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.# | Product name | Source (Host) | Species | Tag | Protein Length | Price |
|---|---|---|---|---|---|---|
| HSP104-1258S | Recombinant Saccharomyces Cerevisiae HSP104 | S.cerevisiae | Yeast | Non |
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| HSP104-319Y | Recombinant Yeast Heat Shock Protein 104 | E.coli | Yeast | Non |
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Involved Pathway
HSP104 involved in several pathways and played different roles in them. We selected most pathways HSP104 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with HSP104 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|
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 |
|---|---|
| ATPase activity, coupled | HSPA6,MYH3,HSPA1B,VPS4A,MYO1E,ABCB1A,PEX1,HSPA8,HSPA1A,NSF |
| ATP binding | IARS,TNNI3K,RBKS,RECQL4,PNKP,TESK2,CHST13,LRRK2,TNK1,RIPK3 |
| chaperone binding | UBL4A,INS1,CTSC,TG,CDC37,AHSA1,Alb,DNAJA2,TIMM44,TP53 |
| ADP binding | APAF1,VCP,ATP1A1,LONP1,ERN1,PRPS1,MYO7A,P2RY1,MYO9B,MIEF1 |
| unfolded protein binding | DNAJB1B,CCDC102A,DNAJB1A,HSP90B1,DNAJA3B,TAPBP,DNAJB6,CRYAB,SRSF12,NPM1 |
| nucleotide binding | ARF4A,Fert2,CELF6,CPSF7,CHD8,HNRNPC,TNK2B,TRA2A,BSK146,PTBP2B |
Interacting Protein
HSP104 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with HSP104 here. Most of them are supplied by our site. Hope this information will be useful for your research of HSP104.
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References
- Yoshiike, Y; Minai, R; et al. Amyloid Oligomer Conformation in a Group of Natively Folded Proteins. PLOS ONE 3:-(2008).
- 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).
