Analytical Data
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Gene name
DNAJB2
- Application
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Alternative Names
DNAJB2；HSJ1；HSPF3;DnaJ homolog subfamily B member 2
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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
P25686
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Expression Region
1-277aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMASYYEILDVPRSASADDIKKAYRRKA LQWHPDKNPDNKEFAEKKFKEVAEAYEVLSDKHKREIYDRYGREGLTGTG TGPSRAEAGSGGPGFTFTFRSPEEVFREFFGSGDPFAELDDLGPFSELQN RGSRHSGPFFTFSSSFPGHSDFSSSSFSFSPGAGAFRSSTSTTFVQGRRI TTRRIMENGQERVEVEEDGQLKSVTINGVPDDLALGLELSRREQQPSVTS RSGGTQVQQTPASCPLDSDLSEDEDLQLAMAYSLSEMEAAGKKPADVF
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Molecular Weight
33 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
DNAJB2 is a member of the DnaJ family of heat shock proteins, which play a crucial role in protein folding, maintenance of protein homeostasis, and response to cellular stress. Research on DNAJB2 has gained attention due to its potential involvement in various biological processes and diseases, including cancer and neurodegenerative disorders. The unique structural characteristics and functional properties of DNAJB2 make it an appealing target for studies focused on its role as a molecular chaperone. Previous studies have demonstrated that DNAJB2 interacts with multiple target proteins, facilitating their proper folding and preventing aggregation, which is particularly important under stress conditions. Additionally, aberrations in DNAJB2 expression levels have been linked to certain pathological conditions, indicating its significance in cellular health. Consequently, researchers aim to explore the detailed mechanisms by which DNAJB2 exerts its effects within cells, and how recombinant forms of this protein can be used for therapeutic applications. By creating recombinant DNAJB2, scientists can investigate its interactions with other proteins and potential roles in disease mechanisms more effectively, paving the way for its application in targeted therapies and personalized medicine. Understanding the biochemical pathways involving DNAJB2 may offer new insights into disease treatment strategies and contribute to advancements in protein engineering and biotechnology.
