Analytical Data
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Gene name
SIAL2
- Application
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Alternative Names
MEU2; N-Acetyl-Alpha-Neuraminidase 2; Cytosolic sialidase
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q64627
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Expression Region
His185~Gln379
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Molecular Weight
25kDa
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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
SIAL2, a member of the sialic acid-binding immunoglobulin-like lectin (Siglec) family, has garnered attention due to its potential role in immune modulation and disease pathology. This protein is primarily expressed on the surface of immune cells, such as T cells and dendritic cells, where it may participate in the regulation of immune responses by interacting with its sialic acid ligands on various cell types. Research has shown that SIAL2 can influence cell signaling pathways, which in turn can affect the outcomes of immune activation or inhibition. Understanding the functional mechanisms of SIAL2 and its interactions in the immune environment could provide insights into its role in autoimmunity, cancer, and infectious diseases. Furthermore, the development of SIAL2 recombinant proteins holds promise for therapeutic applications, including the design of novel immune checkpoint inhibitors or vaccines. Given the growing evidence of the significance of sialic acid interactions in biological processes, SIAL2 presents an intriguing target for further investigation in both basic and translational research settings.
