Analytical Data
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Gene name
HSP70
- Application
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Alternative Names
HSPBP1;HSPBP;Hsp70-binding Protein 1
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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
P0DMV8
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Expression Region
1-641aa
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AA Sequence
MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK PKVQVSYKGE TKAFYPEEIS SMVLTKMKEI AEAYLGYPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI PTKQTQIFTT YSDNQPGVLI QVYEGERAMT KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV D
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Molecular Weight
70 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
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Protein Description
HSP70, or Heat Shock Protein 70, is a highly conserved molecular chaperone found in all eukaryotic cells, playing a crucial role in protein folding, maintenance, and degradation. Its expression is upregulated in response to environmental stressors such as heat, toxins, and oxidative stress, making it integral to cellular homeostasis and survival. Research has revealed that HSP70 not only assists in proper protein folding but also facilitates the transport of proteins across cellular membranes and the assembly of protein complexes. Furthermore, it is implicated in various cellular processes, including apoptosis, antigen presentation, and immune response. Due to its significant role in cellular stress responses and potential involvement in diseases, such as cancer and neurodegenerative disorders, HSP70 has emerged as a prominent target for therapeutic interventions. The study of recombinant HSP70 proteins has expanded our understanding of its structure and function, enabling the development of potential treatments that modulate HSP70 activity. Utilizing recombinant technology allows for large-scale production of HSP70, facilitating in-depth functional analyses and the investigation of its interactions with various proteins. This research is also paving the way for the design of HSP70-based vaccines and therapeutics, harnessing its chaperone properties to enhance immune responses. Overall, the study of HSP70 recombinant proteins is vital for both elucidating fundamental biological processes and exploring innovative strategies for disease management and therapy.
