BAG family molecular chaperone regulator 5 Recombinant Protein | BAG5 recombinant protein

Recombinant Human BAG family molecular chaperone regulator 5

Cat. Num. AAA1453896

• Gene Names: BAG5; BAG-5
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: BAG family molecular chaperone regulator 5; Recombinant Human BAG family molecular chaperone regulator 5; Bcl-2-associated athanogene 5; BAG5 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: 1-447aa; Full Length
• Sequence: MDMGNQHPSISRLQEIQKEVKSVEQQVIGFSGLSDDKNYKKLERILTKQLFEIDSVDTEGKGDIQQARKRAAQETERLLKELEQNANHPHRIEIQNIFEEAQSLVREKIVPFYNGGNCVTDEFEEGIQDIILRLTHVKTGGKISLRKARYHTLTKICAVQEIIEDCMKKQPSLPLSEDAHPSVAKINFVMCEVNKARGVLIALLMGVNNNETCRHLSCVLSGLIADLDALDVCGRTEIRNYRREVVEDINKLLKYLDLEEEADTTKAFDLRQNHSILKIEKVLKRMREIKNELLQAQNPSELYLSSKTELQGLIGQLDEVSLEKNPCIREARRRAVIEVQTLITYIDLKEALEKRKLFACEEHPSHKAVWNVLGNLSEIQGEVLSFDGNRTDKNYIRLEELLTKQLLALDAVDPQGEEKCKAARKQAVRLAQNILSYLDLKSDEWEY
• Sequence Length: 447

• 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 BAG5 recombinant protein

Inhibits both auto-ubiquitination of PARK2 and ubiquitination of target proteins by PARK2. May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding. 1 Publication

Product Categories/Family for BAG5 recombinant protein

Cancer

References

An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators.Takayama S., Xie Z., Reed J.C.J. Biol. Chem. 274:781-786(1999) Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.DNA Res. 5:355-364(1998) The DNA sequence and analysis of human chromosome 14.Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.Nature 421:601-607(2003) 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) High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy.Hasson S.A., Kane L.A., Yamano K., Huang C.H., Sliter D.A., Buehler E., Wang C., Heman-Ackah S.M., Hessa T., Guha R., Martin S.E., Youle R.J.Nature 504:291-295(2013) The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange.Arakawa A., Handa N., Ohsawa N., Shida M., Kigawa T., Hayashi F., Shirouzu M., Yokoyama S.Structure 18:309-319(2010)

NCBI and Uniprot Product Information

• NCBI GI #: 62548854
• NCBI GeneID: 9529
• NCBI Accession #: NP_001015048.1
• NCBI GenBank Nucleotide #: NM_001015048.2
• UniProt Accession #: Q9UL15; O94950; Q86W59
• Molecular Weight: 67.2 kDa
• NCBI Official Full Name: BAG family molecular chaperone regulator 5 isoform b
• NCBI Official Synonym Full Names: BCL2 associated athanogene 5
• NCBI Official Symbol: BAG5
• NCBI Official Synonym Symbols: BAG-5
• NCBI Protein Information: BAG family molecular chaperone regulator 5
• UniProt Protein Name: BAG family molecular chaperone regulator 5
• Protein Family: BAG family molecular chaperone regulator
• UniProt Gene Name: BAG5
• UniProt Synonym Gene Names: KIAA0873; BAG-5
• UniProt Entry Name: BAG5_HUMAN

NCBI Description

The protein encoded by this gene is a member of the BAG1-related protein family. BAG1 is an anti-apoptotic protein that functions through interactions with a variety of cell apoptosis and growth related proteins including BCL-2, Raf-protein kinase, steroid hormone receptors, growth factor receptors and members of the heat shock protein 70 kDa family. This protein contains a BAG domain near the C-terminus, which could bind and inhibit the chaperone activity of Hsc70/Hsp70. Three transcript variants encoding two different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

Uniprot Description

BAG5: Inhibits both auto-ubiquitination of PARK2 and ubiquitination of target proteins by PARK2. May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding. 2 isoforms of the human protein are produced by alternative splicing.

Chromosomal Location of Human Ortholog: 14q32.33

Cellular Component: cytosol; inclusion body; membrane; mitochondrion; nucleus; perinuclear region of cytoplasm

Molecular Function: chaperone binding; protein binding; protein kinase binding; ubiquitin protein ligase binding

Biological Process: Golgi organization and biogenesis; negative regulation of proteasomal ubiquitin-dependent protein catabolic process; negative regulation of protein ubiquitination; negative regulation of ubiquitin-protein ligase activity; protein folding; regulation of ubiquitin-protein ligase activity