DnaJ homolog subfamily B member 1 Recombinant Protein | DNAJB1 recombinant protein

Recombinant Human DnaJ homolog subfamily B member 1 protein

Cat. Num. AAA717051

• Gene Names: DNAJB1; Hdj1; Sis1; HSPF1; Hsp40; RSPH16B
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: DnaJ homolog subfamily B member 1; Recombinant Human DnaJ homolog subfamily B member 1 protein; DnaJ protein homolog 1; Heat shock 40 kDa protein 1; HSP40; Heat shock protein 40Human DnaJ protein 1; hDj-1; DNAJB1 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 1-340aa; Full Length
• Sequence: MGKDYYQTLGLARGASDEEIKRAYRRQALRYHPDKNKEPGAEEKFKEIAEAYDVLSDPRKREIFDRYGEEGLKGSGPSGGSGGGANGTSFSYTFHGDPHAMFAEFFGGRNPFDTFFGQRNGEEGMDIDDPFSGFPMGMGGFTNVNFGRSRSAQEPARKKQDPPVTHDLRVSLEEIYSGCTKKMKISHKRLNPDGKSIRNEDKILTIEVKKGWKEGTKITFPKEGDQTSNNIPADIVFVLKDKPHNIFKRDGSDVIYPARISLREALCGCTVNVPTLDGRTIPVVFKDVIRPGMRRKVPGEGLPLPKTPEKRGDLIIEFEVIFPERIPQTSRTVLEQVLPI
• Sequence Length: 240

• 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 DNAJB1 recombinant protein

Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP.

Product Categories/Family for DNAJB1 recombinant protein

Neuroscience

References

A human homologue of the Escherichia coli DnaJ heat-shock protein.Raabe T., Manley J.L.Nucleic Acids Res. 19:6645-6645(1991) Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ.Ohtsuka K.Biochem. Biophys. Res. Commun. 197:235-240(1993) Genomic cloning of a human heat shock protein 40 (Hsp40) gene (HSPF1) and its chromosomal localization to 19p13.2.Hata M., Okumura K., Seto M., Ohtsuka K.Genomics 38:446-449(1996) 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) The DNA sequence and biology of human chromosome 19.Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.Nature 428:529-535(2004) Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells.Hattori H., Liu Y.-C., Tohnai I., Ueda M., Kaneda T., Kobayashi T., Tanabe K., Ohtsuka K.Cell Struct. Funct. 17:77-86(1992) The cellular inhibitor of the PKR protein kinase, P58(IPK) , is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activity.Melville M.W., Tan S.-L., Wambach M., Song J., Morimoto R.I., Katze M.G.J. Biol. Chem. 274:3797-3803(1999) Regulation of SR protein phosphorylation and alternative splicing by modulating kinetic interactions of SRPK1 with molecular chaperones.Zhong X.Y., Ding J.H., Adams J.A., Ghosh G., Fu X.D.Genes Dev. 23:482-495(2009) 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) N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) 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) Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain.Qian Y.Q., Patel D., Hartl F.-U., McColl D.J.J. Mol. Biol. 260:224-235(1996)

NCBI and Uniprot Product Information

• NCBI GI #: 665505950
• NCBI GeneID: 3337
• NCBI Accession #: NP_001287843.1
• NCBI GenBank Nucleotide #: NM_001300914.1
• UniProt Accession #: P25685; B4DX52
• Molecular Weight: 65 kDa
• NCBI Official Full Name: dnaJ homolog subfamily B member 1 isoform 2
• NCBI Official Synonym Full Names: DnaJ heat shock protein family (Hsp40) member B1
• NCBI Official Symbol: DNAJB1
• NCBI Official Synonym Symbols: Hdj1; Sis1; HSPF1; Hsp40; RSPH16B
• NCBI Protein Information: dnaJ homolog subfamily B member 1
• UniProt Protein Name: DnaJ homolog subfamily B member 1
• Protein Family: DnaJ homolog subfamily
• UniProt Gene Name: DNAJB1
• UniProt Synonym Gene Names: DNAJ1; HDJ1; HSPF1; HSP40; Heat shock protein 40; hDj-1
• UniProt Entry Name: DNJB1_HUMAN

NCBI Description

This gene encodes a member of the DnaJ or Hsp40 (heat shock protein 40 kD) family of proteins. DNAJ family members are characterized by a highly conserved amino acid stretch called the 'J-domain' and function as one of the two major classes of molecular chaperones involved in a wide range of cellular events, such as protein folding and oligomeric protein complex assembly. The encoded protein is a molecular chaperone that stimulates the ATPase activity of Hsp70 heat-shock proteins in order to promote protein folding and prevent misfolded protein aggregation. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2015]

Uniprot Description

Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP.