SRP0289
Cathepsin B Active human
recombinant, expressed in FreeStyle™ 293-F cells, ≥90% (SDS-PAGE)
Synonym(s):
APP secretase, CPSB
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About This Item
UNSPSC Code:
12352204
NACRES:
NA.54
biological source
human
recombinant
expressed in FreeStyle™ 293-F cells
Assay
≥90% (SDS-PAGE)
form
aqueous solution
specific activity
≥2228 pmol/min-μg
mol wt
43 kDa
concentration
>1 mg/mL
technique(s)
activity assay: suitable
solubility
water: soluble
suitability
suitable for molecular biology
NCBI accession no.
application(s)
life science and biopharma
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... CTSB(1508)
General description
Research area: Cell signaling. Human cathepsin B (GenBank Accession No. NM_001908), CD33 signal peptide(amino acids 1-16) + Cathepsin B (amino acids 18-339), with C-terminal HIS tag, MW = 43 kDa, expressed in FreeStyle 293-F cells. Cathepsin B is a cysteine protease, found in the lysosome of normal cells and tissues. Cathepsin B active human is encoded by the gene CTSB, located on human chromosome 8p23.1.
Application
Active human cathepsin B is useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling. Active human cathepsin B has been used in a study to assess maturation through proenzyme activation and proteolytic processing. Active human cathepsin B has also been used in a study to prepare a catalytically active version from its precursor expressed in Escherichia coli in the form of inclusion bodies.
Cathepsin B Active human has been used as a supplement in serum free media for the treatment of MDA-MB-231 cell line. It has also been used as a component in low pH buffer for collagen II and complement 3 processing.
Biochem/physiol Actions
Cathepsin B Active human primarily is a preproenzyme, glycosylated on rough endoplasmic reticulum. Processing of procathepsin B to a 31 kDa, single chain active form occurs in the lysosome. It is further processed to double chain form with a 25/26 kDa heavy chain and 5 kDa heavy chain in lysosome. Cathepsin B, functions as an exopeptidase at low pH. At higher pH in endosomes or neutral pH, cathepsin B functions as endopeptidase. Cathepsin B expression is upregulated in malignant tumors and facilitates tumor invasion. Cathepsin B might reduce the production of amyloid-β peptide associated with Alzheimerβs disease. It also plays a key role in neuroprotective functions.
Physical form
Formulated in 40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 3 mM DTT, 20% glycerol, and 200 mM imidazole.
Preparation Note
Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.
Other Notes
One unit is defined as the amount of enzyme that will cleave 1 pmol of substrate per min at 37°C
Legal Information
FreeStyle is a trademark of Invitrogen Corp.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2
Storage Class Code
6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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The dendritic cell MHC II peptidome derives from a variety of processing pathways and includes peptides with a broad spectrum of HLA-DM sensitivity.
Clement CC, et al.
The Journal of Biological Chemistry, 1863(11), jbc-M115 (2016)
Pericellular cathepsin B and malignant progression.
Roshy S, et al.
Cancer Metastasis Reviews, 22(2-3), 271-286 (2003)
L Mach et al.
The Journal of biological chemistry, 269(17), 13030-13035 (1994-04-29)
Recombinant latent human procathepsin B produced in yeast was purified to near homogeneity. The purified recombinant proenzyme is activated in vitro under acidic conditions resulting in rapid conversion into the mature form of the proteinase. Activation as well as proteolytic
Antiamyloidogenic and neuroprotective functions of cathepsin B: implications for Alzheimer's disease.
Mueller-Steiner S, et al.
Neuron, 51(6), 703-714 (2006)
R Kuhelj et al.
European journal of biochemistry, 229(2), 533-539 (1995-04-15)
A cDNA clone encoding human procathepsin B was expressed at a high level in Escherichia coli using a T7 polymerase expression system, resulting in the formation of insoluble cytoplasmic protein aggregates (inclusion bodies). The recombinant product was solubilized and renatured
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