Murinoglobulin 2 Activators, as a chemical class, are not well-defined due to the predictive nature of the protein's function and the lack of specific, direct chemical activators. The chemicals listed are indirect activators that influence the cellular environment, which may enhance the protein's natural inhibitory activity on proteases. These compounds typically function by preserving the cellular redox state, chelating necessary cofactors for proteolytic enzymes, or directly inhibiting various proteases that could compete with or degrade the substrates of murinoglobulin 2. Each of these compounds plays a distinctive role in altering the proteolytic balance within the extracellular space where murinoglobulin 2 is located. For instance, antioxidants like glutathione, ascorbic acid, and methionine help maintain a cellular milieu that is conducive to the proper function of endogenous protease inhibitors. This environment supports the stability and activity of proteins such as murinoglobulin 2 by preventing oxidative modifications that could potentially affect their structure and function. By maintaining a reduced state, these antioxidants may indirectly enhance the ability of murinoglobulin 2 to perform its role in the negative regulation of proteolytic enzymes, thereby stabilizing the extracellular matrix and preventing unwanted protease activity.
Activating a protein like murinoglobulin 2, which is hypothesized to have endopeptidase inhibitor activity, typically involves complex biological interactions that are not easily replicated or influenced by simple chemical compounds alone. Activation often involves specific alterations in gene expression, protein-protein interactions, or post-translational modifications, which are typically regulated within biological systems. In the absence of specific activators, researchers might look to the general mechanisms that regulate protease activity or endopeptidase inhibitors, such as changes in pH, ionic strength, or the presence of small molecule inhibitors that can indirectly affect the function of murinoglobulin 2 by altering the activity of the proteases themselves.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
N-Acetyl-L-cysteine | 616-91-1 | sc-202232 sc-202232A sc-202232C sc-202232B | 5 g 25 g 1 kg 100 g | $33.00 $73.00 $265.00 $112.00 | 34 | |
This mucolytic agent replenishes intracellular levels of the natural antioxidant glutathione and influences various molecular pathways. By modulating oxidative stress and inflammatory responses, it can indirectly affect the regulatory proteins involved in protease inhibition. | ||||||
Phenylmethylsulfonyl Fluoride | 329-98-6 | sc-3597 sc-3597A | 1 g 100 g | $50.00 $683.00 | 92 | |
PMSF is a serine protease inhibitor that irreversibly inactivates serine proteases by sulfonylation of the serine residue in the active site. Because it targets protease activity, it may indirectly enhance the activity of proteins that inhibit endopeptidases like murinoglobulin 2 by reducing overall protease activity in the environment. | ||||||
1,10-Phenanthroline | 66-71-7 | sc-255888 sc-255888A | 2.5 g 5 g | $23.00 $31.00 | ||
This metalloprotease inhibitor binds to metal ions required for the catalytic activity of certain metalloproteases. Indirectly, it may support the function of murinoglobulin 2 by reducing the activity of competing proteases. | ||||||
E-64 | 66701-25-5 | sc-201276 sc-201276A sc-201276B | 5 mg 25 mg 250 mg | $275.00 $928.00 $1543.00 | 14 | |
As a potent, irreversible cysteine protease inhibitor, E-64 can indirectly increase the functional activity of murinoglobulin 2 by reducing the competitive degradation of peptides, potentially allowing murinoglobulin 2 to be more effective at its site of action. | ||||||
Leupeptin hemisulfate | 103476-89-7 | sc-295358 sc-295358A sc-295358D sc-295358E sc-295358B sc-295358C | 5 mg 25 mg 50 mg 100 mg 500 mg 10 mg | $72.00 $145.00 $265.00 $489.00 $1399.00 $99.00 | 19 | |
Leupeptin is an inhibitor of serine and cysteine proteases that can indirectly support the activity of endopeptidase inhibitors such as murinoglobulin 2 by suppressing the activity of these classes of proteases in the environment. | ||||||
Aprotinin | 9087-70-1 | sc-3595 sc-3595A sc-3595B | 10 mg 100 mg 1 g | $110.00 $400.00 $1615.00 | 51 | |
A protease inhibitor with a broad spectrum of activity, particularly against serine proteases. By inhibiting these enzymes, aprotinin might indirectly preserve the inhibitory function of proteins like murinoglobulin 2 in regulating protease activity. | ||||||
Allopurinol | 315-30-0 | sc-207272 | 25 g | $128.00 | ||
While primarily known for its effect on xanthine oxidase, allopurinol and its metabolites also have an impact on the cellular redox state, which could affect the regulation of protease activity and indirectly support the function of protease inhibitors like murinoglobulin 2. | ||||||
L-Cysteine | 52-90-4 | sc-286072 sc-286072A sc-286072B sc-286072C sc-286072D | 25 g 100 g 500 g 5 kg 10 kg | $50.00 $110.00 $440.00 $1128.00 $2135.00 | 1 | |
As a precursor to glutathione, L-cysteine contributes to the antioxidant defense system, which may indirectly support the functional activity of murinoglobulin 2 by maintaining a reduced environment that is conducive to the proper folding and stability of protease inhibitors. | ||||||
L-Ascorbic acid, free acid | 50-81-7 | sc-202686 | 100 g | $45.00 | 5 | |
As an antioxidant, ascorbic acid can reduce oxidative stress, which has been implicated in the modulation of protease activities. It may indirectly contribute to the regulatory role of murinoglobulin 2 by maintaining a cellular environment that favors protease inhibition. | ||||||
L-Methionine | 63-68-3 | sc-394076 sc-394076A sc-394076B sc-394076C sc-394076D sc-394076E | 25 g 100 g 250 g 1 kg 5 kg 10 kg | $33.00 $36.00 $56.00 $148.00 $566.00 $1081.00 | ||
Methionine acts as an antioxidant and a precursor of glutathione. It could indirectly support the function of murinoglobulin 2 by contributing to the maintenance of a cellular environment that prevents oxidative damage to proteins, including protease inhibitors. | ||||||