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Anti-Hsp60 Recombinant Rabbit Monoclonal antibody

SKU Product Brand Unit Availability Price Quantity  
AB-06-2276
Anti-Hsp60 Recombinant Rabbit Monoclonal antibody
Erpan Tech In stock

Specifications        

Product Cat#: AB-06-2276
Product type: Primary antibody
Antigen: Hsp60
Immunogen: Synthetic peptide within Human Hsp60 aa 421-457 / 573.
Species immunized: Rabbit
Isotype: IgG
Applications: Western Blot (1:500-1:2000); Immunohistochemistry (1:40-1:200)
Reactivity: Mouse, Rat and Human
Clonality (clone number): Monoclonal (ST48-04)
Form: Liquid
Buffer: Tris-HCl buffer (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Concentration: 1 mg/ml
Purity: Protein A affinity purified
Storage: Aliquot and freeze at -20℃. Avoid multiple freeze/thaw cycles.
Alternative names: 60 kDa chaperonin antibody
60 kDa heat shock protein, mitochondrial antibody
CH60_HUMAN antibody
Chaperonin 60 antibody
Chaperonin, 60-KD antibody
CPN60 antibody
Fa04a05 antibody
GROEL antibody
Heat shock 60kDa protein 1 (chaperonin) antibody
Heat shock protein 1 (chaperonin) antibody
Heat shock protein 60 antibody
Heat shock protein 65 antibody
Heat shock protein family D (Hsp60) member 1 antibody
HLD4 antibody
Hsp 60 antibody
HSP 65 antibody
HSP-60 antibody
HSP60 antibody
HSP65 antibody
HSPD1 antibody
HuCHA60 antibody
Mitochondrial matrix protein P1 antibody
P60 lymphocyte protein antibody
Short heat shock protein 60 Hsp60s1 antibody
SPG13 antibody
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Target information

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: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).

Provider

Erpantech Laboratory

download

MSDS-AB-06-2276.pdf (177 downloads )