Cathepsin F Recombinant Protein | CTSF recombinant protein

Recombinant Human Cathepsin F protein

Cat. Num. AAA719379

• Gene Names: CTSF; CATSF; CLN13
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Cathepsin F; Recombinant Human Cathepsin F protein; CTSF recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 273-484aa; partial
• Sequence: PEWDWRSKGAVTKVKDQGMCGSCWAFSVTGNVEGQWFLNQGTLLSLSEQELLDCDKMDKACMGGLPSNAYSAIKNLGGLETEDDYSYQGHMQSCNFSAEKAKVYINDSVELSQNEQKLAAWLAKRGPISVAINAFGMQFYRHGISRPLRPLCSPWLIDHAVLLVGYGNRSDVPFWAIKNSWGTDWGEKGYYYLHRGSGACGVNTMASSAVVD

• Production Note: Special Offer: The E Coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Colihost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to [email protected] for more details.
• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for CTSF recombinant protein

Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.

Product Categories/Family for CTSF recombinant protein

Immunology

References

Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain.Santamaria I., Velasco G., Pendas A.M., Paz A., Lopez-Otin C.J. Biol. Chem. 274:13800-13809(1999) Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen.Naegler D.K., Sulea T., Menard R.Biochem. Biophys. Res. Commun. 257:313-318(1999) The human cathepsin F gene -- a fusion product between an ancestral cathepsin and cystatin gene.Wex T., Wex H., Broemme D.Biol. Chem. 380:1439-1442(1999) Human cathepsins F and W a new subgroup of cathepsins.Wex T., Levy B., Wex H., Bromme D.Biochem. Biophys. Res. Commun. 259:401-407(1999) Cathepsin F, a novel cysteine protease with an extremely long propeptide.Deussing J., Tisljar K., Papazoglou A., Peters C. Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization.Wang B., Shi G.-P., Yao P.M., Li Z., Chapman H.A., Broemme D.J. Biol. Chem. 273:32000-32008(1998) The full-ORF clone resource of the German cDNA consortium.Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.BMC Genomics 8:399-399(2007) Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.J. Proteome Res. 8:651-661(2009) The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators.Somoza J.R., Palmer J.T., Ho J.D.J. Mol. Biol. 322:559-568(2002) Cathepsin F mutations cause Type B Kufs disease, an adult-onset neuronal ceroid lipofuscinosis.Smith K.R., Dahl H.H., Canafoglia L., Andermann E., Damiano J., Morbin M., Bruni A.C., Giaccone G., Cossette P., Saftig P., Groetzinger J., Schwake M., Andermann F., Staropoli J.F., Sims K.B., Mole S.E., Franceschetti S., Alexander N.A., Cooper J.D., Chapman H.A., Carpenter S., Berkovic S.F., Bahlo M.Hum. Mol. Genet. 22:1417-1423(2013)

NCBI and Uniprot Product Information

• NCBI GI #: 6042196
• NCBI GeneID: 8722
• NCBI Accession #: NP_003784.2
• NCBI GenBank Nucleotide #: NM_003793.3
• UniProt Accession #: Q9UBX1; O95240; Q9NSU4; Q9UKQ5; B2R964
• Molecular Weight: 27.4 kDa
• NCBI Official Full Name: cathepsin F
• NCBI Official Synonym Full Names: cathepsin F
• NCBI Official Symbol: CTSF
• NCBI Official Synonym Symbols: CATSF; CLN13
• NCBI Protein Information: cathepsin F
• UniProt Protein Name: Cathepsin F
• Protein Family: Cathepsin
• UniProt Gene Name: CTSF
• UniProt Synonym Gene Names: CATSF
• UniProt Entry Name: CATF_HUMAN

NCBI Description

Cathepsins are papain family cysteine proteinases that represent a major component of the lysosomal proteolytic system. Cathepsins generally contain a signal sequence, followed by a propeptide and then a catalytically active mature region. The very long (251 amino acid residues) proregion of the cathepsin F precursor contains a C-terminal domain similar to the pro-segment of cathepsin L-like enzymes, a 50-residue flexible linker peptide, and an N-terminal domain predicted to adopt a cystatin-like fold. The cathepsin F proregion is unique within the papain family cysteine proteases in that it contains this additional N-terminal segment predicted to share structural similarities with cysteine protease inhibitors of the cystatin superfamily. This cystatin-like domain contains some of the elements known to be important for inhibitory activity. CTSF encodes a predicted protein of 484 amino acids which contains a 19 residue signal peptide. Cathepsin F contains five potential N-glycosylation sites, and it may be targeted to the endosomal/lysosomal compartment via the mannose 6-phosphate receptor pathway. The cathepsin F gene is ubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. [provided by RefSeq, Jul 2008]

Uniprot Description

CTSF: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis. Belongs to the peptidase C1 family.

Protein type: EC 3.4.22.41; Protease

Chromosomal Location of Human Ortholog: 11q13

Cellular Component: extracellular space; lysosomal lumen; lysosome

Molecular Function: cysteine-type endopeptidase activity

Biological Process: antigen processing and presentation of exogenous peptide antigen via MHC class II; proteolysis; proteolysis involved in cellular protein catabolic process

Disease: Ceroid Lipofuscinosis, Neuronal, 13