Analytical Data
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Gene name
CTSF
- Application
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Alternative Names
CTSF;Cathepsin F
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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
Q9UBX1
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Expression Region
273-484aa
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AA Sequence
PEWDWRSKGAVTKVKDQGMCGSCWAFSVTGNVEGQWFLNQGTLLSLSEQELLDCDKMDKACMGGLPSNAYSAIKNLGGLETEDDYSYQGHMQSCNFSAEKAKVYINDSVELSQNEQKLAAWLAKRGPISVAINAFGMQFYRHGISRPLRPLCSPWLIDHAVLLVGYGNRSDVPFWAIKNSWGTDWGEKGYYYLHRGSGACGVNTMASSAVVD
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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
CTSF (Cathepsin F) is a lysosomal cysteine protease that has garnered attention in recent years due to its potential roles in various physiological and pathological processes. Research has shown that CTSF is involved in protein degradation, immune response modulation, and the processing of bioactive peptides. It has also been implicated in certain diseases, including neurodegenerative disorders and cancers, suggesting a crucial role in cellular homeostasis and pathology. The interest in CTSF as a therapeutic target has led to the investigation of recombinant forms of the protein for better understanding its structure-function relationships, enzymatic activity, and substrate specificity. Efforts in recombinant protein technology aim to produce CTSF in sufficient quantities for detailed biochemical studies, which could elucidate its mechanism of action and pave the way for potential drug development. Moreover, understanding the regulation of CTSF expression and activity may unveil new insights into therapeutic approaches for diseases where CTSF is dysregulated. The exploration of CTSF's role in cellular processes and its potential as a biomarker or therapeutic target underscores the need for continued research in this area, making it a significant focus in the fields of molecular biology and biochemistry.
