CTSZ Mouse, Active
Sf9, Baculovirus cells.
Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.
Description
CTSZ Mouse Recombinant produced in Baculovirus is a single, glycosylated, polypeptide chain containing 292 amino acids (23-306 aa) and having a molecular mass of 32.8kDa.
CTSZ is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Product Specs
Cathepsin-Z (CTSZ), also known as cathepsin X or cathepsin P, is a lysosomal cysteine proteinase belonging to the peptidase C1 family. It exhibits both carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is widely expressed in cancer cell lines and primary tumors and, similar to other members of its family, plays a role in tumor development.
Recombinant Mouse CTSZ, produced in Baculovirus, is a single, glycosylated polypeptide chain consisting of 292 amino acids (23-306 aa). It has a molecular weight of 32.8 kDa. The CTSZ protein is fused to an 8 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
The CTSZ solution is provided at a concentration of 0.5 mg/ml in Phosphate Buffered Saline (pH 7.4) with 10% glycerol.
The specific activity is greater than 3,000 pmol/min/µg. One unit is defined as the amount of enzyme that catalyzes the conversion of 1 picomole of Mca-PLGL-Dpa-AR-NH2 to MCA-Pro-Leu-OH per minute at a pH of 3.5 and a temperature of 25°C.
Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.
Sf9, Baculovirus cells.
ARARLYFRSG QTCYHPIRGD QLALLGRRTY PRPHEYLSPA DLPKNWDWRN VNGVNYASVT
RNQHIPQYCG SCWAHGSTSA MADRINIKRK GAWPSILLSV QNVIDCGNAG SCEGGNDLPV
WEYAHKHGIP DETCNNYQAK DQDCDKFNQC GTCTEFKECH TIQNYTLWRV GDYGSLSGRE
KMMAEIYANG PISCGIMATE MMSNYTGGIY AEHQDQAVIN HIISVAGWGV SNDGIEYWIV
RNSWGEPWGE KGWMRIVTST YKGGTGDSYN LAIESACTFG DPIVLEHHHH HH
Product Science Overview
Cathepsin-Z is synthesized as an inactive zymogen and undergoes proteolytic processing to become active. The active form of Cathepsin-Z has a molecular weight of approximately 33.2 kDa, although it may appear as 38 kDa on SDS-PAGE due to glycosylation . It is widely expressed in various tissues, including immune cells such as monocytes, macrophages, and dendritic cells .
Cathepsin-Z exhibits both mono- and di-peptidase activities, primarily at its C-terminus. Unlike other cathepsins, it does not function as an endopeptidase . This enzyme is involved in the degradation of intracellular proteins, playing a significant role in normal cellular processes. It is capable of cleaving regulatory motifs at the C-terminus, thereby affecting the function of targeted molecules .
Cathepsin-Z is implicated in several physiological and pathological processes:
- Immune System: It is predominantly found in immune cells and is involved in the maturation of dendritic cells, which are crucial for initiating adaptive immunity .
- Cancer: Higher levels of Cathepsin-Z are observed in tumor and immune cells of prostate and gastric carcinomas. It is also present in macrophages of gastric mucosa, especially after infection by Helicobacter pylori. This suggests a role in tumor progression and immune response to infections .
- Neurodegenerative Diseases: Cathepsin-Z, along with other cysteine cathepsins, is involved in neurodegenerative diseases such as Alzheimer’s, Parkinson’s, and Huntington’s diseases. These proteases participate in the degradation of extracellular matrix components, contributing to disease progression .
Recombinant Mouse Cathepsin-Z is produced using HEK293 cells, ensuring high purity and activity. The recombinant protein is typically lyophilized from a sterile PBS solution and can be reconstituted for experimental use. It is measured by its ability to cleave specific fluorogenic peptide substrates, with a specific activity of 1,200 pmoles/min/μg .
