Clusterin Recombinant Protein | CLU recombinant protein

Recombinant Human Clusterin

Cat. Num. AAA1265506

• Gene Names: CLU; CLI; AAG4; APOJ; CLU1; CLU2; KUB1; SGP2; APO-J; SGP-2; SP-40; TRPM2; TRPM-2; NA1/NA2
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Clusterin; Recombinant Human Clusterin; Aging-associated gene 4 protein; Apolipoprotein J; Apo-J; Complement cytolysis inhibitor; CLI; Complement-associated protein SP-40; 40; Ku70-binding protein 1; NA1/NA2; Testosterone-repressed prostate message 2; TRPM-2; CLU 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: 23-224aa; Partial
• Sequence: DQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLIEKTNEERKTLLSNLEEAKKKKEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHMLDVMQDHFSRASSIIDELFQDRFFTREPQDTYHYLPFSLPHRRPHFFFPKSR
• Sequence Length: 224

• 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 CLU recombinant protein

Isoform 1 functions as extracellular chaperone that prevents aggregation of nonnative proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. Secreted isoform 1 protects cells against apoptosis and against cytolysis by complent. Intracellular isoforms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity. Nuclear isoforms promote apoptosis. Mitochondrial isoforms suppress BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis. Plays a role in the regulation of cell proliferation

Product Categories/Family for CLU recombinant protein

Apoptosis

References

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Thromb. 11:645-652(1991) Purification and characterization of apolipoprotein J.de Silva H., Stuart W.D., Park Y.B., Mao S.J.T., Gil C.M., Wetterau J.R., Busch S.J., Harmony J.A.K.J. Biol. Chem. 265:14292-14297(1990) The cerebrospinal-fluid soluble form of Alzheimer's amyloid beta is complexed to SP-40,40 (apolipoprotein J) , an inhibitor of the complement membrane-attack complex.Ghiso J., Matsubara E., Koudinov A., Choi-Miura N.-H., Tomita M., Wisniewski T., Frangione B.Biochem. J. 293:27-30(1993) A serum protein SP40,40 modulates the formation of membrane attack complex of complement on erythrocytes.Choi N.H., Mazda T., Tomita M.Mol. Immunol. 26:835-840(1989) HDL particle associated proteins in plasma and cerebrospinal fluid identification and partial sequencing.Hochstrasser A.-C., James R.W., Martin B.M., Harrington M., Hochstrasser D.F., Pometta D., Merril C.R.Appl. Theor. Electrophor. 1:73-76(1988) Apolipoprotein J structure and tissue distribution.de Silva H.V., Harmony J.A.K., Stuart W.D., Gil C.M., Robbins J.Biochemistry 29:5380-5389(1990) Human gliomas and epileptic foci express high levels of a mRNA related to rat testicular sulfated glycoprotein 2, a purported marker of cell death.Danik M., Chabot J.G., Mercier C., Benabid A.L., Chauvin C., Quirion R., Suh M.Proc. Natl. Acad. Sci. U.S.A. 88:8577-8581(1991) Glew M.D., Kirszbaum L., Bozas S.E., Walker I.D. Molecular cloning and characterization of the novel, human complement-associated protein, SP-40,40 a link between the complement and reproductive systems.Kirszbaum L., Sharpe J.A., Murphy B., D'Apice J.F.A., Classon B., Hudson P., Walker I.D.EMBO J. 8:711-718(1989) SP-40,40, a protein involved in the control of the complement pathway, possesses a unique array of disulphide bridges.Kirszbaum L., Bozas S.E., Walker I.D.FEBS Lett. 297:70-76(1992) Identification of human aging-associated gene.Kim J.W.The apolipoprotein A-I binding protein of placenta and the SP-40,40 protein of human blood are different proteins which both bind to apolipoprotein A-I.Ehnholm C., Bozas S.E., Tenkanen H., Kirszbaum L., Metso J., Murphy B., Walker I.D.Biochim. Biophys. Acta 1086:255-260(1991) Identification of the disulfide bonds in human plasma protein SP-40,40 (apolipoprotein-J) .Choi-Miura N.H., Takahashi Y., Nakano Y., Tobe T., Tomita M.J. Biochem. 112:557-561(1992) Apolipoprotein J is associated with paraoxonase in human plasma.Kelso G.J., Stuart W.D., Richter R.J., Furlong C.E., Jordan-Starck T.C., Harmony J.A.K.Biochemistry 33:832-839(1994) Identification and characterization of glycosylation sites in human serum clusterin.Kapron J.T., Hilliard G.M., Lakins J.N., Tenniswood M.P., West K.A., Carr S.A., Crabb J.W.Protein Sci. 6:2120-2133(1997) Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state.Poon S., Easterbrook-Smith S.B., Rybchyn M.S., Carver J.A., Wilson M.R.Biochemistry 39:15953-15960(2000) Suppression of apolipoprotein C-II amyloid formation by the extracellular chaperone, clusterin.Hatters D.M., Wilson M.R., Easterbrook-Smith S.B., Howlett G.J.Eur. J. Biochem. 269:2789-2794(2002) Mildly acidic pH activates the extracellular molecular chaperone clusterin.Poon S., Rybchyn M.S., Easterbrook-Smith S.B., Carver J.A., Pankhurst G.J., Wilson M.R.J. Biol. Chem. 277:39532-39540(2002) Synthesis and functional analyses of nuclear clusterin, a cell death protein.Leskov K.S., Klokov D.Y., Li J., Kinsella T.J., Boothman D.A.J. Biol. Chem. 278:11590-11600(2003) Essential requirement of apolipoprotein J (clusterin) signaling for IkappaB expression and regulation of NF-kappaB activity.Santilli G., Aronow B.J., Sala A.J. Biol. Chem. 278:38214-38219(2003) Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.Zhang H., Li X.-J., Martin D.B., Aebersold R.Nat. Biotechnol. 21:660-666(2003) Isolation and characterization of a novel gene CLUAP1 whose expression is frequently upregulated in colon cancer.Takahashi M., Lin Y.-M., Nakamura Y., Furukawa Y.Oncogene 23:9289-9294(2004) Screening for N-glycosylated proteins by liquid chromatography mass spectrometry.Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.Proteomics 4:454-465(2004) Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.J. Proteome Res. 4:2070-2080(2005) Clusterin inhibits apoptosis by interacting with activated Bax.Zhang H., Kim J.K., Edwards C.A., Xu Z., Taichman R., Wang C.Y.Nat. Cell Biol. 7:909-915(2005) Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection.Leong W.F., Chow V.T.Cell. Microbiol. 8:565-580(2006) Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.J. Proteome Res. 5:1493-1503(2006) Elucidation of N-glycosylation sites on human platelet proteins a glycoproteomic approach.Lewandrowski U., Moebius J., Walter U., Sickmann A.Mol. Cell. Proteomics 5:226-233(2006) Effects of glycosylation on the structure and function of the extracellular chaperone clusterin.Stewart E.M., Aquilina J.A., Easterbrook-Smith S.B., Murphy-Durland D., Jacobsen C., Moestrup S., Wilson M.R.Biochemistry 46:1412-1422(2007) Multiple pathways regulating the anti-apoptotic protein clusterin in breast cancer.Ranney M.K., Ahmed I.S., Potts K.R., Craven R.J.Biochim. Biophys. Acta 1772:1103-1111(2007) Characterization of an eppin protein complex from human semen and spermatozoa.Wang Z., Widgren E.E., Richardson R.T., O'Rand M.G.Biol. Reprod. 77:476-484(2007) The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures.Yerbury J.J., Poon S., Meehan S., Thompson B., Kumita J.R., Dobson C.M., Wilson M.R.FASEB J. 21:2312-2322(2007) Differential regulation of clusterin and its isoforms by androgens in prostate cells.Cochrane D.R., Wang Z., Muramaki M., Gleave M.E., Nelson C.C.J. Biol. Chem. 282:2278-2287(2007) The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species.Kumita J.R., Poon S., Caddy G.L., Hagan C.L., Dumoulin M., Yerbury J.J., Stewart E.M., Robinson C.V., Wilson M.R., Dobson C.M.J. Mol. Biol. 369:157-167(2007) Clusterin expression in normal mucosa and colorectal cancer.Andersen C.L., Schepeler T., Thorsen K., Birkenkamp-Demtroder K., Mansilla F., Aaltonen L.A., Laurberg S., Orntoft T.F.Mol. Cell. Proteomics 6:1039-1048(2007) Stress-induced retrotranslocation of clusterin/ApoJ into the cytosol.Nizard P., Tetley S., Le Drean Y., Watrin T., Le Goff P., Wilson M.R., Michel D.Traffic 8:554-565(2007) Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.Proteomics 8:3833-3847(2008) Structural characterization of clusterin-chaperone client protein complexes.Wyatt A.R., Yerbury J.J., Wilson M.R.J. Biol. Chem. 284:21920-21927(2009) Clusterin is a short half-life, poly-ubiquitinated protein, which controls the fate of prostate cancer cells.Rizzi F., Caccamo A.E., Belloni L., Bettuzzi S.J. Cell. Physiol. 219:314-323(2009) 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) A strategy for precise and large scale identification of core fucosylated glycoproteins.Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.Mol. Cell. Proteomics 8:913-923(2009) Enrichment of glycopeptides for glycan structure and attachment site identification.Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.Nat. Methods 6:809-811(2009) Identification of human plasma proteins as major clients for the extracellular chaperone clusterin.Wyatt A.R., Wilson M.R.J. Biol. Chem. 285:3532-3539(2010) Clusterin facilitates COMMD1 and I-kappaB degradation to enhance NF-kappaB activity in prostate cancer cells.Zoubeidi A., Ettinger S., Beraldi E., Hadaschik B., Zardan A., Klomp L.W., Nelson C.C., Rennie P.S., Gleave M.E.Mol. Cancer Res. 8:119-130(2010) Clusterin facilitates in vivo clearance of extracellular misfolded proteins.Wyatt A.R., Yerbury J.J., Berghofer P., Greguric I., Katsifis A., Dobson C.M., Wilson M.R.Cell. Mol. Life Sci. 68:3919-3931(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) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

• NCBI GI #: 355594753
• NCBI GeneID: 1191
• NCBI Accession #: NP_001822.3
• NCBI GenBank Nucleotide #: NM_001831.3
• UniProt Accession #: P10909; P11380; P11381; Q2TU75; Q5HYC1; Q7Z5B9; B2R9Q1; B3KSE6; AAB25217
• Molecular Weight: 27.8 kDa
• NCBI Official Full Name: clusterin preproprotein
• NCBI Official Synonym Full Names: clusterin
• NCBI Official Symbol: CLU
• NCBI Official Synonym Symbols: CLI; AAG4; APOJ; CLU1; CLU2; KUB1; SGP2; APO-J; SGP-2; SP-40; TRPM2; TRPM-2; NA1/NA2
• NCBI Protein Information: clusterin
• UniProt Protein Name: Clusterin
• Protein Family: Clusterin
• UniProt Gene Name: CLU
• UniProt Synonym Gene Names: APOJ; CLI; KUB1; Apo-J; CLI; TRPM-2
• UniProt Entry Name: CLUS_HUMAN

NCBI Description

The protein encoded by this gene is a secreted chaperone that can under some stress conditions also be found in the cell cytosol. It has been suggested to be involved in several basic biological events such as cell death, tumor progression, and neurodegenerative disorders. Alternate splicing results in both coding and non-coding variants.[provided by RefSeq, May 2011]

Uniprot Description

CLU: Isoform 1 functions as extracellular chaperone that prevents aggregation of nonnative proteins. Prevents stress- induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. Secreted isoform 1 protects cells against apoptosis and against cytolysis by complement. Intracellular isoforms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity. Nuclear isoforms promote apoptosis. Mitochondrial isoforms suppress BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis. Plays a role in the regulation of cell proliferation. Belongs to the clusterin family. 5 isoforms of the human protein are produced by alternative splicing.

Protein type: Secreted, signal peptide; Apoptosis; Secreted; Mitochondrial

Chromosomal Location of Human Ortholog: 8p21-p12

Cellular Component: cell surface; cytoplasm; cytosol; endoplasmic reticulum; extracellular matrix; extracellular region; extracellular space; Golgi apparatus; growth cone; intracellular; mitochondrial membrane; mitochondrion; nucleus; perinuclear region of cytoplasm; protein complex

Molecular Function: ATPase activity; chaperone binding; misfolded protein binding; protein binding; protein N-terminus binding; ubiquitin protein ligase binding

Biological Process: activation of NF-kappaB transcription factor; aging; blood coagulation; cell morphogenesis; chaperone-mediated protein complex assembly; complement activation; complement activation, classical pathway; endocrine pancreas development; innate immune response; lipid metabolic process; microglial cell activation; myelin maintenance in the central nervous system; negative regulation of protein homooligomerization; neurite morphogenesis; platelet activation; platelet degranulation; positive regulation of apoptosis; positive regulation of cell differentiation; positive regulation of cell proliferation; positive regulation of nitric oxide biosynthetic process; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; positive regulation of tumor necrosis factor production; protein import; protein stabilization; release of cytochrome c from mitochondria; response to light stimulus; response to misfolded protein; response to virus; reverse cholesterol transport