HSP10 recombinant protein

HSP10, 1-102aa, Human, E Coli

Cat. Num. AAA203119

• Gene Names: HSPE1; EPF; CPN10; GROES; HSP10
• Applications: SDS-Page
• Purity: > 95% by SDS-PAGE
• Synonyms: HSP10; 1-102aa; Human; E Coli; Heat shock protein 10; Chaperonin 10; CPN10; GroES; Heat shock protein 10 10 kDa chaperonin; HSPE 1; HSPE1; 10 kDa heat shock protein mitochondrial; Cpn 10; Early pregnancy factor; EPF; Heat shock 10kD protein 1; Heat shock 10kD protein 1 chaperonin 10; Heat shock 10kDa protein 1; HSP 10; Heat shock 10kDa protein 1 chaperonin 10; ; HSP10 recombinant protein

• Host: E Coli
• Purity/Purification: > 95% by SDS-PAGE
• Form/Format: Liquid in 20mM Tris pH 8.0, 50mM NaCl
• Concentration: 1 mg/ml (determined by Bradford assay) (varies by lot)
• Sequence Positions: 1-102
• Sequence: MAGQAFRKFL PLFDRVLVER SAAETVTKGG IMLPEKSQGK VLQATVVAVG SGSKGKGGEI QPVSVKVGDK VLLPEYGGTK VVLDDKDYFL FRDGDILGKY VD
• Sequence Length: 102

• Applicable Applications for HSP10 recombinant protein: SDS-PAGE
• Tag: Non-tagged
• Endotoxin Level: < 1.0 EU per 1 microgram of protein (determined by LAL method)
• Preparation and Storage: Can be stored at 2-8°C for 1 week.; For long term storage, aliquot and store at -20°C to -80°C.; Avoid repeated freezing and thawing cycles.

SDS-Page

(3 ug by SDS-PAGE under reducing condition and visualized by coomasie blue stain)

Related Product Information for HSP10 recombinant protein

Heat shock protein (HSP) 10 is a member of the highly conserved group of molecular chaperons, which are necessary for efficient folding of many proteins in normal and stress conditions and have been implicated in several human diseases. HSP10 is the ~10kD mammalian equivalent to GroES of E Coli. The function of Hsp10 is to bind Hsp60 (also known as chaperonin-60), in the presence of ATP, thereby promoting a conformational change in Hsp60 and enclosing the protein substrate within the complex. ATP hydrolysis by Hsp60 destabilizes the Hsp60/ Hsp10 complex, allowing it to dissociate and release the substrate protein. Recombinant human HSP10 was expressed in E Coli and purified by using conventional chromatography techniques.

Product Categories/Family for HSP10 recombinant protein

Heat Shock Proteins

References

Lin KM., et al. (2004), FASEB J. 18 (9):1004-6; Hohfeld J., et al. (1994), J. Cell BIol. 126 (2):305-15

NCBI and Uniprot Product Information

• NCBI GI #: 4504523
• NCBI GeneID: 3336
• NCBI Accession #: NP_002148
• NCBI GenBank Nucleotide #: NM_002157.2
• UniProt Accession #: P61604; O95421; Q04984; Q53X54; Q9UDH0
• Molecular Weight: 10 kDa (102 aa), confirmed by MALDI-TOF.
• NCBI Official Full Name: 10 kDa heat shock protein, mitochondrial
• NCBI Official Synonym Full Names: heat shock protein family E (Hsp10) member 1
• NCBI Official Symbol: HSPE1
• NCBI Official Synonym Symbols: EPF; CPN10; GROES; HSP10
• NCBI Protein Information: 10 kDa heat shock protein, mitochondrial
• UniProt Protein Name: 10 kDa heat shock protein, mitochondrial
• Protein Family: 10 kDa heat shock protein
• UniProt Gene Name: HSPE1
• UniProt Synonym Gene Names: Hsp10; CPN10; EPF

NCBI Description

This gene encodes a major heat shock protein which functions as a chaperonin. Its structure consists of a heptameric ring which binds to another heat shock protein in order to form a symmetric, functional heterodimer which enhances protein folding in an ATP-dependent manner. This gene and its co-chaperonin, HSPD1, are arranged in a head-to-head orientation on chromosome 2. Naturally occurring read-through transcription occurs between this locus and the neighboring locus MOBKL3.[provided by RefSeq, Feb 2011]

Uniprot Description

Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates 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 (PubMed:7912672, PubMed:1346131, PubMed:11422376). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable).