Analytical Data
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Gene name
SERHL
- Application
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Alternative Names
SERHL; SERHL2; Serine hydrolase-like protein; SHL; EC 3.1.-.-
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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
Q9NQF3
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Expression Region
1-203 aa
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AA Sequence
MAENAAPGLI SELKLAVPWG HIAAKAWGSL QGPPVLCLHG WLDNASSFDR LIPLLPQDFY YVAMDFGGHG LSSHYSPGVP YYLQTFVSEI RRVVAALKWN RFSILGHSFG GVVGGMFFCT FPEMVDKLIL LDTPLFLLES DEMENLLTYK RRAIEHVLQV EASQEPSHVF SLKQLLQRQR TALTSSAGSC VRIPSGSCRP MSC
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Molecular Weight
22.4 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
SERHL (serine-rich hydrophilic protein) is a newly identified protein that has garnered attention due to its potential role in various biological processes and its involvement in diseases. Research indicates that SERHL is predominantly expressed in specific tissues, suggesting a specialized function that may be linked to cell signaling, stress response, or development. Its unique serine-rich domain raises questions about its biochemical properties and interaction with other cellular components. Early studies have shown that alterations in SERHL expression correlate with certain pathological conditions, including inflammatory diseases and cancer, positioning it as a potential biomarker for diagnosis or a target for therapeutic intervention. This research background highlights the need for further investigation into the molecular mechanisms governing SERHL’s activity and its implications in health and disease, paving the way for innovative approaches in biomedical research and treatment strategies. As scientists continue to explore the functional aspects of SERHL, the potential for discovering novel pathways and therapeutic targets remains a compelling area of study.
