Neuraminidase Activators are chemical compounds that either directly enhance the functional activity of Neuraminidase or facilitate the assessment of its activity in various assays. Compounds such as Zanamivir, Oseltamivir phosphate, Peramivir, and Laninamivir are known neuraminidase inhibitors that, through competitive inhibition, bind to the active site of the enzyme, preventing it from cleaving sialic acid. This counterintuitive approach of using inhibitors as activators serves a crucial role in assay systems by allowing for the better characterization of Neuraminidase's enzymatic activity, as they can stabilize the enzyme-substrate complex or enhance detection. The presence of the enzyme's natural substrate, sialic acid, also serves to enhance Neuraminidase's catalytic function by providing more target molecules for cleavage, while DANA, a sialic acid analog, helps to refine the understanding of Neuraminidase's catalytic mechanism by acting as a transition state inhibitor.
Further enhancement of Neuraminidase activity is achieved through the use of various other compounds that affect the enzyme's stability and interaction with substrates. Calcium ions are essential for the structural integrity of Neuraminidase and can enhance its activity by maintaining its conformational stability
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Zanamivir | 139110-80-8 | sc-208495 | 1 mg | $270.00 | 6 | |
This neuraminidase inhibitor binds to the active site of Neuraminidase, preventing it from cleaving sialic acid and thus indirectly enhancing its detection and study in assays. | ||||||
Oseltamivir phosphate | 204255-11-8 | sc-208135 sc-208135A | 10 mg 200 mg | $179.00 $650.00 | 5 | |
Another neuraminidase inhibitor, which through competitive inhibition, allows for better characterization of Neuraminidase activity in biological systems. | ||||||
Peramivir | 330600-85-6 | sc-478569 | 1 mg | $317.00 | ||
A cyclopentane neuraminidase inhibitor that serves to stabilize the enzyme-substrate complex, enabling improved analysis of Neuraminidase function. | ||||||
Laninamivir | 203120-17-6 | sc-488700 sc-488700A sc-488700B sc-488700C sc-488700D sc-488700E | 500 µg 5 mg 50 mg 100 mg 250 mg 1 g | $411.00 $2710.00 $18212.00 $27417.00 $41101.00 $70752.00 | ||
Inhibitor of Neuraminidase that also acts by binding to its active site, thereby facilitating the study of Neuraminidase action on sialic acid-containing substrates. | ||||||
N-Acetylneuraminic acid | 131-48-6 | sc-281055A sc-281055 sc-281055D sc-281055B sc-281055C | 1 g 5 g 25 g 100 g 250 g | $84.00 $156.00 $326.00 $572.00 $1363.00 | ||
As the substrate of Neuraminidase, increased levels of sialic acid can enhance the enzyme's natural activity by providing more target molecules for cleavage. | ||||||
N-Acetyl-2,3-dehydro-2-deoxyneuraminic acid | 24967-27-9 | sc-215433 sc-215433A sc-215433B | 5 mg 10 mg 25 mg | $168.00 $278.00 $549.00 | ||
A sialic acid analog that acts as a transition state inhibitor of Neuraminidase; its presence in assays can help refine the understanding of the enzyme's mechanism. | ||||||
Calcium | 7440-70-2 | sc-252536 | 5 g | $209.00 | ||
Necessary for the stability and activity of Neuraminidase, Ca^2+ ions can enhance Neuraminidase activity by maintaining its conformational integrity. | ||||||
Triton X-100 | 9002-93-1 | sc-29112 sc-29112A | 100 ml 500 ml | $20.00 $42.00 | 55 | |
A non-ionic surfactant that can be used to solubilize Neuraminidase, increasing its availability and activity in assays. | ||||||
L-Arginine | 74-79-3 | sc-391657B sc-391657 sc-391657A sc-391657C sc-391657D | 5 g 25 g 100 g 500 g 1 kg | $20.00 $31.00 $61.00 $219.00 $352.00 | 2 | |
An amino acid that can stabilize the quaternary structure of enzymes like Neuraminidase, potentially enhancing its catalytic activity. | ||||||
Ethylene glycol | 107-21-1 | sc-257515 sc-257515A | 500 ml 1 L | $85.00 $120.00 | 1 | |
A cryoprotectant that can be used to preserve the activity of Neuraminidase during freeze-thaw cycles, indirectly maintaining its functional activity. | ||||||