HSPD1 / HSP60 recombinant protein

Recombinant Mouse HSPD1 / HSP60 Protein (His tag)

Cat. Num. AAA2546891

• Gene Names: Hspd1; 60kDa; Hsp60
• Purity: > 95 % as determined by SDS-PAGE
• Synonyms: HSPD1 / HSP60; Recombinant Mouse HSPD1 / HSP60 Protein (His tag); Hsp60; HSPD1 / HSP60 recombinant protein

• Host: E Coli
• Purity/Purification: > 95 % as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH 7.4
• Sequence Length: 573

• Application Notes: The recombinant mouse HSP60 consisting of 583 amino acids and has a calculated molecular mass of 62.3 kDa. rmHSP60 migrates as an approximately 58 kDa band in SDS-PAGE under reducing conditions.
• Predicted N Terminal: Met
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

Related Product Information for HSPD1 / HSP60 recombinant protein

Background: HSPD1, also known as HSP60, is a member of the chaperonin family. HSPD1 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. It may also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. HSPD1 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. Mutations associated with this gene cause autosomal recessive spastic paraplegia 13.Defects in HSPD1 are a cause of spastic paraplegia autosomal dominant type 13 (SPG13). Spastic paraplegia is a degenerative spinal cord disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Defects in HSPD1 are the cause of leukodystrophy hypomyelinating type 4 (HLD4); also called mitochondrial HSP60 chaperonopathy or MitCHAP-60 disease. HLD4 is a severe autosomal recessive hypomyelinating leukodystrophy. HSPD1 is cinically characterized by infantile-onset rotary nystagmus, progressive spastic paraplegia, neurologic regression, motor impairment, profound mental retardation. Death usually occurrs within the first two decades of life.

Description: A DNA sequence encoding the mouse HSP60 (NP_034607.3) (Leu 2-Phe 573) was expressed, with a polyhistide tag at the N-terminus.

NCBI and Uniprot Product Information

• NCBI GI #: 183396771
• NCBI GeneID: 15510
• NCBI Accession #: NP_034607.3
• NCBI GenBank Nucleotide #: NM_010477.4
• UniProt Accession #: P63038; P19226; P19227; P97602; Q3KQP2; Q3UIP0; Q8C2C7; Q8VEF4
• Molecular Weight: 27,015 Da
• NCBI Official Full Name: 60 kDa heat shock protein, mitochondrial
• NCBI Official Synonym Full Names: heat shock protein 1 (chaperonin)
• NCBI Official Symbol: Hspd1
• NCBI Official Synonym Symbols: 60kDa; Hsp60
• NCBI Protein Information: 60 kDa heat shock protein, mitochondrial
• UniProt Protein Name: 60 kDa heat shock protein, mitochondrial
• UniProt Gene Name: Hspd1
• UniProt Synonym Gene Names: Hsp60; CPN60; HSP-60; Hsp60

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: 1|1 C1.2

Cellular Component: cell surface; coated pit; cyclin-dependent protein kinase activating kinase holoenzyme complex; cytoplasm; cytosol; early endosome; extracellular matrix; extracellular space; Golgi apparatus; intracellular membrane-bound organelle; lipid raft; lipopolysaccharide receptor complex; membrane; mitochondrial crista; mitochondrial inner membrane; mitochondrion; myelin sheath; peroxisomal matrix; plasma membrane; protein complex; rough endoplasmic reticulum; secretory granule

Molecular Function: chaperone binding; double-stranded RNA binding; insulin binding; lipopolysaccharide binding; misfolded protein binding; p53 binding; protease binding; protein complex binding; protein heterodimerization activity; ubiquitin protein ligase binding

Biological Process: apoptotic mitochondrial changes; B cell activation; B cell cytokine production; B cell proliferation; caspase activation; chaperone cofactor-dependent protein folding; detection of misfolded protein; isotype switching to IgG isotypes; MyD88-dependent toll-like receptor signaling pathway; negative regulation of apoptosis; negative regulation of neuron apoptosis; positive regulation of apoptosis; positive regulation of inflammatory response; positive regulation of interferon-alpha production; positive regulation of interferon-gamma production; positive regulation of interleukin-10 production; positive regulation of interleukin-12 production; positive regulation of interleukin-6 production; positive regulation of macrophage activation; positive regulation of T cell activation; positive regulation of T cell mediated immune response to tumor cell; protein refolding; protein stabilization; response to unfolded protein; T cell activation