Analytical Data
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Gene name
HSP70/DnaK
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简介
The HSP70/DnaK protein is a molecular chaperone that primarily responds to stress, especially heat shock. It plays a crucial role in helping proteins fold correctly and prevent misfolding or aggregation during cellular stress. HSP70/DnaK Protein, E. coli (P.pastoris, His) is the recombinant E. coli-derived HSP70/DnaK protein, expressed by P. pastoris , with N-6*His labeled tag.
- Application
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Alternative Names
dnaK; HSP70; Heat shock 70kDa protein; Heat shock protein 70
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Species
E.coli
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Source
P. pastoris
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q1RGI8
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Expression Region
M1-K638
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AA Sequence
MGKIIGIDLGTTNSCVAIMDGTTPRVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQRDVSIMPFKIIAADNGDAWVEVKGQKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGLEVKRIINEPTAAALAYGLDKGTGNRTIAVYDLGGGTFDISIIEIDEVDGEKTFEVLATNGDTHLGGEDFDSRLINYLVEEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIEPLKVALQDAGLSVSDIDDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTGDVKDVLLLDVTPLSLGIETMGGVMTTLIAKNTTIPTKHSQVFSTAEDNQSAVTIHVLQGERKRAADNKSLGQFNLDGINPAPRGMPQIEVTFDIDADGILHVSAKDKNSGKEQKITIKASSGLNEDEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPADDKTAIESALTALETALKGEDKAAIEAKMQELAQVSQKLMEIAQQQHAQQQTAGADASANNAKDDDVVDAEFEEVKDKK
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Protein Length
Full Length
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Molecular Weight
71.1 kDa
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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
Related Products
Protein Description
The HSP70 family of heat shock proteins, including DnaK in bacteria, plays a crucial role in protein folding, stabilization, and degradation under stress conditions, such as elevated temperatures or denaturing environments. These molecular chaperones are involved in preventing misfolding and aggregation of proteins, thereby maintaining cellular homeostasis. Due to their essential functions in cellular stress response and their involvement in various pathological conditions—including neurodegenerative diseases and cancer—HSP70 proteins, particularly the well-studied DnaK protein, have garnered significant attention in research. Recombinant DnaK protein is frequently utilized in studies to elucidate its molecular mechanisms, interactions with client proteins, and its role in cellular pathways. Advanced techniques such as X-ray crystallography and cryo-electron microscopy have been employed to investigate the structural features of DnaK, enhancing our understanding of its chaperone activity. Additionally, the exploration of DnaK's interactions with co-chaperones and its regulation under stress conditions provides insight into its potential therapeutic applications. As a model for mammalian HSP70s, bacterial DnaK offers a plethora of possibilities for biotechnological applications, including its use in the production of recombinant proteins and vaccine development. Consequently, ongoing research into HSP70/DnaK not only enriches our knowledge of cellular stress responses but also holds promise for advancing medical and biotechnological applications.
