Analytical Data
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Gene name
CYSRT1
- Application
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Alternative Names
CYSRT1；C9orf169；Cysteine-rich tail Protein 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
B8A4K4
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Expression Region
1-184aa
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AA Sequence
MAPPLPRREKAAASRSTQALGPRAQKTERTDCRVATTGWTMDPQEMVVKNPYAHISIPRAHLRPDLGQQLEVASTCSSSSEMQPLPVGPCAPEPTHLLQPTEVPGPKGAKGNQGAAPIQNQQAWQQPGNPYSSSQRQAGLTYAGPPPAGRGDDIAHHCCCCPCCHCCHCPPFCRCHSCCCCVIS
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Molecular Weight
25.2 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
CYSRT1 is a member of the sialic acid-binding immunoglobulin-like lectin (Siglec) family, which plays a crucial role in cell-cell interactions and immune response modulation. Research into CYSRT1 has gained momentum due to its potential implications in various pathological conditions, including autoimmune disorders and cancer. The protein is characterized by its ability to bind sialic acids, which are often present on the surface of glycoproteins and glycolipids, influencing cellular signaling pathways. This interaction can lead to the regulation of immune responses, making CYSRT1 a compelling target for therapeutic interventions. Additionally, studies suggest that altered expression of CYSRT1 may be linked to the progression of certain diseases, highlighting its significance in both basic and translational research. By generating recombinant CYSRT1 proteins, researchers aim to delve deeper into its functional mechanisms and explore its potential as a biomarker or therapeutic target, contributing to the development of novel treatments for a range of diseases. The growing interest in CYSRT1 underscores the necessity for a comprehensive understanding of its role in physiology and pathology, paving the way for innovative approaches in disease management.
