Protease Inhibitors

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A1276 Amastatin hydrochloride hydrate ≥97% (HPLC) It inhibits cytosolic leucine aminopeptidase (EC.3.4.11.1), microsomal aminopeptidase M (EC.3.4.11.2) and bacterial leucine aminopeptidase (EC.3.4.11.10). It is less effective against aminopeptidase A (EC 3.4.11.7), the enzyme that converts angiotensin II to angiotensin III. Potentiates the CNS effects of vasopressin and oxytocin in vivo.1

Effective concentration: 1-10 μM.
It inhibits cytosolic leucine aminopeptidase (EC.3.4.11.1), microsomal aminopeptidase M (EC.3.4.11.2) and bacterial leucine aminopeptidase (EC.3.4.11.10). It is less effective against aminopeptidase A (EC 3.4.11.7), the enzyme that converts angiotensin II to angiotensin III. Potentiates the CNS effects of vasopressin and oxytocin in vivo.1Effective concentration: 1-10 μM.
A6191 Antipain dihydrochloride from microbial source protease inhibitor Reversible inhibitor of serine/cysteine proteases and some trypsin-like serine proteases. Its action resembles leupeptin; however, its plasmin inhibition is less and its cathepsin A inhibition is more than that observed with leupeptin. Chronic administration of antipain can reduce the frequency of chemically induced transformation in BALB/c-/3T3 cells.1
A6279 Aprotinin from bovine lung saline solution, 3-7 TIU/mg protein Aprotinin is a competitive serine protease inhibitor that forms stable complexes with and blocks the active sites of enzyme. This binding is reversible, and most aprotinin-protease complexes will dissociate at extreme pH levels >10 or <3. Structurally, Aprotinin is a monomeric globular protein derived from bovine lung that consists of 58 amino acids, arranged in a single polypeptide chain with three crosslinking disulfide bridges.
A1153 Aprotinin from bovine lung lyophilized powder, 3-8 TIU/mg solid Aprotinin is a competitive serine protease inhibitor that forms stable complexes with and blocks the active sites of enzyme. This binding is reversible, and most aprotinin-protease complexes will dissociate at extreme pH levels >10 or <3. Structurally, Aprotinin is a monomeric globular protein derived from bovine lung that consists of 58 amino acids, arranged in a single polypeptide chain with three crosslinking disulfide bridges.
E0881 Elastatinal microbial Potent, irreversible elastase inhibitor. Elastatinal is a much stronger inhibitor of elastase from pancreas than from leucocytes.1
E3389 Epiamastatin hydrochloride ≥97% (HPLC) Epimer of amastatin at the 2-position. There are no reports of aminopeptidase inhibition by this epimer; on the contrary, there are suggestions that a 2S-hydroxyl group is important for the stability of an initial collision complex with the enzyme.
H6027 Histatin 5 ≥97% (HPLC) A human salivary peptide that inhibits the protease of Bacteroides gingivalis, as well as clostripain.
The antifungal (Candida, Leishmania) activity of histatin 5 involves penetration of the microbial cell, localization in the mitochondria, and inhibition of F1-F0 ATPase, with rapid depletion of ATP.1
L2884 Leupeptin hemisulfate salt microbial, ≥90% (HPLC) Inhibitor of serine and cysteine proteases. Inhibits plasmin, trypsin, papain, calpain, and cathepsin B. Does not inhibit pepsin, cathepsins A and D, thrombin, or α-chymotrypsin. Effective concentration 10-100 μM. There have been numerous studies using leupeptin to protect against hearing loss caused by acoustic overstimulation or the ototoxic antibiotic gentamicin.1 (Loss of cochlear hair cells is believed to be mediated by calpain.)
L0649 Leupeptin hydrochloride microbial, ≥70% (HPLC) Inhibitor of serine and cysteine proteases. Inhibits plasmin, trypsin, papain, calpain, and cathepsin B. Does not inhibit pepsin, cathepsins A and D, thrombin, or α-chymotrypsin. Effective concentration 10-100 μM. There have been numerous studies using leupeptin to protect against hearing loss caused by acoustic overstimulation or the ototoxic antibiotic gentamicin.1 (Loss of cochlear hair cells is believed to be mediated by calpain.)
L2023 Leupeptin trifluoroacetate salt ≥90% (HPLC), microbial Inhibitor of serine and cysteine proteases. Inhibits plasmin, trypsin, papain, calpain, and cathepsin B. Does not inhibit pepsin, cathepsins A and D, thrombin, or α-chymotrypsin. Effective concentration 10-100 μM. There have been numerous studies using leupeptin to protect against hearing loss caused by acoustic overstimulation or the ototoxic antibiotic gentamicin.1 (Loss of cochlear hair cells is believed to be mediated by calpain.)
P5318 Pepstatin A microbial, ≥90% (HPLC) Pepstatin A is an inhibitor of acid proteases (aspartyl peptidases). It forms a 1:1 complex with proteases such as pepsin, renin, cathepsin D, bovine chymosin, and protease B (Aspergillus niger). The inhibitor is highly selective and does not inhibit thiol proteases, neutral proteases, or serine proteases. Solubilized γ-secretase and retroviral protease are also inhibited by Pepstatin A. It has been used to characterize proteases from several sources.
P4265 Pepstatin A microbial, ≥75% (HPLC) Pepstatin A is an inhibitor of acid proteases (aspartyl peptidases). It forms a 1:1 complex with proteases such as pepsin, renin, cathepsin D, bovine chymosin, and protease B (Aspergillus niger). The inhibitor is highly selective and does not inhibit thiol proteases, neutral proteases, or serine proteases. Solubilized γ-secretase and retroviral protease are also inhibited by Pepstatin A. It has been used to characterize proteases from several sources.