Analytical Data
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Gene name
ST3GAL4
- Application
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Alternative Names
ST3GAL4; CGS23; NANTA3; SIAT4C; STZ; CMP-N-acetylneuraminate-beta-galactosamide-alpha-2.3-sialyltransferase 4; Alpha 2.3-ST 4; Beta-galactoside alpha-2.3-sialyltransferase 4; EC 2.4.99.2; EC 2.4.99.4; Alpha 2.3-sialyltransferase IV; Gal-NAc6S; Gal-beta-1.4-GalNAc-alpha-2.3-sialyltransferase; SAT-3; ST-4; ST3Gal IV; ST3GalIV; ST3GalA.2; STZ; Sialyltransferase 4C; SIAT4-C
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q11206
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Expression Region
31-130 aa
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AA Sequence
FYFPIPEKKEPCLQGEAESKASKLFGNYSRDQPIFLRLEDYFWVKTPSAYELPYGTKGSEDLLLRVLAITSSSIPKNIQSLRCRRCVVVGNGHRLRNSSL
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Molecular Weight
36.74 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
ST3GAL4, a member of the ST3Gal family of sialyltransferases, plays a crucial role in the biosynthesis of glycoproteins and glycolipids by adding sialic acid to terminal galactose residues. This enzymatic activity is vital for various cellular processes, including cell-cell interactions, immune response modulation, and the maintenance of protein stability. Dysregulation of ST3GAL4 has been implicated in several diseases, notably cancer, where alterations in sialylation patterns can promote tumor progression and metastasis. Research on ST3GAL4 recombinant protein has gained significant attention as scientists aim to understand its functional mechanisms and explore its potential as a therapeutic target. Using recombinant DNA technology, researchers can produce ST3GAL4 in a controlled environment, allowing for detailed analysis of its enzymatic properties, substrate specificity, and the impact of its activity on cellular behavior. Such studies not only enhance our comprehension of sialylation biology but also pave the way for developing novel treatments for sialic acid-related disorders. By elucidating the role of ST3GAL4 in pathophysiological contexts, researchers hope to uncover new diagnostic markers and therapeutic avenues, contributing to advancements in precision medicine. Thus, the investigation of ST3GAL4 recombinant protein is a critical endeavor in understanding the complexities of glycosylation and its implications in health and disease.
