Caspase-5 Recombinant Protein | CASP5 recombinant protein

Recombinant Human Caspase-5

Cat. Num. AAA949923

• Gene Names: CASP5; ICH-3; ICEREL-III; ICE(rel)III
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Caspase-5; Recombinant Human Caspase-5; ICE(rel)-III; Protease ICH-3; Protease TY; CASP5 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: 137-327aa; Partial(Caspase-5 subunit p20 Chain)
• Sequence: DQKITSVKPLLQIEAGPPESAESTNILKLCPREEFLRLCKKNHDEIYPIKKREDRRRLALIICNTKFDHLPARNGAHYDIVGMKRLLQGLGYTVVDEKNLTARDMESVLRAFAARPEHKSSDSTFLVLMSHGILEGICGTAHKKKKPDVLLYDTIFQIFNNRNCLSLKDKPKVIIVQACRGEKHGELWVRD

• 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 CASP5 recombinant protein

Mediator of programmed cell death (apoptosis).

Product Categories/Family for CASP5 recombinant protein

Cell Biology

References

Identification of a novel exon encoding the amino-terminus of the predominant caspase-5 variants.Eckhart L., Kittel C., Gawlas S., Gruber F., Mildner M., Jilma B., Tschachler E.Biochem. Biophys. Res. Commun. 348:682-688(2006) 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 chromosome 11 DNA sequence and analysis including novel gene identification.Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.Nature 440:497-500(2006) Molecular cloning and pro-apoptotic activity of ICErelII and ICErelIII, members of the ICE/CED-3 family of cysteine proteases.Munday N.A., Vaillancourt J.P., Ali A., Casano F.J., Miller D.K., Molineaux S.M., Yamin T.-T., Yu V.L., Nicholson D.W.J. Biol. Chem. 270:15870-15876(1995) Identification of a cysteine protease closely related to interleukin-1 beta-converting enzyme.Faucheu C., Blanchet A.-M., Collard-Dutilleul V., Lalanne J.-L., Diu-Hercend A.Eur. J. Biochem. 236:207-213(1996) NIEHS SNPs program

NCBI and Uniprot Product Information

• NCBI GI #: 209870071
• NCBI GeneID: 838
• NCBI Accession #: NP_001129581.1
• NCBI GenBank Nucleotide #: NM_001136109.1
• UniProt Accession #: P51878; Q0QVY7; Q0QVY8; Q0QVZ0; Q0QVZ1; Q0QVZ2; Q14DD6; Q1HBJ3; Q6DJV7; B4DKP5
• Molecular Weight: 23.8 kDa
• NCBI Official Full Name: caspase-5 isoform b
• NCBI Official Synonym Full Names: caspase 5
• NCBI Official Symbol: CASP5
• NCBI Official Synonym Symbols: ICH-3; ICEREL-III; ICE(rel)III
• NCBI Protein Information: caspase-5
• UniProt Protein Name: Caspase-5
• Protein Family: Caspase
• UniProt Gene Name: CASP5
• UniProt Synonym Gene Names: ICH3; CASP-5
• UniProt Entry Name: CASP5_HUMAN

NCBI Description

This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. Overexpression of the active form of this enzyme induces apoptosis in fibroblasts. Max, a central component of the Myc/Max/Mad transcription regulation network important for cell growth, differentiation, and apoptosis, is cleaved by this protein; this process requires Fas-mediated dephosphorylation of Max. The expression of this gene is regulated by interferon-gamma and lipopolysaccharide. Alternatively spliced transcript variants have been identified for this gene. [provided by RefSeq, Aug 2010]

Uniprot Description

Mediator of programmed cell death (apoptosis).