Analytical Data
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Gene name
cysP
- Application
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Alternative Names
cysP；Ctsl1；Procathepsin L
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Species
E.coli
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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
P16700
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Expression Region
26-338aa
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AA Sequence
TELLNSSYDVSRELFAALNPPFEQQWAKDNGGDKLTIKQSHAGSSKQALAILQGLKADVVTYNQVTDVQILHDKGKLIPADWQSRLPNNSSPFYSTMGFLVRKGNPKNIHDWNDLVRSDVKLIFPNPKTSGNARYTYLAAWGAADKADGGDKGKTEQFMTQFLKNVEVFDTGGRGATTTFAERGLGDVLISFESEVNNIRKQYEAQGFEVVIPKTNILAEFPVAWVDKNVQANGTEKAAKAYLNWLYSPQAQTIITDYYYRVNNPEVMDKLKDKFPQTELFRVEDKFGSWPEVMKTHFTSGGELDKLLAAGRN
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Molecular Weight
48.0 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
CysP, or cysteine phosphatase, is a significant enzyme that plays a crucial role in the regulation of various biological processes, including cellular response to stress, signaling pathways, and metabolism. Research into CysP has gained attention due to its potential implications in understanding cellular redox states and its involvement in the modulation of cysteine metabolism. The enzymatic activity of CysP is vital for maintaining homeostasis in both prokaryotic and eukaryotic organisms, making it an important target for therapeutic intervention in conditions characterized by oxidative stress or metabolic disorders. Recombining the CysP protein allows for detailed biochemical studies and offers insights into its structural and functional properties. By producing CysP in a recombinant form, researchers can explore its enzymatic mechanisms, substrate specificity, and potential interactions with other cellular pathways. This research not only enhances our grasp of CysP’s biological roles but also opens avenues for the development of novel pharmacological agents that could modulate its activity in disease contexts. Understanding CysP's function and mechanisms further provides a foundational knowledge that could inform therapeutic strategies targeting related metabolic and oxidative stress disorders. Overall, the study of recombinant CysP is indicative of broader trends in biochemical research, emphasizing the importance of understanding enzymes at a molecular level to harness their potential in health and disease.
