Rabbit anti-Hamster Heat Shock Protein 104 Polyclonal Antibody | anti-HSP104 antibody

Heat Shock Protein 104 (HSP104)

Cat. Num. AAA610443

• Reactivity: Hamster
• Applications: Western Blot
• Purity: Serum
• Synonyms: Heat Shock Protein 104; Polyclonal Antibody; Heat Shock Protein 104 (HSP104); Anti -Heat Shock Protein 104 (HSP104); anti-HSP104 antibody

• Host: Rabbit
• Reactivity: Hamster
• Clonality: Polyclonal
• Isotype: IgG
• Specificity: Detects a 104kD protein, corresponding to the apparent molecular mass of Hsp104 on SDS-PAGE immunoblots, in samples from yeast (S. cerevisiae). This antibody also Detects a ~50kD band in yeast samples on immunoblot analysis. No reactivity is detected in immunoblot analysis with human, mouse, rat monkey and hamster proteins.
• Purity/Purification: Serum
• Form/Format: Serum

• Applicable Applications for anti-HSP104 antibody: Western Blot (WB)
• Immunogen: A 15 residue synthetic peptide DDDNEDSMEIDDDLD based on the S. cerevisiae Hsp104 (residues 894-908) (3) was synthesized and the peptide coupled to KLH.
• Preparation and Storage: -20 degree C

Related Product Information for anti-HSP104 antibody

In response to adverse changes in their environment, cells from many organisms increase the expression of a class of proteins referred to as heat shock or stress proteins. The most well recognized are the Hsp70 and Hsp90 families of proteins. More recently discovered is the Hsp100 (Clp) family of proteins that are highly conserved from eukaryotes to bacteria (which includes yeast, plants, and trypanosomes with the exception of Drosophilia). They share a common function in helping organisms to survive extreme stress. Hsp100 proteins generally have amino acid sequences of about 900 residues and contain two nucleotide binding sites. The two ATP-binding domains of yeast Hsp104 have different functions. One controls the assembly of the protein into a homoligomeric complex and the other controls most of the ATPase activity. Hsp104 of yeast and ClpB of E. coli have significant sequence homology particularly in the two nucleotide binding sites and both of these proteins are required for thermotolerance at extreme temperatures (1,4). Hsp104 can protect yeast cells against high temperature and high concentrations of ethanol but mutation studies have shown this protein is not required for normal growth. The biochemical activities of Hsp100 proteins that allows them to provide thermotolerance are not currently understood. In yeast, Hsp104 has been observed to possess partial functional interchangeability with the Hsp70 family of proteins. This suggests that both protein families may be performing at least some complementary biological function (2). Hsp104 might promote the proteolysis of damaged proteins that are not salvageable by Hsp70, or Hsp104 might serve as another chaperone, binding to damaged proteins and promoting refolding.

Product Categories/Family for anti-HSP104 antibody

Antibodies; Abs to Heat Shock Proteins

NCBI and Uniprot Product Information

• NCBI GI #: 1346246
• NCBI GeneID: 850633
• UniProt Accession #: P31539; D6VXX8
• Molecular Weight: 102,035 Da
• NCBI Official Full Name: Heat shock protein 104
• NCBI Official Symbol: HSP104
• NCBI Protein Information: Hsp104p
• UniProt Protein Name: Heat shock protein 104
• Protein Family: Heat shock protein
• UniProt Gene Name: HSP104
• UniProt Entry Name: HS104_YEAST

Uniprot Description

Function: Required, in concert with Hsp40 (YDJ1) and Hsp70 (SSA1) and small Hsps (HSP26), for the dissociation, resolubilization and refolding of aggregates of damaged proteins after heat or other environmental stresses. Extracts proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexamer, after which they can be refolded by components of the Hsp70/Hsp40 chaperone system. Substrate binding is ATP-dependent, and release of bound polypeptide is triggered by ATP hydrolysis. Also responsible for the maintenance of prions by dissociating prion fibrils into smaller oligomers, thereby producing transmissible seeds that can infect daughter cells during mitosis and meiosis. Loss of HSP104 can cure yeast cells of the prions [PSI+], [URE3] and [PIN+]. Excess HSP104 can also specifically cure cells of [PSI+]. Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.14 Ref.17 Ref.19 Ref.20 Ref.21 Ref.23 Ref.27 Ref.31 Ref.36 Ref.39 Ref.40 Ref.41 Ref.44 Ref.45 Ref.47 Ref.48 Ref.49 Ref.50 Ref.54

Enzyme regulation: Inhibited by micromolar concentrations of guanidinium chloride. Inhibits the ATPase activity, but does not dissociate the hexameric protein. Ref.35

Subunit structure: Homohexamer, forming a ring with a central pore. The hexamer is stabilized by high protein concentrations and by ADP or ATP. Oligomerization influences ATP hydrolysis activity at NBD2. Interacts with YDJ1. Interacts (via C-terminal DDLD tetrapeptide) with CNS1, CPR7 and STI1 (via TPR repeats); under respiratory growth conditions. Ref.9 Ref.14 Ref.17 Ref.22 Ref.24 Ref.43 Ref.46 Ref.52

Subcellular location: Cytoplasm. Nucleus. Note: Shuttles between the cytoplasm and the nucleus in an importin KAP95- and KAP121-dependent and an exportin XPO1-dependent manner. Accumulation in the nucleus is enhanced by severe heat shock. In the cytoplasm, concentrates on a perivacuolar compartment, the 'insoluble protein deposit' (IPOD), in which terminally aggregated proteins are sequestered. It is also found, to a lesser extend, at a 'juxtanuclear quality control' (JUNQ) compartment, where soluble ubiquitinated misfolded proteins accumulate. Ref.13 Ref.18 Ref.32 Ref.55 Ref.56

Induction: By heat stress dependent on the heat shock transcription factor HSF1 and the general stress transcription factors MSN2 and MSN4. Expressed at a higher level in respiring cells than in fermenting cells. Expressed in stationary phase cells and spores (at protein level). Ref.7 Ref.9 Ref.12 Ref.28 Ref.35 Ref.38

Domain: Has 2 AAA ATPase type nucleotide-binding domains (NBDs) per monomer, a low-affinity, high-turnover site (NBD1) and a high-affinity site (NBD2) with a 300-fold slower rate of hydrolysis. There is allosteric regulation between the 2 sites. ATP binding to NBD1 triggers binding of polypeptides and stimulates ATP hydrolysis at NBD2. Nucleotide binding to NBD2 is crucial for oligomerization.The C-terminal extension is involved in oligomerization.

Miscellaneous: Present with 32800 molecules/cell in log phase SD medium. Ref.33

Sequence similarities: Belongs to the clpA/clpB family.

Biophysicochemical propertiesKinetic parameters:KM=170 µM for ATP (at NBD1) Ref.15 Ref.17 Ref.24 Ref.25 Ref.36KM=4.7 µM for ATP (at NBD2)Vmax=1.25 nmol/min/µg enzyme for ATP