Clusterin (CLU), human, recombinant

Organism: Homo sapiens (Human). Source: Mammalian cell. Expression Region: 23-449aa. Protein Length: Full Length of Mature Protein. Tag Info: C-terminal 6xHis-tagged. Target Protein Sequence: DQTVSDNELQ EMSNQGSKYV NKEIQNAVNG VKQIKTLIEK TNEERKTLLS NLEEAKKKKE DALNETRESE TKLKELPGVC NETMMALWEE CKPCLKQTCM KFYARVCRSG SGLVGRQLEE FLNQSSPFYF WMNGDRIDSL LENDRQQTHM LDVMQDHFSR ASSIIDELFQ DRFFTREPQD TYHYLPFSLP HRRPHFFFPK SRIVRSLMPF SPYEPLNFHA MFQPFLEMIH EAQQAMDIHF HSPAFQHPPT EFIREGDDDR TVCREIRHNS TGCLRMKDQC DKCREILSVD CSTNNPSQAK LRRELDESLQ VAERLTRKYN ELLKSYQWKM LNTSSLLEQL NEQFNWVSRL ANLTQGEDQY YLRVTTVASH TSDSDVPSGV TEVVVKLFDS DPITVTVPVE VSRKNPKFME TVAEKALQEY RKKHREE. Purity: Greater than 85% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 °C/-80 °C. The shelf life of lyophilized form is 12 months at -20 °C/-80 °C. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: [Isoform 1]: Functions as extracellular chaperone that prevents aggregation of non native 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 . Protects cells against apoptosis and against cytolysis by complement . Intracellular forms 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 . A mitochondrial form suppresses BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis . Plays a role in the regulation of cell proliferation . An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5 . Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity . Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3. Plays a role in the clearance of immune complexes that arise during cell injury., [Isoform 6]: Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity., [Isoform 4]: Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity . Promotes cell death through interaction with BCL2L1 that releases and activates BAX . Reference: NIEHS SNPs programDNA sequence and analysis of human chromosome 8.Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.Nature 439:331-335(2006). Function: nan