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HSP60 Recombinant Protein | HSPD1 recombinant protein

HSP60 Protein, Human, Recombinant (His & GST Tag)

Gene Names
HSPD1; HLD4; CPN60; GROEL; HSP60; HSP65; SPG13; HSP-60; HuCHA60
Purity
>90% as determined by SDS-PAGE
Synonyms
HSP60; HSP60 Protein; Human; Recombinant (His & GST Tag); Human HSPD1/HSP60 Protein (His & GST Tag); CPN60 Protein; GROEL Protein; HLD4 Protein; HSP-60 Protein; HSP65 Protein; HuCHA60 Protein; SPG13 Protein; heat shock 60kDa protein 1 (chaperonin); HSPD1 recombinant protein
Ordering
For Research Use Only!
Host
E Coli
Purity/Purification
>90% as determined by SDS-PAGE
Form/Format
Lyophilized from sterile PBS, pH7.4. Normally 5%-8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
Sequence
Leu2-Phe573
Species
Human
Predicted N Terminal
Met
Tag
N-GST & His
Protein Construction
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.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Preparation and Storage
Samples are stable for up to twelve months from date of receipt at -20 degree C to -80 degree C. Store it under sterile conditions at -20 degree C to -80 degree C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid.
They are shipped out with blue ice.

SDS-Page

SDS-Page
Related Product Information for HSPD1 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 clinically characterized by infantile-onset rotary nystagmus, progressive spastic paraplegia, neurologic regression, motor impairment, profound mental retardation. Death usually occurs within the first two decades of life.
References
Hansen J J, et al. (2002) Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60. Am J Hum Genet. 70: 1328-32.
Magen D, et al. (2008) Mitochondrial Hsp60 chaperonopathy causes an autosomal-recessive neurodegenerative disorder linked to brain hypomyelination and leukodystrophy. Am J Hum Genet. 83: 30-42.
Venner TJ, et al. (1990) Nucleotide sequences and novel structural features of human and Chinese hamster hsp60 (chaperonin) gene families. DNA Cell Biol. 9 (8): 545-52.

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
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; chaperonin 60; 60 kDa chaperonin; heat shock protein 65; P60 lymphocyte protein; mitochondrial matrix protein P1; short heat shock protein 60 Hsp60s1
Protein Family

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Product Notes

The HSPD1 (Catalog #AAA8120790) is a Recombinant Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. The amino acid sequence is listed below: Leu2-Phe57 3. It is sometimes possible for the material contained within the vial of "HSP60, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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