Date published: 2026-4-24

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Meprin A alpha Inhibitors

Santa Cruz Biotechnology now offers a broad range of Meprin A α Inhibitors for use in various applications. Meprin A α is a metalloprotease enzyme that plays a critical role in the proteolytic processing of extracellular matrix proteins, peptides, and cytokines. It is involved in various physiological processes, including tissue remodeling, inflammation, and the regulation of cell signaling pathways. Meprin A α has been implicated in pathological conditions such as fibrosis, cancer, and inflammatory diseases, making it a significant target for scientific research. Meprin A α Inhibitors are essential tools for researchers seeking to understand the enzyme's function and its impact on biological systems. By inhibiting Meprin A α, scientists can study the downstream effects on extracellular matrix composition, cytokine activity, and cellular behavior, providing insights into the mechanisms underlying disease progression and tissue homeostasis. These inhibitors are widely used in biochemical assays, cell culture studies, and animal models to investigate the role of Meprin A α in health and disease. Additionally, Meprin A α Inhibitors are valuable in the development of scientific strategies aimed at modulating protease activity to treat conditions associated with excessive proteolysis or abnormal extracellular matrix degradation. The availability of these inhibitors has significantly advanced research in fields such as biochemistry, molecular biology, and pathology, offering crucial tools for exploring the complex interactions between proteases and their substrates in various biological contexts. View detailed information on our available Meprin A α Inhibitors by clicking on the product name.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

TAPI-0

143457-40-3sc-203410
sc-203410A
1 mg
5 mg
$269.00
$1248.00
15
(2)

TAPI-0, functioning as a Meprin A alpha, showcases remarkable reactivity as an acid halide, primarily through its selective electrophilic nature. The compound's unique ability to form transient complexes with nucleophiles accelerates reaction kinetics, facilitating rapid hydrolysis. Its distinct conformational flexibility allows for varied molecular interactions, while its solvation dynamics contribute to its stability in diverse environments, making it a fascinating subject for further exploration in chemical reactivity.

Phosphoramidon

119942-99-3sc-201283
sc-201283A
5 mg
25 mg
$199.00
$632.00
8
(1)

A competitive inhibitor that binds directly to the active site of Meprin Aα, chelating the metal ion, and preventing substrate binding.

1,10-Phenanthroline

66-71-7sc-255888
sc-255888A
2.5 g
5 g
$23.00
$32.00
(0)

It chelates zinc in the active site of Meprin Aα, altering its structure and making it unavailable for substrate interaction.

Batimastat

130370-60-4sc-203833
sc-203833A
1 mg
10 mg
$179.00
$377.00
24
(1)

A hydroxamate-based inhibitor that forms a tight bond with the zinc ion in the active site of Meprin Aα, preventing substrate binding and cleavage.

Marimastat

154039-60-8sc-202223
sc-202223A
sc-202223B
sc-202223C
sc-202223E
5 mg
10 mg
25 mg
50 mg
400 mg
$168.00
$218.00
$404.00
$629.00
$4900.00
19
(1)

Interacts with the active site of Meprin Aα, chelating the zinc ion, and hence preventing substrate-enzyme interaction.

GM 6001

142880-36-2sc-203979
sc-203979A
1 mg
5 mg
$77.00
$270.00
55
(1)

Another hydroxamate-based molecule; it chelates the zinc ion in the Meprin Aα active site, inhibiting the proteolytic activity of the enzyme.

TAPI-2

187034-31-7sc-205851
sc-205851A
1 mg
5 mg
$286.00
$1019.00
15
(1)

Binds to Meprin Aα and chelates the metal ion in the active site, restricting its proteolytic function.

E-64

66701-25-5sc-201276
sc-201276A
sc-201276B
5 mg
25 mg
250 mg
$281.00
$947.00
$1574.00
14
(0)

While E-64 primarily targets cysteine proteases, it can indirectly modulate the environment of Meprin Aα, affecting its function.

o-Phenanthroline monohydrate

5144-89-8sc-202256
sc-202256A
1 g
25 g
$43.00
$188.00
1
(1)

Acts as a metal chelator, binding to the zinc in Meprin Aα, leading to enzyme structural changes and diminished activity