HSPD1 antibody (Atto 488)

Catalog No. ABIN2486149

Product Details anti-HSPD1 Antibody (Atto 488)

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

Reactivity: Human

Host: Rabbit

Clonality: Polyclonal

Conjugate: This HSPD1 antibody is conjugated to Atto 488

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

Specificity: Detects ~60 kDa.

Cross-Reactivity: Chicken, Cow, Dog, Hamster, Human, Mouse, Rabbit, Rat

Purification: Protein A Purified

Immunogen: Human HSP60 produced through recombinant DNA methods in E.coli

Application Details

Application Notes:

• WB (1:1000)
• ICC/IF (1:100)
• optimal dilutions for assays should be determined by the user.

Comment:

1 μg/ml of ABIN2486149 was sufficient for detection of HSP60 in 20 μg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using goat anti-mouse IgG as the secondary antibody.

Restrictions: For Research Use only

Handling

Format: Liquid

Concentration: 1 mg/mL

Buffer: PBS, 50 % glycerol, 0.09 % sodium azide, Storage buffer may change when conjugated

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: 4 °C

Storage Comment: Conjugated antibodies should be stored at 4°C

Target Details for HSPD1

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

Alternative Name: HSP60 (HSPD1 Products)

Background: In both prokaryotic and eukaryotic cells, the misfolding and aggregation of proteins during biogenesis and under conditions of cellular stress are prevented by molecular chaperones. Members of the HSP60 family of heat shock proteins are some of the best characterized chaperones. HSP60, also known as Cpn60 or GroEl, is an abundant protein synthesized constitutively in the cell that is induced to a higher concentration after brief cell shock. It is present in many species and exhibits a remarkable sequence homology among various counterparts in bacteria, plants, and mammals with more than half of the residues identical between bacterial and mammalian HSP60 (1-3). Whereas mammalian HSP60 is localized within the mitochondria, plant HSP60, or otherwise known as Rubisco-binding protein, is located in plant chloroplasts. It has been indicated that these proteins carry out a very important biological function due to the fact that HSP60 is present in so many 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 Mg2+ and ATP, iv) ATPase activity and v) a role in folding and assembly of oligomeric protein structures (4). 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 (5). HSP60 has however been linked to a number of autoimmune diseases, as well as Alzheimer's, coronary artery diseases, MS, and diabetes (6-9).

Gene ID: 3329

NCBI Accession: NP_002147

UniProt: P10809

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