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Anti-HSPD1 / HSP60 Antibody (clone LK1)

Mouse Anti Human Monoclonal Antibody

     
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immuno electron microscopy
  • EIA=Enzyme Immunoassay
WB, IHC-P, IP, FC
Primary Accession P10809
Predicted Human, Mouse, Rat, Rabbit, Hamster, Monkey, Pig, Chicken, Sheep, Xenopus, Bovine, Guinea Pig, Drosophila
Host Mouse
Clonality Monoclonal
Isotype IgG1
Clone Names LK1
Calculated MW 61055 Da
Dilution Flo (1:100), IHC-P (10 µg/ml), IP (1:80), WB (1:1000)
Additional Information
Gene ID 3329
Alias Symbol HSPD1
Other Names HSPD1, 60 kDa chaperonin, CPN60, Heat shock protein 65, Heat shock protein 60, HSP-60, HSP60, HuCHA60, HLD4, HSP65, p60 lymphocyte protein, SPG13, Chaperonin 60, GROEL
Reconstitution & Storage Protein G purified
PrecautionsAnti-HSPD1 / HSP60 Antibody (clone LK1) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name HSPD1
Synonyms HSP60
Function Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:11422376, PubMed:1346131). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back- to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable).
Cellular Location Mitochondrion matrix.
Research Areas
Citations (0)
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$ 533.50
Cat# ALS17615
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