Analytical Data
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Gene name
PRSS23
- Application
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Alternative Names
PRSS23；ZSIG13；Serine protease 23
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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
O95084
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Expression Region
20-383aa
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AA Sequence
QVSPYSAPWKPTWPAYRLPVVLPQSTLNLAKPDFGAEAKLEVSSSCGPQCHKGTPLPTYEEAKQYLSYETLYANGSRTETQVGIYILSSSGDGAQHRDSGSSGKSRRKRQIYGYDSRFSIFGKDFLLNYPFSTSVKLSTGCTGTLVAEKHVLTAAHCIHDGKTYVKGTQKLRVGFLKPKFKDGGRGANDSTSAMPEQMKFQWIRVKRTHVPKGWIKGNANDIGMDYDYALLELKKPHKRKFMKIGVSPPAKQLPGGRIHFSGYDNDRPGNLVYRFCDVKDETYDLLYQQCDAQPGASGSGVYVRMWKRQQQKWERKIIGIFSGHQWVDMNGSPQDFNVAVRITPLKYAQICYWIKGNYLDCREG
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Molecular Weight
45.1 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
PRSS23, also known as serine protease 23, is a member of the serine protease family, which plays a critical role in various biological processes, including blood coagulation, immune response, and cellular signaling. Recent studies have highlighted its potential involvement in pathological conditions such as cancer and inflammatory diseases, prompting researchers to investigate its mechanisms of action and physiological relevance. The interest in PRSS23 has grown due to its unique structural features and expression patterns, suggesting it may have specialized functions that differ from other serine proteases. Furthermore, understanding PRSS23 could provide insights into novel therapeutic targets for diseases linked to dysregulated protease activity. The quest for effective modulation of PRSS23 activity has led to advancements in recombinant protein technology, allowing for the production and characterization of PRSS23 in a laboratory setting. This research aims to elucidate the functional roles and regulatory mechanisms of PRSS23, which may ultimately pave the way for innovative approaches in disease treatment and prevention.
