Recombinant Mouse Cathepsin B Protein (His Tag)
Beta LifeScience
SKU/CAT #: BLPSN-0597
Recombinant Mouse Cathepsin B Protein (His Tag)
Beta LifeScience
SKU/CAT #: BLPSN-0597
Collections: Enzymes, Protease, Recombinant proteins
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
Tag | His |
Host Species | Mouse |
Accession | P10605 |
Synonym | CB |
Background | Cathepsin B is a papain-family cysteine protease that is normally located in lysosomes, where it is involved in the turnover of proteins and plays various roles in maintaining the normal metabolism of cells. This protease has been implicated in pathological conditions, e.g., tumor progression and arthritis. In disease conditions, increases in the expression of cathepsin B occur at both the gene and protein levels. Cathepsin B is synthesized as a preproenzyme and the primary pathways for its normal trafficking to the lysosome utilize mannose 6-phosphate receptors (MPRs). Mature cathepsin B has the ability to degrade several extracellular matrix components at both neutral and acidic pH and has been implicated in the progression of several human and rodent tumors progression and arthritis. Cathepsin B expression is increased in many human cancers at the mRNA, protein and activity levels. It is also frequently overexpressed in premalignant lesions, an observation that associates this protease with local invasive stages of cancer. Increased expression of cathepsin B in primary cancers, and especially in preneoplastic lesions, suggests that this enzyme might have pro-apoptotic features. Active cathepsin B is also secreted from tumours, a mechanism likely to be facilitated by lysosomal exocytosis or extracellular processing by surface activators. Cathepsin B is localized to caveolae on the tumour surface, where binding to the annexin II heterotetramer occurs. Thus CTSB is suggested as a tumor marker. Additionally, Cathepsin B can degrade extracellular matrix proteins, such as collagen IV and laminin, and can activate the precursor form of urokinase plasminogen activator (uPA), perhaps thereby initiating an extracellular proteolytic cascade. |
Description | A DNA sequence encoding the mouse CTSB (P10605) (Met 1-Phe 339) was fused with a His tag at the C-terminus. |
Source | HEK293 |
Predicted N Terminal | His 18 |
AA Sequence | Met 1-Phe 339 |
Molecular Weight | The secreted recombinant mouse CTSB (pro form) consists of 333 a.a. and has a predicted molecular mass of 36.6 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rm CTSB is approximately 35-43 kDa due to glycosylation. |
Purity | >95% as determined by SDS-PAGE |
Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method |
Bioactivity | Measured by its ability to cleave the fluorogenic peptide substrate Z-LR-AMC (R&D Systems, Catalog # ES008). The specific activity is >2,000 pmoles/min/ug. |
Formulation | Lyophilized from sterile PBS, pH 7.4. |
Stability | The recombinant proteins are stable for up to 1 year from date of receipt at -70°C. |
Usage | For Research Use Only |
Storage | Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |