Analytical Data
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Gene name
ST3GAL5
- Application
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Alternative Names
ST3GAL5;SIAT9;Lactosylceramide alpha-2.3-sialyltransferase
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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
Q9UNP4
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Expression Region
83-418aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSLKLNYTT EECDMKKMHY VDPDHVKRAQ KYAQQVLQKE CRPKFAKTSM ALLFEHRYSV DLLPFVQKAP KDSEAESKYD PPFGFRKFSS KVQTLLELLP EHDLPEHLKA KTCRRCVVIG SGGILHGLEL GHTLNQFDVV IRLNSAPVEG YSEHVGNKTT IRMTYPEGAP LSDLEYYSND LFVAVLFKSV DFNWLQAMVK KETLPFWVRL FFWKQVAEKI PLQPKHFRIL NPVIIKETAF DILQYSEPQS RFWGRDKNVP TIGVIAVVLA THLCDEVSLA GFGYDLNQPR TPLHYFDSQC MAAMNFQTMH NVTTETKFLL KLVKEGVVKD LSGGIDREF
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Molecular Weight
41 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
ST3GAL5, or ST3 beta-galactoside alpha-2,3-sialyltransferase 5, is an enzyme critical for the biosynthesis of sialic acid-containing glycoconjugates. Research into ST3GAL5 has garnered significant interest due to its potential implications in various biological processes and disease mechanisms. Sialylation, the addition of sialic acid residues to glycans, plays a vital role in cellular interactions, immune responses, and pathogen recognition. Dysregulation of sialylation has been linked to cancer progression, inflammatory diseases, and viral infections. Studies suggest that ST3GAL5 may influence tumor cell behavior and immune evasion by altering the sialylation patterns of glycoproteins and glycolipids on the cell surface. Furthermore, the enzyme's role in developing therapeutic strategies, particularly in cancer immunotherapy and vaccine design, has highlighted its importance. Understanding the structure and function of ST3GAL5 is essential for uncovering the mechanisms by which it regulates sialylation and impacts cellular functions. Consequently, exploring ST3GAL5 provides a promising avenue for advancing our knowledge of glycobiology and developing targeted therapies for diseases associated with aberrant sialylation. Current efforts focus on characterizing ST3GAL5's enzymatic properties, identifying its substrates, and elucidating its role in pathophysiological contexts, which ultimately may lead to novel therapeutic insights and applications.
