protein

Recombinant Human Ubiquitin carboxyl-terminal hydrolase 14

MBS955431

0.05 mg (Mammalian-C

190 USD

Recombinant Protein

Recombinant Human Ubiquitin carboxyl-terminal hydrolase 14

Ubiquitin carboxyl-terminal hydrolase 14

Deubiquitinating enzyme 14; Ubiquitin thioesterase 14; Ubiquitin-specific-processing protease 14

ubiquitin carboxyl-terminal hydrolase 14 isoform b; Ubiquitin carboxyl-terminal hydrolase 14; ubiquitin carboxyl-terminal hydrolase 14; ubiquitin specific peptidase 14 (tRNA-guanine transglycosylase); Deubiquitinating enzyme 14; Ubiquitin thioesterase 14; Ubiquitin-specific-processing protease 14

USP14

USP14; USP14; TGT; TGT

UBP14_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

1-494, Full length

494

MPLYSVTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGV
QPARQKVMVKGGTLKDDDWGNIKIKNGMTLLMMGSADAL
PEEPSAKTVFVEDMTEEQLASAMELPCGLTNLGNTCYMN
ATVQCIRSVPELKDALKRYAGALRASGEMASAQYITAAL
RDLFDSMDKTSSSIPPIILLQFLHMAFPQFAEKGEQGQY
LQQDANECWIQMMRVLQQKLEAIEDDSVKETDSSSASAA
TPSKKKSLIDQFFGVEFETTMKCTESEEEEVTKGKENQL
QLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYI
KSSKISRLPAYLTIQMVRFFYKEKESVNAKVLKDVKFPL
MLDMYELCTPELQEKMVSFRSKFKDLEDKKVNQQPNTSD
KKSSPQKEVKYEPFSFADDIGSNNCGYYDLQAVLTHQGR
SSSSGHYVSWVKRKQDEWIKFDDDKVSIVTPEDILRLSG
GGDWHIAYVLLYGPRRVEIMEEESEQ

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Epigenetics and Nuclear Signaling

Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. Indispensable for synaptic development and function at neuromuscular junctions (NMJs).

tRNA-guanine transglycosylase cDNA from human placenta.Deshpande K.L., Katze J.R. Cloning of human full-length CDSs in BD Creator(TM) system donor vector.Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.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) DNA sequence and analysis of human chromosome 18.Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.Nature 437:551-555(2005) Heil O., Ebert L., Hennig S., Henze S., Radelof U., Schneider D., Korn B. Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport.Reuter T.Y., Medhurst A.L., Waisfisz Q., Zhi Y., Herterich S., Hoehn H., Gross H.J., Joenje H., Hoatlin M.E., Mathew C.G., Huber P.A.Exp. Cell Res. 289:211-221(2003) Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.J. Proteome Res. 7:5167-5176(2008) Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome.Koulich E., Li X., De;Martino G.N.Mol. Biol. Cell 19:1072-1082(2008) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) USP14 inhibits ER-associated degradation via interaction with IRE1alpha.Nagai A., Kadowaki H., Maruyama T., Takeda K., Nishitoh H., Ichijo H.Biochem. Biophys. Res. Commun. 379:995-1000(2009) Deubiquitination of CXCR4 by USP14 is critical for both CXCL12-induced CXCR4 degradation and chemotaxis but not ERK activation.Mines M.A., Goodwin J.S., Limbird L.E., Cui F.F., Fan G.H.J. Biol. Chem. 284:5742-5752(2009) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.Sci. Signal. 2:RA46-RA46(2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.Sci. Signal. 4:RS3-RS3(2011) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14.Hu M., Li P., Song L., Jeffrey P.D., Chenova T.A., Wilkinson K.D., Cohen R.E., Shi Y.EMBO J. 24:3747-3756(2005)

82880645

NP_001032411.1

NM_001037334.1

P54578

60.1kD

This gene encodes a member of the ubiquitin-specific processing (UBP) family of proteases that is a deubiquitinating enzyme (DUB) with His and Cys domains. This protein is located in the cytoplasm and cleaves the ubiquitin moiety from ubiquitin-fused precursors and ubiquitinylated proteins. Mice with a mutation that results in reduced expression of the ortholog of this protein are retarded for growth, develop severe tremors by 2 to 3 weeks of age followed by hindlimb paralysis and death by 6 to 10 weeks of age. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. [provided by RefSeq, Jul 2008]

USP14: Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. Indispensable for synaptic development and function at neuromuscular junctions (NMJs). Homodimer (Potential). Associates with the 26S proteasome. Interacts with FANCC, CXCR4 and ERN1. Belongs to the peptidase C19 family. USP14/UBP6 subfamily. Protein type: EC 3.4.19.12; Ubiquitin conjugating system; Protease; Ubiquitin-specific protease. Chromosomal Location of Human Ortholog: 18p11.32. Cellular Component: cell surface; cytoplasm; cytoplasmic membrane-bound vesicle; plasma membrane; proteasome complex; synapse. Molecular Function: cysteine-type endopeptidase activity; endopeptidase inhibitor activity; protein binding; tRNA guanylyltransferase activity; ubiquitin-specific protease activity. Biological Process: protein deubiquitination; regulation of chemotaxis; synaptic transmission; ubiquitin-dependent protein catabolic process

0.05 mg (Mammalian-Cell)

190 USD

0.05 mg (Baculovirus)

460

0.1 mg (Baculovirus)

750

0.5 mg (E-Coli)

950

0.1 mg (Mammalian-Cell)

1170