Analytical Data
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Gene name
CTSH
- Application
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Alternative Names
CTSH；CPSB；Pro-cathepsin H
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P09668
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Expression Region
1-335aa
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AA Sequence
MWATLPLLCAGAWLLGVPVCGAAELCVNSLEKFHFKSWMSKHRKTYSTEEYHHRLQTFASNWRKINAHNNGNHTFKMALNQFSDMSFAEIKHKYLWSEPQNCSATKSNYLRGTGPYPPSVDWRKKGNFVSPVKNQGACGSCWTFSTTGALESAIAIATGKMLSLAEQQLVDCAQDFNNHGCQGGLPSQAFEYILYNKGIMGEDTYPYQGKDGYCKFQPGKAIGFVKDVANITIYDEEAMVEAVALYNPVSFAFEVTQDFMMYRTGIYSSTSCHKTPDKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLIERGKNMCGLAACASYPIPLV
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
CTSH, or Cathepsin H, is a lysosomal cysteine protease that plays a critical role in various physiological processes, including protein degradation, antigen processing, and the immune response. Its involvement in several pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders, has sparked significant interest in understanding its mechanisms of action. Research on CTSH, particularly in the context of recombinant protein studies, has gained momentum as scientists aim to elucidate its structure-function relationship and regulatory mechanisms. By producing recombinant CTSH, researchers can investigate its enzymatic activity, substrate specificity, and potential as a therapeutic target. Additionally, recombinant CTSH provides a valuable tool for studying its interactions with inhibitors and other cellular processes, contributing to a deeper understanding of its role in health and disease. This body of research not only aids in characterizing the enzyme but also holds promise for developing novel strategies for disease intervention and therapy, particularly in targeting CTSH-related pathways in diseases where its dysregulation is evident. Thus, the study of recombinant CTSH continues to be a vibrant area of research with implications for both basic science and translational medicine.
