Human Heat Shock 60kD Protein 1, Chaperonin (HSPD1) RTU ELISA Kit | HSPD1 rtu elisa kit

Human Heat Shock 60kD Protein 1, Chaperonin (HSPD1) ELISA Kit

Cat. Num. AAA459983

• Gene Names: HSPD1; HLD4; CPN60; GROEL; HSP60; HSP65; SPG13; HSP-60; HuCHA60
• Reactivity: Human
• Synonyms: Heat Shock 60kD Protein 1; Chaperonin (HSPD1); Human Heat Shock 60kD Protein 1; Chaperonin (HSPD1) ELISA Kit; HSP60; GROEL; CPN60; HuCHA60; Heat Shock Protein 60; Spastic Paraplegia 13; Autosomal Dominant; 60 kDa chaperonin; Mitochondrial matrix protein P1; P60 lymphocyte protein; HSPD1 rtu elisa kit

• Reactivity: Human
• Sequence Length: 573

• Assay Type: Sandwich
• Samples: Serum, Plasma, Tissue Homogenates, Cell Lysates, Cell Culture Supernates or Other Biological Fluids.
• Detection Range: 0.156-10ng/mL
• Sensitivity: 0.063ng/mL
• RTU ELISA Kit's Advantage: The Ready-To-Use (RTU) Kits require fewer steps in setup and take less time to run. Detection Solutions are pre-diluted and total incubation time is shorter than many other ELISA Kits.
• Preparation and Storage: For unopened kits: All the reagents should be kept at 4 degree C upon receipt.; For opened kits: Once the kit is opened, the remaining reagents still need to be stored according to the above storage conditions. In addition, return the unused wells to the foil pouch containing the desiccant pack and reseal along entire edge of zip-seal.

Typical Testing Data/Standard Curve (for reference only)

Related Product Information for HSPD1 rtu elisa kit

Test Principle: The microtiter plate provided in this kit has been pre-coated with an antibody specific to HSPD1. Standards or samples are then added to the appropriate microtiter plate wells with a biotin-conjugated antibody preparation specific to HSPD1. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain HSPD1, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of HSPD1 in the samples is then determined by comparing the O.D. of the samples to the standard curve.

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).