Analytical Data
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Gene name
Prss22
- Application
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Alternative Names
PRSS22;BSSP4;PRSS26;Brain-specific serine protease 4
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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
Q9GZN4
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Expression Region
33-317aa
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AA Sequence
ARIPVPPACGKPQQLNRVVGGEDSTDSEWPWIVSIQKNGTHHCAGSLLTS RWVITAAHCFKDNLNKPYLFSVLLGAWQLGNPGSRSQKVGVAWVEPHPVY SWKEGACADIALVRLERSIQFSERVLPICLPDASIHLPPNTHCWISGWGS IQDGVPLPHPQTLQKLKVPIIDSEVCSHLYWRGAGQGPITEDMLCAGYLE GERDACLGDSGGPLMCQVDGAWLLAGIISWGEGCAERNRPGVYISLSAHR SWVEKIVQGVQLRGRAQGGGALRAPSQGSGAAARSHHHHHH
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Molecular Weight
32 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
PRSS22, also known as serine protease 22, is a member of the serine protease family, which plays a critical role in a variety of biological processes, including inflammation, blood coagulation, and immune responses. The research surrounding PRSS22 has gained momentum due to its potential implications in various diseases, particularly in cancer and autoimmune disorders. Increased expression of PRSS22 has been observed in certain tumors, suggesting it may be involved in tumorigenesis and metastasis. This has spurred interest in characterizing the proteolytic activity of PRSS22 and understanding its substrate specificity. Additionally, investigations into the molecular mechanisms underlying its regulation and function could provide insights into its role in disease pathways. By studying recombinant PRSS22 proteins, researchers aim to elucidate its biochemical properties, interactions with other proteins, and potential as a therapeutic target. The production and purification of recombinant PRSS22 enable detailed functional assays and structural studies, which are critical for developing strategies to inhibit its activity in pathological conditions. Furthermore, understanding the role of PRSS22 in the context of the tumor microenvironment can lead to novel biomarkers for cancer diagnosis and prognosis, as well as new therapeutic approaches utilizing serine protease inhibitors. Overall, the research on PRSS22 is not only significant for basic biological understanding but also holds promise for translational applications in the field of medicine.
