PRODUCT CODE: 1007-1

HSP60 Antibody (1007-1)

Applications

  • WB

  • ICC

  • IHC-P

  • FC

REACTIVITY

  • Human

  • Mouse

  • Rat

Western blot analysis on different cell lysates using anti-HSP60 rabbit polyclonal antibody
  • Western blot analysis on different cell lysates using anti-HSP60 rabbit polyclonal antibody
Western blot analysis on different cell lysates using anti-HSP60 rabbit polyclonal antibody

Applications

  • WB

  • ICC

  • IHC-P

  • FC

REACTIVITY

  • Human

  • Mouse

  • Rat

SPECIFICATIONS

Product Type

Rabbit polyclonal primary

Product Name

HSP60 Antibody (1007-1)

Immunogen

Peptide

Host

Rabbit

Positive Control

Hela, MCF-7, PC12, mouse kidney

Conjugation

Unconjugated

Clonality

Polyclonal

PROPERTIES

Form

Liquid

Storage Condition

Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.

Storage Buffer

1*PBS (pH7.4), 0.2% BSA, 25% Glycerol. Preservative: 0.05% Sodium Azide.

Concentration

1 ug/ul

PURIFICATION

Immunogen affinity purified

MOLECULAR WEIGHT

61kDa

Isotype

IgG

APPLICATION DILUTION

  • WB

  • 1:5000

TARGET

UNIPROT #

PROTEIN NAME

60 kDa heat shock protein, mitochondrial

GENE NAME

HSPD1

SYNONYMS

CPN60,HSP-60,Hsp60

SEQUENCE SIMILARITIES

Belongs to the chaperonin (HSP60) family.

SUBCELLULAR LOCATION

Mitochondrion matrix.

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. 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).