HSPD1 / 60 kDa Heat Shock Protein Recombinant Protein | HSPD1 recombinant protein

Human HSPD1 / 60 kDa Heat Shock Protein, Mitochondrial Recombinant Protein

• Gene Names: HSPD1; HLD4; CPN60; GROEL; HSP60; HSP65; SPG13; HSP-60; HuCHA60
• Applications: ELISA, Western Blot
• Purity: >95% by SDS-PAGE
• Synonyms: HSPD1 / 60 kDa Heat Shock Protein; Human HSPD1 / 60 kDa Heat Shock Protein; Mitochondrial Recombinant Protein; 60 kDa heat shock protein; mitochondrial; 60 kDa chaperonin; Chaperonin 60; CPN60; Heat shock protein 60; HSP-60; HuCHA60; Mitochondrial matrix protein P1; P60 lymphocyte protein; HSP60; HSPD1 recombinant protein

• Host: E Coli
• Purity/Purification: >95% by SDS-PAGE
• Form/Format: Liquid; 50mM NaH2PO4, 500mM NaCl Buffer with 500mM Imidazole, 10% Glycerol (PH8.0)
• Concentration: Reconstitution Dependent (varies by lot)
• Sequence Length: 573

• Applicable Applications for HSPD1 recombinant protein: ELISA (EIA), Western Blot (WB), Antigen Protein (AP), Protein Array
• Species: Human
• Tag: His
• Subunit: (Microbial infection) Interacts with HBV protein X and HTLV-1 protein p40tax (PubMed:15120623, PubMed:1731090).
• Entry Function: 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.
• Preparation and Storage: Store at -20 degree C. Avoid repeated freezing and thawing.

NCBI and Uniprot Product Information

• NCBI GI #: 31542947
• NCBI GeneID: 3329
• NCBI Accession #: NP_002147.2
• NCBI GenBank Nucleotide #: NP_002147.2
• UniProt Accession #: P10809
• 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
• UniProt Entry Name: CH60_HUMAN

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

HSP60: Implicated in mitochondrial protein import and macromolecular assembly. May facilitate 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. Interacts with HRAS. Interacts with HBV protein X and HTLV-1 protein p40tax. Belongs to the chaperonin (HSP60) family.

Protein type: Chaperone; Mitochondrial

Chromosomal Location of Human Ortholog: 2q33.1

Cellular Component: extracellular space; protein complex; cell surface; mitochondrion; early endosome; coated pit; cytosol; secretory granule; membrane; mitochondrial matrix; cytoplasm; mitochondrial inner membrane; plasma membrane; lipopolysaccharide receptor complex; cyclin-dependent protein kinase activating kinase holoenzyme complex

Molecular Function: protein binding; lipopolysaccharide binding; p53 binding; ubiquitin protein ligase binding; chaperone binding; unfolded protein binding; double-stranded RNA binding; ATPase activity; DNA replication origin binding; ATP binding; single-stranded DNA binding

Biological Process: caspase activation; B cell proliferation; viral reproduction; B cell activation; protein stabilization; T cell activation; positive regulation of interleukin-12 production; positive regulation of apoptosis; protein maturation; isotype switching to IgG isotypes; positive regulation of interleukin-6 production; B cell cytokine production; positive regulation of interleukin-10 production; response to unfolded protein; MyD88-dependent toll-like receptor signaling pathway; positive regulation of interferon-gamma production; 'de novo' protein folding; protein refolding; positive regulation of T cell mediated immune response to tumor cell; positive regulation of T cell activation; chaperone-mediated protein complex assembly; positive regulation of interferon-alpha production; negative regulation of apoptosis; positive regulation of macrophage activation

Disease: Spastic Paraplegia 13, Autosomal Dominant; Leukodystrophy, Hypomyelinating, 4