High Quality Protease Inhibitors

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Proteolytic cleavage of peptide bonds is one of the most important mechanisms affecting the properties of proteins. Proteases are ubiquitously distributed in all tissues and biological fluids. They are involved in a multitude of physiological processes ranging from functional activation or inactivation of proteins to their complete dissolution to simple amino acids.

Small molecule inhibitors offer a powerful approach to identify and study the involvement of proteases in both normal physiological and pathological processes both in cell culture in vitro and in animals in vivo. Calbiochem® provides high quality small molecules that potently inhibit a broad-spectrum of proteases, which have been cited in numerous peer-reviewed publications.



Calpain Inhibitors

Calpains belong to a family of calcium-dependent thiol-proteases that proteolyze a wide variety of cytoskeletal, membrane associated, and regulatory proteins. Over-expression of calpains has been positively linked to both acute and chronic neurodegenerative processes including ischemia, trauma, and Alzheimer’s disease. Calpain proteolysis is usually the late-stage common pathway towards cell death induced by excitotoxic compounds; hence, a selective inhibition of calpains to limit neuronal damage appears to be a viable therapeutic measure ...


Collagenase Inhibitors

Mammalian collagenases belong to the family of metalloproteinases that specifically cleave collagen. Collagenases are produced by macrophages, fibroblasts, and keratinocytes that are involved in the wound-healing process. However, in patients with chronic non-healing wounds and ulcers, there may be impairment of endogenous collagenase production leading to insufficient removal of dead tissue. Collagenases also play an important role in separating cells from their anchors. They dissolve desmosomes and thereby enable cells to migrate on a matrix of fibronectin. Fibroblast migration also requires these proteases to enable fibroblasts to move within the wound ...


Matrix Metalloproteinase (MMP) Inhibitors

The proteolytic degradation of the extracellular matrix (ECM) by tumor cells requires the action of highly specialized MMPs that are expressed in cell- or tissue-specific patterns. MMPs also play an important role in wound healing, angiogenesis, embryogenesis, and in pathological processes such as tumor invasion and metastasis. A major control point in the regulation of active enzyme is inhibition of the active form by the TIMP family of inhibitors (21-28 kDa). TIMPs regulate the function of MMPs either by inhibiting active MMPs or by controlling their activation process ...


Protease Inhibitors

Protease inhibitors offer a powerful approach to identify and study the involvement of proteases in both normal physiological and pathological processes both in cell culture in vitro and in animals in vivo.


Proteasome and Ubiquitination Pathway Inhibitors

Proteasomes are large multi-subunit complexes, localized in the nucleus and cytosol that selectively degrade intracellular proteins. A protein marked for degradation is covalently attached to multiple molecules of ubiquitin (Ubq). Several distinct groups of compounds, designed to act as selective proteasome inhibitors, have helped immensely in understanding the biological role and importance of the ubiquitin-proteasome pathway. These compounds are designed to block proteasome function in cancer cells without significantly affecting biological processes in the normal cell ...

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