Heat Shock 60kD Protein 1, Chaperonin (HSPD1) Recombinant Protein | HSPD1 recombinant protein

Recombinant Heat Shock 60kD Protein 1, Chaperonin (HSPD1)

Cat. Num. AAA2011597

• Gene Names: HSPD1; HLD4; CPN60; GROEL; HSP60; HSP65; SPG13; HSP-60; HuCHA60
• Applications: SDS-Page, Western Blot, ELISA, Immunoprecipitation
• Purity: > 95%
• Synonyms: Heat Shock 60kD Protein 1; Chaperonin (HSPD1); Recombinant Heat Shock 60kD Protein 1; HSPD1 recombinant protein

• Host: E Coli
• Purity/Purification: > 95%
• Form/Format: Supplied as lyophilized form in PBS,pH7.4, containing 5% sucrose, 0.01% sarcosyl.
• Sequence: The target protein is fused with N-terminal His-Tag, its sequence is listed below.; MGHHHHHHSGS-ATISANGDK EIGNIISDAM KKVGRKGVIT VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ DAYVLLSEKK ISSIQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL TLNLEDVQPH DLG
• Sequence Length: 573

• Applicable Applications for HSPD1 recombinant protein: SDS-PAGE, Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP)
• Organism: Homo sapiens (Human)
• Expression System: Prokaryotic expression
• Residues: Ala172~Gly343 (Accession # P10809) with N-terminal His-Tag
• Endotoxin Level: <1.0EU per 1ug (determined by the LAL method)
• Reconstitution: Reconstitute in sterile PBS, pH7.2-pH7.4.
• Preparation and Storage: Avoid repeated freeze/thaw cycles. Store at 2-8 degree C for one month. Aliquot and store at -80 degree C for 12 months.; Stability Test: The thermal stability is described by the loss rate of the targetprotein. The loss rate was determined by accelerated thermal degradation test,that is, incubate the protein at 37 degree C for 48h, and no obvious degradation andprecipitation were observed. (Referring from China Biological Products Standard,which was calculated by the Arrhenius equation.) The loss of this protein is lessthan 5% within the expiration date under appropriate storage condition.

SDS-Page

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
• Molecular Weight: 19.8kDa
• 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; 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
• 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; cell surface; protein complex; mitochondrion; early endosome; coated pit; cytosol; secretory granule; membrane; mitochondrial matrix; mitochondrial inner membrane; cytoplasm; 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; double-stranded RNA binding; unfolded protein binding; DNA replication origin binding; single-stranded DNA binding; ATP binding

Biological Process: B cell proliferation; caspase activation; 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; 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