL 2; CATL2; CATL2_HUMAN; CTS L2; CTS U; CTS V; CTSL 2; CTSL2; CTSU; CTSV; MGC125957; PRO305; UNQ268
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O60911
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Expression Region
1-334aa
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AA Sequence
MNLSLVLAAFCLGIASAVPKFDQNLDTKWYQWKATHRRLYGANEEGWRRAVWEKNMKMIELHNGEYSQGKHGFTMAMNAFGDMTNEEFRQMMGCFRNQKFRKGKVFREPLFLDLPKSVDWRKKGYVTPVKNQKQCGSCWAFSATGALEGQMFRKTGKLVSLSEQNLVDCSRPQGNQGCNGGFMARAFQYVKENGGLDSEESYPYVAVDEICKYRPENSVANDTGFTVVAPGKEKALMKAVATVGPISVAMDAGHSSFQFYKSGIYFEPDCSSKNLDHGVLVVGYGFEGANSNNSKYWLVKNSWGPEWGSNGYVKIAKDKNNHCGIATAASYPNV
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Molecular Weight
63.7 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
CTSL2, or Cathepsin L2, is a member of the cathepsin family of proteases, which are primarily involved in protein degradation and processing within lysosomal pathways. Research has highlighted its significant role in various physiological processes, including tissue remodeling, immune responses, and cellular homeostasis. Notably, CTSL2 has been implicated in pathological conditions such as cancer, neurodegenerative diseases, and inflammation, making it a focal point in biomedical research. Given its association with these critical biological processes, the recombinant expression of CTSL2 protein has garnered attention in both fundamental and applied studies. Utilizing recombinant DNA technology, researchers can produce CTSL2 in host cells, facilitating the study of its biochemical properties, substrate specificity, and interaction with other molecules. This approach not only enhances our understanding of CTSL2's functional roles in health and disease but also opens avenues for the development of potential therapeutic interventions targeting CTSL2-related pathways. By investigating the structure-function relationships and regulatory mechanisms governing CTSL2 activity, scientists aim to elucidate its contribution to pathological processes and explore its potential as a biomarker or therapeutic target in various diseases. Overall, studies involving recombinant CTSL2 protein hold promise for advancing our knowledge of lysosomal proteases and their relevance in human health.
