Anti-HSP60 (Mab11-13) Antibody

Cat# OAED00191

Size : 50ug

Brand : Aviva Systems Biology

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Phone : +1 850 650 7790

Datasheets/ManualsPrintable datasheet for Anti-HSP60 (Mab11-13) Antibody (OAED00191)
Product Info
Predicted Species ReactivityBovine|Dog|Dolphin|Drosophila|Fish|Guinea Pig|Hamster|Human|Monkey|Mosquito|Mouse|Porcine|Rabbit|Rat|Snake
ClonalityMonoclonal
CloneMab-11-13
IsotypeIgG2a
HostMouse
ApplicationFlow cytometry|Immunofluorescence|Western blot
Reconstitution and StorageLong Term Storage : -20C
ImmunogenRecombinant human Hsp60.
SpecificityRecognizes human, mouse, rat, bovine, dog, dolphin, Drosophila, fish, guinea pig, hamster, mosquito, monkey, pig, rabbit and snake HSP60. Detects a band of ~60kDa by Western blot.
FormulationLiquid. In PBS, pH 7.2, containing 50% glycerol and 0.09% sodium azide.
PurityProtein G affinity purified.
Application InfoFlow Cytometry (10μg/ml)
Immunofluorescence
Immunohistochemistry (paraffin sections)
Western Blot (1:1000, colorimetric)
Optimal conditions must be determined individually for each application.
Gene SymbolHSPD1
Gene Full Nameheat shock protein family D (Hsp60) member 1
Alias Symbols60 kDa chaperonin;60 kDa heat shock protein, mitochondrial;chaperonin 60;CPN60;epididymis secretory sperm binding protein;GROEL;heat shock 60kDa protein 1 (chaperonin);Heat shock protein 60;heat shock protein 65;HLD4;HSP60;HSP-60;HSP65;HuCHA60;mitochondrial matrix protein P1;P60 lymphocyte protein;short heat shock protein 60 Hsp60s1;SPG13.
NCBI Gene Id3329
Protein Name60 kDa heat shock protein, mitochondrial
Description of TargetChaperonin 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:1346131, PubMed:11422376). 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).
Uniprot IDP10809