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.
Greater than 95% as determined by SDS-PAGE.
This section provides a brief overview of Cathepsin-Z (CTSZ), including its alternative names, family classification, functions, and relevance to cancer.
This section specifies the composition and concentration of the CTSZ protein solution, including the buffer system and any additives like glycerol.
This part provides guidelines for storing the CTSZ protein solution to maintain its stability, including recommended temperatures and the use of carrier proteins for long-term storage.
This indicates the purity level of the CTSZ protein, determined by SDS-PAGE analysis, which should exceed 95%.
This section describes how the specific activity of CTSZ is measured, outlining the assay conditions, substrate used, and the expected activity level, which is greater than 1,400 pmol/min/ug.
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.
GLYFRRGQTC YRPLRGDGLA PLGRSTYPRP HEYLSPADLP KSWDWRNVDG VNYASITRNQ
HIPQYCGSCW AHASTSAMAD RINIKRKGAW PSTLLSVQNV IDCGNAGSCE GGNDLSVWDY
AHQHGIPDET CNNYQAKDQE CDKFNQCGTC NEFKECHAIR NYTLWRVGDY GSLSGREKMM
AEIYANGPIS CGIMATERLA NYTGGIYAEY QDTTYINHVV SVAGWGISDG TEYWIVRNSW
GEPWGERGWL RIVTSTYKDG KGARYNLAIE EHCTFGDPIV LEHHHHHH
Cathepsin-Z contains a signal sequence, a propeptide, and a mature chain . It exhibits both carboxy-monopeptidase and carboxy-dipeptidase activities, but unlike Cathepsin B, it does not function as an endopeptidase . The enzyme has a very short pro-region that shows no similarity to those of other cathepsins and a three-residue insertion motif that forms a characteristic 'mini loop’ .
Cathepsin-Z is widely expressed in human tissues, suggesting its involvement in normal intracellular protein degradation in various cell types . It is predominantly found in cells of the immune system, such as monocytes, macrophages, and dendritic cells . The enzyme is capable of cleaving regulatory motifs at the C-terminus, affecting the function of targeted molecules .
Cathepsin-Z plays a crucial role in the maturation of dendritic cells, which is essential for the initiation of adaptive immunity . Higher levels of Cathepsin-Z are found in tumor and immune cells of prostate and gastric carcinomas, as well as in macrophages of the gastric mucosa, especially after infection by Helicobacter pylori . This enzyme is also ubiquitously distributed in cancer cell lines and primary tumors from different sources, suggesting its participation in tumor progression .
The recombinant form of Cathepsin-Z (Human, Sf9) is produced using the Sf9 insect cell expression system. This system is commonly used for the production of recombinant proteins due to its ability to perform post-translational modifications similar to those in mammalian cells . The recombinant protein is typically tagged with a His-tag to facilitate purification and is lyophilized for storage .