Obp1a Activators
Obp1a Activators are a class of chemical compounds that can engage with the Obp1a protein to enhance its natural function of binding odorants. These activators include various ions that serve as cofactors or allosteric modulators, as well as organic molecules that can alter the protein's conformation and binding properties. The primary mechanism by which these activators exert their influence is through direct interaction with the protein, resulting in structural changes that either stabilize its active form or increase its affinity for odorants.
Chemical activators such as cyclodextrins are particularly interesting as they form inclusion complexes with odorants, potentially making them more accessible to Obp1a. Other organic molecules like cinnamaldehyde, eugenol, and menthol may bind to different sites on the protein, inducing conformational changes that in turn might improve Obp1a's ability to interact with its ligands. Metal ions are also critical, as they can modulate the protein's structure and dynamics. These various interactions underline the diversity of mechanisms through which Obp1a's function can be modulated without involving complex biological materials or pathways.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
β-Cyclodextrin | 7585-39-9 | sc-204430 sc-204430A | 25 g 500 g | $59.00 $527.00 | 3 | |
Cyclodextrins are cyclic oligosaccharides that have the ability to form inclusion complexes with various molecules, potentially enhancing the solubility and stability of odorants, thus facilitating their interaction with Odorant Binding Protein 1A (Obp1a). | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
Zinc ions can act as allosteric modulators of protein function. By binding to specific sites on Obp1a, they may induce conformational changes that enhance the protein's ability to bind odorants. | ||||||
Copper | 7440-50-8 | sc-211129 | 100 g | $50.00 | ||
Similar to zinc, copper ions can bind to proteins and influence their structure and function. Their interaction with Obp1a might increase its affinity for specific odorants or stabilize its active form. | ||||||
Calcium | 7440-70-2 | sc-252536 | 5 g | $209.00 | ||
Calcium ions play a significant role in modulating protein interactions and function. By binding to Obp1a, they may alter its conformation and thereby modulate its odorant binding activity. | ||||||
Sodium benzoate | 532-32-1 | sc-251009 | 250 g | $21.00 | ||
Sodium benzoate is a chemical preservative that, at certain concentrations, may influence protein conformation and stability, potentially affecting Obp1a and its ability to bind odorants. | ||||||
Cinnamic Aldehyde | 104-55-2 | sc-294033 sc-294033A | 100 g 500 g | $102.00 $224.00 | ||
Cinnamaldehyde can bind to and modulate the function of various proteins. Its interaction with Obp1a may influence the binding dynamics between the protein and odorants. | ||||||
Eugenol | 97-53-0 | sc-203043 sc-203043A sc-203043B | 1 g 100 g 500 g | $31.00 $61.00 $214.00 | 2 | |
Eugenol, a compound found in essential oils, may interact with proteins such as Obp1a, possibly altering their binding properties or stabilizing the protein structure to improve odorant binding. | ||||||
(±)-Menthol | 89-78-1 | sc-250299 sc-250299A | 100 g 250 g | $38.00 $67.00 | ||
Menthol is known to interact with lipid membranes and proteins. It may influence Obp1a's structure or its interaction with odorants, thus serving as a modulator of its activity. | ||||||
Salicylic acid | 69-72-7 | sc-203374 sc-203374A sc-203374B | 100 g 500 g 1 kg | $46.00 $92.00 $117.00 | 3 | |
Salicylic acid may interact with odorant binding proteins like Obp1a, potentially changing their conformation and enhancing their ability to bind odorants. | ||||||
Citric Acid, Anhydrous | 77-92-9 | sc-211113 sc-211113A sc-211113B sc-211113C sc-211113D | 500 g 1 kg 5 kg 10 kg 25 kg | $49.00 $108.00 $142.00 $243.00 $586.00 | 1 | |
Citric acid can chelate metal ions and may influence protein function and stability. By modulating the microenvironment of Obp1a, it could enhance its binding activity with odorants. | ||||||