HSC82 Antibody

Code CSB-PA322752XA01SVG
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Product Details

Full Product Name
Rabbit anti-Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) HSC82 Polyclonal antibody
Uniprot No.
Target Names
HSC82
Alternative Names
HSC82 antibody; YMR186W antibody; YM8010.16 antibody; ATP-dependent molecular chaperone HSC82 antibody; 82 kDa heat shock cognate protein antibody; Heat shock protein Hsp90 constitutive isoform antibody
Raised in
Rabbit
Species Reactivity
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Immunogen
Recombinant Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) HSC82 protein
Immunogen Species
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Conjugate
Non-conjugated
Clonality
Polyclonal
Isotype
IgG
Purification Method
Antigen Affinity Purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Tested Applications
ELISA, WB (ensure identification of antigen)
Protocols
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Value-added Deliverables
① 200ug * antigen (positive control);
② 1ml * Pre-immune serum (negative control);
Quality Guarantee
① Antibody purity can be guaranteed above 90% by SDS-PAGE detection;
② ELISA titer can be guaranteed 1: 64,000;
③ WB validation with antigen can be guaranteed positive;
Lead Time
Made-to-order (14-16 weeks)

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Target Background

Function
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction such as CNA2. Undergoes a functional cycle that is linked to its ATPase activity. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.
Gene References into Functions
  1. Hsc82 is more critical than Hsp82 for growth at 37 degrees C in the absence of mitochondrial DNA. PMID: 21439406
  2. These data support a conserved three-state chaperone cycle where the conformational equilibrium varies between species, implicating evolutionary tuning to meet the particular client protein and metabolic environment of an organism. PMID: 19061638
  3. Structural-thermodynamic relationships of interactions in the N-terminal ATP-binding domain of Hsp90. PMID: 19631219
  4. show that amino-terminal ATP-binding site residue is a conserved, strong regulator of Hsp90 functions, including ATP hydrolysis and chaperone activity. PMID: 19696785
Subcellular Location
Cytoplasm. Mitochondrion.
Protein Families
Heat shock protein 90 family
Database Links

KEGG: sce:YMR186W

STRING: 4932.YMR186W

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