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Human Cathepsin H
Native whole molecule & biologically active
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Proteins Synonyms: CatH, CTSH Biological Activity: > 1 unit/mg protein Source: Human Liver Purity: ≥ 90% by SDS-PAGE Physical State: Frozen in 20 mM Na Acetate, pH 4.5, with 1 mM EDTA and 100mM NaCl Manufacturer: |
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Athens Research & Technology
Produktdetails
Synonyms
CatH, CTSH
Description of Human Cathepsin H
Human Cathepsin H is a 28 kDa protein. Cathepsin H (CatH) is a lysosomal cysteine protease distinguished by its unique dual aminopeptidase and endopeptidase activities. Unlike other cathepsins, it includes a disulfide-linked mini-chain that anchors substrate N-termini via electrostatic interactions, enabling sequential cleavage of N-terminal basic residues (Arg/Lys). This exopeptidase function, optimal at neutral pH, facilitates its role in extracellular spaces, while its endopeptidase activity at acidic pH (4.5–5.5) supports lysosomal protein degradation. Clinically, CatH overexpression correlates with aggressive tumor phenotypes. In colorectal cancer, CatH activity is elevated promoting metastasis via extracellular matrix remodeling. Serum CatH levels >45 ng/mL serve as a prognostic marker for melanoma metastasis and reduced survival. Conversely, decreased CatH in head/neck squamous carcinomas and polycystic kidney disease suggests tissue-specific regulatory roles. In Alzheimer’s disease, CatH contributes to amyloid-β plaque formation by cleaving tau and amyloid precursor proteins, while in Parkinson’s models, it degrades α-synuclein aggregates. Therapeutically, CatH’s role in neuropeptide processing (e.g., enkephalin and galanin biosynthesis) highlights its potential in pain management and neurodegenerative therapies. Inhibitors targeting its active site (e.g., E-64) reduce tumor invasion in preclinical models, while pH-selective compounds (Z-Arg-NHMec) spare lysosomal functions. Diagnostic applications leverage its elevated expression in gliomas and breast cancers for early detection and stratification. These multifunctional roles position CatH as a critical node in both lysosomal proteostasis and disease pathogenesis.
Source
Prepared from liver shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA-required tests.
Biological Activity
> 1 unit/mg protein. One unit is defined as the amount of enzyme that hydrolyzes 1 µmol of L-arginine-beta-napthylamide per minute at 40 °C using 75 mM potassium phosphate, pH 6.8, with 1 mM EDTA and 3 mM cysteine as the activation buffer.
Storage
For long term, store Human Cathepsin H at ≤ -80°C.
Applications
Cancer, Alzheimer's, Parkinson's, In Vitro Diagnostic.
Citations/Publications
Lambeth, T. R., et al., (2021), 'Proteolysis of Amyloid β by Lysosomal Enzymes as a Function of Fibril Morphology', ACS Omega, 6: pp 31520−31527. Available at:https://doi.org/10.1021/acsomega.1c03915
NCBI: https://www.ncbi.nlm.nih.gov/protein/P09668
Shipped with dry ice
Gel Scan of Human Cathepsin H
| Fig. 1: SDS-PAGE Gel |
Usage: For research use only. Not for use in diagnostic or therapeutic procedures. Not for human use.
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Payment Methods
Paying by bank transfer
