HSPD1 antibody (PerCP)

Catalog No. ABIN2484802

The Rabbit Polyclonal anti-HSPD1 antibody has been validated for WB, IHC, IF and ICC. It is suitable to detect HSPD1 in samples from Plasmodium falciparum.

Quick Overview for HSPD1 antibody (PerCP) (ABIN2484802)

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

Reactivity: Plasmodium falciparum

Host: Rabbit

Clonality: Polyclonal

Conjugate: This HSPD1 antibody is conjugated to PerCP

Application: Western Blotting (WB), Immunohistochemistry (IHC), Immunofluorescence (IF), Immunocytochemistry (ICC)

Product Details anti-HSPD1 Antibody (PerCP)

Specificity: Detects ~ 60 kDa. Cross-reacts with E.coli HSP60, GroEl.

Cross-Reactivity: Bacteria, Human, Plasmodium falciparum

Purification: Protein A Purified

Immunogen: Recombinant full length PfHSP60

Application Details

Application Notes:

• WB (1:2000)
• optimal dilutions for assays should be determined by the user.

Comment:

0.9 μg/ml of ABIN2484802 was sufficient for detection of PfHSP60 in 20 μg of P. falciparum lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.

Restrictions: For Research Use only

Handling

Format: Liquid

Concentration: 1.83 mg/mL

Buffer: PBS pH 7.4, 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

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). Another important function of HSP60 and HSP10 is their protective functions against infection and cellular stress. HSP60 has however been linked to a number of autoimmune diseases, as well as Alzheimer's, coronary artery diseases, MS, and diabetes (6-9).

NCBI Accession: XM_001347402

UniProt: P34940

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