HSPD1 antibody (AA 80-109)

Catalog No. ABIN3031151

The Rabbit Polyclonal anti-HSPD1 antibody has been validated for WB, IHC and ELISA. It is suitable to detect HSPD1 in samples from Human and Mouse.

Quick Overview for HSPD1 antibody (AA 80-109) (ABIN3031151)

Target: HSPD1 (Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1))

Reactivity: Human, Mouse

Host: Rabbit

Clonality: Polyclonal

Conjugate: This HSPD1 antibody is un-conjugated

Application: Western Blotting (WB), Immunohistochemistry (IHC), ELISA

Product Details anti-HSPD1 Antibody

Binding Specificity: AA 80-109

Purification: Purified

Immunogen: A portion of amino acids 80-109 from the human protein was used as the immunogen for this HSP60 antibody.

Isotype: Ig Fraction

Application Details

Application Notes: Titration of the HSP60 antibody may be required due to differences in protocols and secondary/substrate sensitivity.\. Western blot: 1:1000,IHC (Paraffin): 1:50-1:100

Restrictions: For Research Use only

Handling

Format: Liquid

Buffer: In 1X PBS, pH 7.4, with 0.09 % sodium azide

Preservative: Sodium azide

Precaution of Use: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Storage: -20 °C

Storage Comment: Aliquot the HSP60 antibody and store frozen at -20°C or colder. Avoid repeated freeze-thaw cycles.

Target Details for HSPD1

Target: HSPD1 (Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1))

Alternative Name: HSP60

Background: Hsp60 is a member of a highly conserved family which includes molecular chaperones from several species such as plant Hsp60 (known as Rubisco binding protein), GroEL, the E.coli Hsp60 and 65 kDa major antigen of mycobacteria. In eukaryotes, Hsp60 is localized in the mitochondrial matrix and in plants Hsp60 is localized in the chloroplast. Mitochondria, chloroplasts and bacteria have a common ancestry (>1 billion years) and this fact together with the high degree of homology between the divegent Hsp60s would indicate that these proteins carry out a primitive but important function which is similar to all of these different species.The common characteristics of the Hsp60s from the divergent species are i) high abundance, ii) induction with environmental stress such as heat shock, iii) homo oligomeric structures of either 7 or 14 subunits which reversibly dissociate in the presence of magnesium ions and ATP, iv) ATPase activity and v) a role in folding and assembly of oligomeric protein structures. These similarities are supported by recent studies where the single ring human mitochondrial homolog, Hsp60 with its co chaperonin, Hsp10 were expressed in a E. coli strain, engineered so that the groE operon is under strict regulatory control. This study has demonstrated that expression of Hsp60-Hsp10 was able to carry out all essential in vivo functions of GroEL and its co chaperonin, GroES. Consistent with their functions as chaperones, Hsp60 and Hsp10 have been suggested to act as docking molecules with a passive role in the maturation of caspase processing. Data demonstrates that recombinant Hsp60 and Hsp10 have been shown to accelerate the activation of procaspase 3 by cytochrome c and dATP in an ATP dependent manner. Hsps are intracellular proteins which are thought to serve protective functions against infection and cellular stress, however several recent studies indicate that members of the Hsp60 family are linked to a number of autoimmune diseases, artherosclerosis and chlamydial disease.

UniProt: Q0VDF9

Pathways: Activation of Innate immune Response, Regulation of Leukocyte Mediated Immunity, Positive Regulation of Immune Effector Process, Production of Molecular Mediator of Immune Response, Positive Regulation of Endopeptidase Activity