hsp104
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  • Official Full Name
  • Hsp104p
  • Synonyms
  • HSP104; Hsp104p; L0948; Heat shock protein 104; Hsp 104; Heat shock protein that cooperates with Ydj1p (Hsp40) and Ssa1p (Hsp70) to refold and reactivate previously denatured, aggregated proteins; responsive to stresses including: heat, ethanol, and sodium arsenite; involved in [PSI+] propagation
Cat.#:HSP104-1258STag:N/A
Source (Host):E. coliSpecies:Yeast
Product nameRecombinant Saccharomyces Cerevisiae HSP104
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Cat.#:HSP104-319YTag:N/A
Source (Host):E. coliSpecies:Yeast
Product nameRecombinant Yeast Heat Shock Protein 104
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Protein Function

HSP104 has several biochemical functions, for example, ADP binding, ATP binding, ATPase activity, coupled. Some of the functions are cooperated with other proteins, some of the functions could acted by HSP104 itself. We selected most functions HSP104 had, and list some proteins which have the same functions with HSP104. You can find most of the proteins on our site.
Function
Related Protein
Function ADP binding
Related Protein TAP1; MYO9B; GLUD1; GCLC; VCP; CYB5R3; ACTA1; MYO7A; P2RY1; MYO6
Function ATP binding
Related Protein EHD2; EPHA2A; RUNX2; KIF3CB; PFKMB; ACTR2; HYOU1; MAP2K2A; MCMDC2; EP400
Function ATPase activity, coupled
Related Protein HSP104; HSPA8; HSPA1A; VPS4B; HSPA1B; MYH3; NSF; MYO1E; CCT8; PEX1
Function chaperone binding
Related Protein AHSA1L; DNAJB2; Alb; SLC25A17; BAK1; ATP1A2; AMFR; GRPEL2; SERPINA7; HSP104
Function nucleotide binding
Related Protein ATP8B3; RAF1A; OASL2; UMPS; SMOK2B; ACSM2; U2SURP; DDX3; NT5C3A; RBFOX2
Function unfolded protein binding
Related Protein PDRG1; ERLEC1; CHAF1B; CALR3B; CRYABA; AFG3L2; RUVBL2; SSUH2RS1; UGGT1; PFDN6

HSP104 Related Articles

Josse, L; Smales, CM; et al. Transient Expression of Human TorsinA Enhances Secretion of Two Functionally Distinct Proteins in Cultured Chinese Hamster Ovary (CHO) Cells. BIOTECHNOLOGY AND BIOENGINEERING 105:556-566(2010).
Yoshiike, Y; Minai, R; et al. Amyloid Oligomer Conformation in a Group of Natively Folded Proteins. PLOS ONE 3:-(2008).