CTSF Human, Sf9
Sf9, Baculovirus cells.
CTSF, CATSF, CLN13.
Sterile filtered colorless solution.
Greater than 90.0% as determined by SDS-PAGE.
Description
CTSF produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 474 amino acids (20-484.a.a) and having a molecular mass of 52.5kDa.
CTSF is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Cathepsin F (CTSF), a member of the peptidase C1 family, is a cysteine proteinase belonging to the papain family. These proteinases constitute a significant part of the lysosomal proteolytic system. CTSF exhibits ubiquitous expression, and its gene is located on chromosome 11q13, in proximity to the gene encoding cathepsin W. This proteinase participates in the regular breakdown of proteins. Moreover, CTSF is implicated in certain degradative processes associated with tumor progression, as its expression is elevated in specific cancer cell lines.
Produced in Sf9 Baculovirus cells, CTSF is a single, glycosylated polypeptide chain with a molecular weight of 52.5kDa. It comprises 474 amino acids (20-484.a.a). The protein is expressed with a 6 amino acid His tag at the C-Terminus and purified using proprietary chromatographic methods.
Sterile filtered, colorless solution.
The CTSF protein solution (0.25mg/ml) is supplied in Phosphate buffered saline (pH7.4) with 40% glycerol.
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the protein frozen at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. It is crucial to avoid repeated cycles of freezing and thawing.
Purity exceeds 90.0% as assessed by SDS-PAGE.
The specific activity, defined as the amount of enzyme required to hydrolyze 1 picomole of Z-Phe-Arg-AMC to Z-Phe-Arg and AMC per minute at a pH of 5.0 and a temperature of 37°C, is greater than 5 pmol/min/ug.
CTSF, CATSF, CLN13.
Sf9, Baculovirus cells.
ADLAPAQPRA ASFQAWGPPS PELLAPTRFA LEMFNRGRAA GTRAVLGLVR GRVRRAGQGS LYSLEATLEE PPCNDPMVCR LPVSKKTLLC SFQVLDELGR HVLLRKDCGP VDTKVPGAGE PKSAFTQGSA MISSLSQNHP DNRNETFSSV ISLLNEDPLS QDLPVKMASI FKNFVITYNR TYESKEEARW RLSVFVNNMV RAQKIQALDR GTAQYGVTKF SDLTEEEFRT IYLNTLLRKE PGNKMKQAKS VGDLAPPEWD WRSKGAVTKV KDQGMCGSCW AFSVTGNVEG WFLNQGTLL SLSEQELLDC DKMDKACMGG LPSNAYSAIK NLGGLETEDD YSYQGHMQSC NFSAEKAKVY INDSVELSQN EQKLAAWLAK RGPISVAINA FGMQFYRHGI SRPLRPLCSP WLIDHAVLLV GYGNRSDVPF WAIKNSWGTD WGEKGYYYLH RGSGACGVNT MASSAVVDHH HHHH
Product Science Overview
Cathepsin-F is produced as a single, glycosylated polypeptide chain containing 474 amino acids, with a molecular mass of approximately 52.5 kDa . The recombinant form of Cathepsin-F is often expressed in Sf9 Baculovirus cells, which are derived from the fall armyworm, Spodoptera frugiperda . This recombinant protein includes a 6-amino acid His tag at the C-terminus, which facilitates purification using chromatographic techniques .
Cathepsin-F plays a role in normal protein catabolism and is involved in various degradative processes, including those occurring during tumor progression . It is highly expressed in some cancer cell lines, indicating its potential role in cancer biology . The enzyme exhibits specific activity, defined as the amount of enzyme that hydrolyzes 1 pmole of Z-Phe-Arg-AMC to Z-Phe-Arg and AMC per minute at pH 5.0 at 37°C .
The recombinant Cathepsin-F protein is typically formulated in a phosphate-buffered saline solution (pH 7.4) with 40% glycerol . For short-term storage, it can be kept at 4°C, while for long-term storage, it should be frozen at -20°C. To maintain its stability, it is recommended to add a carrier protein, such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA), and to avoid multiple freeze-thaw cycles .
Cathepsin-F is ubiquitously expressed in various tissues, including the heart, skeletal muscle, brain, testis, and ovary . It has moderate expression levels in the prostate, placenta, liver, and colon, but no detectable expression in peripheral leukocytes and thymus . The enzyme’s activity is optimal at a pH range of 5.2 to 6.8, and it is relatively unstable at cytosolic pH (7.2), with a half-life of approximately 2 minutes . This suggests that Cathepsin-F functions primarily in acidic cellular compartments, such as lysosomes .
Recombinant Cathepsin-F produced in Sf9 cells is used extensively in laboratory research to study its role in protein degradation and its involvement in diseases such as cancer . The enzyme’s activity and stability make it a valuable tool for investigating the mechanisms of lysosomal proteolysis and the development of potential therapeutic interventions targeting cathepsin activity.
