Cathepsin B Recombinant Protein | CTSB recombinant protein

Recombinant Human Cathepsin B

Cat. Num. AAA717185

• Gene Names: CTSB; APPS; CPSB
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Cathepsin B; Recombinant Human Cathepsin B; APP secretase; APPS; Cathepsin B1; CTSB recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 82-333aa; Partial
• Sequence: ASFDAREQWPQCPTIKEIRDQGSCGSCWAFGAVEAISDRICIHTNAHVSVEVSAEDLLTCCGSMCGDGCNGGYPAEAWNFWTRKGLVSGGLYESHVGCRPYSIPPCEHHVNGSRPPCTGEGDTPKCSKICEPGYSPTYKQDKHYGYNSYSVSNSEKDIMAEIYKNGPVEGAFSVYSDFLLYKSGVYQHVTGEMMGGHAIRILGWGVENGTPYWLVANSWNTDWGDNGFFKILRGQDHCGIESEVVAGIPRTD
• Sequence Length: 333

• 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 CTSB 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 CTSB recombinant protein

Neuroscience

References

Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs.Chan S.J., San Segundo B., McCormick M.B., Steiner D.F.Proc. Natl. Acad. Sci. U.S.A. 83:7721-7725(1986) Human gastric adenocarcinoma cathepsin B isolation and sequencing of full-length cDNAs and polymorphisms of the gene.Cao L., Taggart R.T., Berquin I.M., Moin K., Fong D., Sloane B.F.Gene 139:163-169(1994) 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) Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries.Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.DNA Res. 12:117-126(2005)

NCBI and Uniprot Product Information

• NCBI GI #: 4503139
• NCBI GeneID: 1508
• NCBI Accession #: NP_001899.1
• NCBI GenBank Nucleotide #: NM_001908.4
• UniProt Accession #: P07858; Q503A6; Q96D87; B3KQR5; B3KRR5
• Molecular Weight: 54.6 kDa
• NCBI Official Full Name: cathepsin B isoform 1 preproprotein
• NCBI Official Synonym Full Names: cathepsin B
• NCBI Official Symbol: CTSB
• NCBI Official Synonym Symbols: APPS; CPSB
• NCBI Protein Information: cathepsin B
• UniProt Protein Name: Cathepsin B
• Protein Family: Cathepsin
• UniProt Gene Name: CTSB
• UniProt Synonym Gene Names: CPSB; APPS
• UniProt Entry Name: CATB_HUMAN

NCBI Description

This gene encodes a member of the C1 family of peptidases. Alternative splicing of this gene results in multiple transcript variants. At least one of these variants encodes a preproprotein that is proteolytically processed to generate multiple protein products. These products include the cathepsin B light and heavy chains, which can dimerize to form the double chain form of the enzyme. This enzyme is a lysosomal cysteine protease with both endopeptidase and exopeptidase activity that may play a role in protein turnover. It is also known as amyloid precursor protein secretase and is involved in the proteolytic processing of amyloid precursor protein (APP). Incomplete proteolytic processing of APP has been suggested to be a causative factor in Alzheimer's disease, the most common cause of dementia. Overexpression of the encoded protein has been associated with esophageal adenocarcinoma and other tumors. Multiple pseudogenes of this gene have been identified. [provided by RefSeq, Nov 2015]

Uniprot Description

CTSB: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis. Dimer of a heavy chain and a light chain cross-linked by a disulfide bond. Interacts with SRPX2. Belongs to the peptidase C1 family.

Protein type: Motility/polarity/chemotaxis; Autophagy; Protease; EC 3.4.22.1

Chromosomal Location of Human Ortholog: 8p22

Cellular Component: apical plasma membrane; caveola; external side of plasma membrane; extracellular region; extracellular space; intracellular; intracellular membrane-bound organelle; lysosome; melanosome; mitochondrion; nucleolus; perinuclear region of cytoplasm; sarcolemma

Molecular Function: collagen binding; cysteine-type endopeptidase activity; cysteine-type peptidase activity; kininogen binding; peptidase activity; peptide binding; protein binding; protein self-association; proteoglycan binding

Biological Process: autophagy; collagen catabolic process; decidualization; entry of virus into host cell; epithelial cell differentiation; extracellular matrix disassembly; extracellular matrix organization and biogenesis; innate immune response; proteolysis; proteolysis involved in cellular protein catabolic process; regulation of apoptosis; regulation of catalytic activity; response to amine stimulus; response to ethanol; response to glucose stimulus; response to organic cyclic substance; response to peptide hormone stimulus; response to wounding; skeletal muscle development; spermatogenesis; toll-like receptor signaling pathway