HSPD1 / HSP60 recombinant protein

Recombinant Human HSPD1 / HSP60 Protein (His & GST tag)

Cat. Num. AAA2545810

• Gene Names: HSPD1; HLD4; CPN60; GROEL; HSP60; HSP65; SPG13; HSP-60; HuCHA60
• Purity: > 90 % as determined by SDS-PAGE
• Synonyms: HSPD1 / HSP60; Recombinant Human HSPD1 / HSP60 Protein (His & GST tag); HSPD1; CPN60; GROEL; HLD4; HSP60; HSP65; HuCHA60; SPG13; HSPD1 / HSP60 recombinant protein

• Host: E Coli
• Purity/Purification: > 90 % as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH 7.4
• Sequence Length: 573

• Application Notes: The recombinant human HSP60/GST chimera consists of 809 amino acids and has a calculated molecular mass of 88.7 KDa. It migrates as an approximately 52-65 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 human HSP60 (NP_955472.1) (Leu 2-Phe 573) was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.

NCBI and Uniprot Product Information

• NCBI GI #: 41399285
• NCBI GeneID: 3329
• NCBI Accession #: NP_955472.1
• NCBI GenBank Nucleotide #: NM_199440.1
• 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
• 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

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

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

Biological Process: 'de novo' protein folding; apoptotic mitochondrial changes; B cell activation; B cell cytokine production; B cell proliferation; caspase activation; chaperone-mediated protein complex assembly; isotype switching to IgG isotypes; MyD88-dependent toll-like receptor signaling pathway; negative regulation of apoptosis; positive regulation of apoptosis; 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 import into mitochondrial intermembrane space; protein maturation; protein refolding; protein stabilization; response to cold; response to unfolded protein; T cell activation

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