Analytical Data
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Gene name
HSPD1 / HSP60
- Application
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Alternative Names
HSPD1 / HSP60;
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P10809
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Expression Region
27-573aa
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AA Sequence
AKDV KFGADARALM LQGVDLLADA VAVTMGPKGR TVIIEQSWGS PKVTKDGVTV AKSIDLKDKY KNIGAKLVQD VANNTNEEAG DGTTTATVLA RSIAKEGFEK ISKGANPVEI RRGVMLAVDA VIAELKKQSK PVTTPEEIAQ 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
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
HSPD1, also known as Heat Shock Protein 60 (HSP60), is a highly conserved mitochondrial chaperonin that plays a crucial role in protein folding and assembly within the mitochondria. It facilitates the proper folding of newly synthesized proteins, thereby maintaining mitochondrial function and cellular homeostasis. Dysregulation or mutations in HSPD1 have been linked to various diseases, including neurodegenerative disorders and certain types of cancer. The study of recombinant HSPD1, or HSP60, has garnered attention as researchers seek to better understand its functional mechanisms and interactions with other cellular components. Recombinant protein technology allows for the production of HSP60 in vitro, enabling researchers to investigate its structure, dynamics, and role in diseases more effectively. Additionally, recombinant HSPD1 has potential therapeutic applications, including the development of vaccines and targeted therapies that harness the immune response against cancer cells or aberrant proteins. The exploration of HSPD1/HSP60 as a biomarker for disease progression and prognosis is also an emerging field, shedding light on its potential role in diagnostic and therapeutic strategies. Thus, the study of HSPD1/HSP60 recombinant protein not only contributes to our understanding of mitochondrial biology but also holds promise for the advancement of medical research and therapeutic interventions.











