GROEL recombinant protein

Recombinant Human GroEL (HSP60)

Cat. Num. AAA143379

• Gene Names: HSPD1; HLD4; CPN60; GROEL; HSP60; HSP65; SPG13; HSP-60; HuCHA60
• Purity: Greater than 95.0% as determined by SDS-PAGE.
• Synonyms: GroEL; Recombinant Human GroEL (HSP60); GroEL Human; GroEL (HSP60) Human Recombinant; CPN60; GROEL; HSP60; HSP65; SPG13; CHA60; GROL; crpA; mopA; 60 kDa heat shock protein mitochondrial; Heat shock protein 60; HSP-60; 60 kDa chaperonin; Chaperonin 60; Mitochondrial matrix protein P1; P60 lymphocyte protein; HuCHA60; HSPD1; GROEL recombinant protein

• Host: E Coli
• Purity/Purification: Greater than 95.0% as determined by SDS-PAGE.
• Form/Format: The GroEL protein contains 20mM Tris-HCl buffer pH-8.0, 5mM DTT and 10% Glycerol.; Sterile filtered colorless solution.
• 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
• Sequence Length: 573

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

Related Product Information for GROEL recombinant protein

Description: Recombinant Human GroEL, HSP60 produced in E Coli is a single, non-glycosylated polypeptide chain fused to a 20 a.a. His tag at N-terminus containing 593 amino acids (1-573 a.a.) and having a molecular mass of 63kDa.The HSP60 is purified by proprietary chromatographic techniques.

Introduction: GroEL, HSP60 is a chaperonin located in the mitochondria which is responsible for the transportation & refolding of proteins from the cytoplasm directly into the mitochondrial matrix. GroEL is regulated by the HSP10 cochaperonin, which is a single heptameric protein ring having a molecular mass of 10 kDa which form a unique complex with HSP60. HSP10, GroES 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.

Product Categories/Family for GROEL recombinant protein

Heat Shock Proteins; Recombinant Proteins; Heat Shock Protein

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 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; 60 kDa chaperonin; P60 lymphocyte protein; chaperonin 60; heat shock protein 65; 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; 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; p53 binding; lipopolysaccharide binding; chaperone binding; ubiquitin protein ligase binding; ATPase activity; unfolded protein binding; double-stranded RNA binding; DNA replication origin binding; ATP binding; single-stranded DNA binding

Biological Process: caspase activation; B cell proliferation; viral reproduction; T cell activation; B cell activation; protein stabilization; 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; 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 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