Analytical Data
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Gene name
CTSE
- Application
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Alternative Names
CTSE；Cathepsin E
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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
P14091-1
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Expression Region
20-396aa
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AA Sequence
SLHRVPLRRHPSLKKKLRARSQLSEFWKSHNLDMIQFTESCSMDQSAKEP LINYLDMEYFGTISIGSPPQNFTVIFDTGSSNLWVPSVYCTSPACKTHSR FQPSQSSTYSQPGQSFSIQYGTGSLSGIIGADQVSVEGLTVVGQQFGESV TEPGQTFVDAEFDGILGLGYPSLAVGGVTPVFDNMMAQNLVDLPMFSVYM SSNPEGGAGSELIFGGYDHSHFSGSLNWVPVTKQAYWQIALDNIQVGGTV MFCSEGCQAIVDTGTSLITGPSDKIKQLQNAIGAAPVDGEYAVECANLNV MPDVTFTINGVPYTLSPTAYTLLDFVDGMQFCSSGFQGLDIHPPAGPLWI LGDVFIRQFYSVFDRGNNRVGLAPAVPVDHHHHHH
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Molecular Weight
42 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
CTSE (Cathepsin E) is a lysosomal cysteine protease that plays a crucial role in various biological processes, including antigen presentation and immune response modulation. Research into CTSE recombinant proteins has gained momentum due to their potential applications in understanding autoimmune diseases, cancer immunology, and therapeutic interventions. CTSE is upregulated in a variety of malignancies and is implicated in processing and presenting specific antigens, which makes it a target of interest for cancer immunotherapy. Additionally, its involvement in the cleavage of extracellular matrix proteins suggests a role in tissue remodeling and inflammation. The development of CTSE recombinant proteins allows for detailed studies of its enzymatic activity, substrate specificity, and regulatory mechanisms. Furthermore, these proteins can serve as tools for elucidating the pathophysiological roles of CTSE in disease states. By using advanced molecular biology techniques, researchers can produce high-yield, active forms of CTSE, enabling detailed structural and functional analyses. This research not only enhances our understanding of CTSE's roles but may also lead to novel therapeutic strategies aimed at modulating its activity in various diseases. Overall, the investigation of CTSE recombinant proteins is a rapidly evolving field that holds significant promise for advancing our knowledge of immune regulation and developing innovative treatments for diseases characterized by dysregulated proteolytic activity.
