Hsp83 Antibody

Code CSB-PA355879XA01DLU
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Product Details

Full Product Name
Rabbit anti-Drosophila melanogaster (Fruit fly) Hsp83 Polyclonal antibody
Uniprot No.
Target Names
Hsp83
Alternative Names
Hsp83 antibody; Hsp82 antibody; CG1242 antibody; Heat shock protein 83 antibody; HSP 82 antibody
Raised in
Rabbit
Species Reactivity
Drosophila melanogaster (Fruit fly)
Immunogen
Recombinant Drosophila melanogaster (Fruit fly) Hsp83 protein
Immunogen Species
Drosophila melanogaster (Fruit fly)
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 for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Together with Hop and piwi, mediates canalization, also known as developmental robustness, likely via epigenetic silencing of existing genetic variants and suppression of transposon-induced new genetic variation. Required for piRNA biogenesis by facilitating loading of piRNAs into PIWI proteins.
Gene References into Functions
  1. Hsp90 binds close to the transcriptional start site of around one-third of all Drosophila coding genes. PMID: 29177663
  2. We show that while Hsp70 or Hsp83 expression under normal or stress conditions was not affected by AR feeding, Hsp27 levels were elevated in AR-fed wild-type control as well as heat-shocked larvae PMID: 27966490
  3. The results revealed that the high-fat diet augmented the rate of lipid peroxidation and SOD and CAT activity and induced a higher expression of HSP83 and MPK2 mRNA. PMID: 27579152
  4. Hsp83 facilitates methoprene-tolerant nuclear import to modulate juvenile hormone signaling. PMID: 25122763
  5. Interaction of Spag with both Hsp70 and Hsp90 suggests a model whereby R2TP would accompany clients from Hsp70 to Hsp90 to facilitate their assembly into macromolecular complexes. PMID: 24394412
  6. Our results reveal that Hsp83 plays a heretofore unappreciated role in promoting APC/C function during cell cycle exit and suggest a mechanism by which Hsp90 inhibition could promote genomic instability and carcinogenesis PMID: 24086162
  7. Using computational and biochemical analyses, study find that Hsp90 maintains and optimizes RNA polymerase II pausing via stabilization of the negative elongation factor complex. PMID: 22579285
  8. Data suggest that that an Sgt1/Hsp90-LKB1-AMPK pathway acts redundantly with a microtubule-induced polarity pathway to generate neuroblast cortical polarity, and the absence of neuroblast cortical polarity can produce neuroblast tumors. PMID: 22248825
  9. A natural genetic variation in Hsp90 may mediate the evolution of canalized morphological traits even if it does not influence the expression of variation for uncanalized traits. PMID: 20200026
  10. Hsp90 is required for Ago2 to receive the small interfering RNA (siRNA) duplex from the RNA-induced silencing complex-loading complex in RNA interference. PMID: 20639883
  11. To determine the effect of Hsp90 on quantitative trait variability we deconstructed genetic, stochastic and environmental components of variation in traits of genetically matched flies, differing only by Hsp90 loss-of-function or wild-type alleles. PMID: 17183707
  12. Up to 120-fold differences in penetrance among six highly related selection lines, selected for and against a deformed eye trait, did not translate into measurable differences in viability, lifespan or competitive fitness. PMID: 17183708
  13. Hsp83 mutations can generate new variation by transposon-mediated 'canonical' mutagenesis PMID: 20062045
  14. Hsp90 masks variation affecting target pathways and traits in populations independent of purely nongenetic sources of variation PMID: 14595030
  15. heat shock inhibits eIF4F activity, and Hsp90 mRNA translation is sensitive to eIF4F inactivation PMID: 15347681
  16. The results suggest that a multicomponent protein chaperone complex involving both Hsp90 and Hsp70 signals the cessation of heat shock protein synthesis, the restoration of normal translation, and likely the establishment of thermotolerance. PMID: 16218955
  17. Data show that Smaug can recruit the CCR4-NOT deadenylase to trigger Hsp83 mRNA degradation despite the fact that it is being translated. PMID: 18794360
  18. These findings suggest that Sgt1 is involved in the stabilization of Polo allowing normal centrosome maturation, entry and progression though mitosis. PMID: 19131964
  19. Hsp90 cooperates with Trx at chromatin for maintaining the active expression state of targets like the Hox genes. PMID: 19144915

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Subcellular Location
Cytoplasm.
Protein Families
Heat shock protein 90 family
Database Links

KEGG: dme:Dmel_CG1242

STRING: 7227.FBpp0305095

UniGene: Dm.2800

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