Human HSP60 ELISA Kit | HSPD1 elisa kit

Human HSP60 ELISA Kit

Cat. Num. AAA8291358

• Gene Names: HSPD1; HLD4; CPN60; GROEL; HSP60; HSP65; SPG13; HSP-60; HuCHA60
• Reactivity: Human
• Synonyms: HSP60; Human HSP60 ELISA Kit; 60 kDa heat shock protein; mitochondrial; 60 kDa chaperonin; Chaperonin 60; CPN60; Heat shock protein 60; HSP-60; Hsp60; HuCHA60; Mitochondrial matrix protein P1; P60 lymphocyte protein; HSPD1 elisa kit

• Reactivity: Human
• Specificity: The Human HSP60 ELISA Kit allows for the detection and quantification of endogenous levels of natural and/or recombinant Human HSP60 proteins within the range of 312 pg/ml - 20,000 pg/ml.
• Sequence Length: 158

• Samples: Cell culture supernates, serum, plasma, cell lysates, tissue homogenates
• Sensitivity: < 150 pg/ml
• Preparation and Storage: Store at 4 degree C for 6 months, store at -20 degree C for one year. Avoid freeze/thaw cycles.

Typical Testing Data/Standard Curve (for reference only)

Related Product Information for HSPD1 elisa kit

Principle of the Assay: The MyBioSource' Human HSP60 ELISA (Enzyme-Linked Immunosorbent Assay) kit is an in vitro enzyme-linked immunosorbent assay for the quantitative measurement of Human HSP60 in Cell Culture Supernates, Serum, Plasma, Cell Lysates, Tissue Homogenates. This assay employs an antibody specific for Human HSP60 coated on a 96-well plate. Standards and samples are pipetted into the wells and HSP60 present in a sample is bound to the wells by the immobilized antibody. The wells are washed and biotinylated anti-Human HSP60 antibody is added. After washing away unbound biotinylated antibody, HRP-conjugated streptavidin is pipetted to the wells. The wells are again washed, a TMB substrate solution is added to the wells and color develops in proportion to the amount of HSP60 bound. The Stop Solution changes the color from blue to yellow, and the intensity of the color is measured at 450 nm.

Background/Introduction: Heat shock proteins (HSPs) are a family of highly conserved stress response proteins. Heat shock proteins function primarily as molecular chaperones by facilitating the folding of other cellular proteins, preventing protein aggregation or targeting improperly folded proteins to specific degradative pathways. HSPs are typically expressed at low levels under normal physiological conditions but are dramatically upregulated in response to cellular stress. Heat Shock Protein 60 (HSP60), also known as Chaperonin 60 (CPN60), is a mitochondrial matrix protein belonging to a highly conserved family of molecular chaperone and stress response proteins. HSP60 plays a role in stabilizing and refolding proteins in response to heat-shock or other cellular stress.

NCBI and Uniprot Product Information

• NCBI GI #: 31542947
• NCBI GeneID: 3329
• NCBI Accession #: NP_002147.2
• NCBI GenBank Nucleotide #: NM_002156.4
• UniProt Accession #: P10809; Q38L19; Q9UCR6; B2R5M6; B7Z712
• Molecular Weight: 17,100 Da
• NCBI Official Full Name: 60 kDa heat shock protein, mitochondrial
• NCBI Official Synonym Full Names: heat shock protein family D (Hsp60) member 1
• NCBI Official Symbol: HSPD1
• NCBI Official Synonym Symbols: HLD4; CPN60; GROEL; HSP60; HSP65; SPG13; HSP-60; HuCHA60
• NCBI Protein Information: 60 kDa heat shock protein, mitochondrial
• UniProt Protein Name: 60 kDa heat shock protein, mitochondrial
• Protein Family: 60 kDa heat shock protein
• UniProt Gene Name: HSPD1
• UniProt Synonym Gene Names: HSP60; CPN60; HSP-60; Hsp60

NCBI Description

This gene encodes a member of the chaperonin family. The encoded mitochondrial protein may function as a signaling molecule in the innate immune system. This protein is essential for the folding and assembly of newly imported proteins in the mitochondria. This gene is adjacent to a related family member and the region between the 2 genes functions as a bidirectional promoter. Several pseudogenes have been associated with this gene. Two transcript variants encoding the same protein have been identified for this gene. Mutations associated with this gene cause autosomal recessive spastic paraplegia 13. [provided by RefSeq, Jun 2010]

Uniprot Description

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).