GroEL (Hsp60) Recombinant Protein | GroEL recombinant protein

Recombinant Human GroEL (Hsp60)

Cat. Num. AAA197040

• Gene Names: HSPD1; HLD4; CPN60; GROEL; HSP60; HSP65; SPG13; HSP-60; HuCHA60
• Purity: Greater than 95% as determined by SDS-PAGE and RP-HPLC.
• Synonyms: GroEL (Hsp60); Recombinant Human GroEL (Hsp60); GroEL recombinant protein

• Host: E Coli
• Specificity: Human GroEL (Hsp60)
• Purity/Purification: Greater than 95% as determined by SDS-PAGE and RP-HPLC.
• Form/Format: Sterile-filtered colorless solution contains 25mM Tris-HCl, pH 7.5, 100mM NaCl, 5mM DTT, and 10% glycerol. Purified by proprietary chromatographic techniques.
• Sequence: MGSSHHHHHH SSGLVPRGSH MLRLPTVFRQ MRPVSRVLAP HLTRAYAKDV KFGADARALMLQGVDLLADA VAVTMGPKGR TVIIEQSWGS PKVTKDGVTV AKSIDLKDKY KNIGAKLVQDVANNTNEEAG DGTTTATVLA RSIAKEGFEK ISKGANPVEI RRGVMLAVDA VIAELKKQSKPVTTPEEIAQ VATISANGDK EIGNIISDAM KKVGRKGVIT VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ DAYVLLSEKK ISSIQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL TLNLEDVQPH DLGKVGEVIV TKDDAMLLKG KGDKAQIEKR IQEIIEQLDV TTSEYEKEKL NERLAKLSDG VAVLKVGGTS DVEVNEKKDR VTDALNATRA AVEEGIVLGG GCALLRCIPA LDSLTPANED QKIGIEIIKR TLKIPAMTIA KNAGVEGSLI VEKIMQSSSE VGYDAMAGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT TAEVVVTEIP KEEKDPGMGA MGGMGGGMGG GMF

• Preparation and Storage: Store at 4 degree C if entire vial will be used within 2-4 weeks. Store at or below -20 degree C for longer periods of time. For long term storage, addition of a carrier protein (0.1% HSA or BSA) is recommended.

Related Product Information for GroEL recombinant protein

Hsp60 is a mitochondrial chaperonin responsible for transportation and refolding of proteins from the cytoplasm directly into the mitochondrial matrix. Hsp60 is regulated by the Hsp10 cochaperonin. Hsp10 coordinates the ATPase activity of the Hsp60 subunits in order to allow the release of bound polypeptide in a manner that is productive for its correct folding.

Recombinant Human GroEL (Hsp60) produced in E. coli is a single, nonglycosylated polypeptide chain containing 553 amino acids with a molecular weight of 63kDa.

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; Q53QD5; Q53SE2
• Molecular Weight: 61,055 Da
• NCBI Official Full Name: 60 kDa heat shock protein, mitochondrial
• NCBI Official Synonym Full Names: heat shock 60kDa protein 1 (chaperonin)
• 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; chaperonin 60; 60 kDa chaperonin; OTTHUMP00000205744; heat shock protein 65; P60 lymphocyte protein; mitochondrial matrix protein P1; short heat shock protein 60 Hsp60s1
• UniProt Protein Name: 60 kDa heat shock protein, mitochondrial
• UniProt Gene Name: HSPD1
• UniProt Synonym Gene Names: 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]

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: Mitochondrial; Chaperone

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

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

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