Analytical Data
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Gene name
HSPF3
- Application
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Alternative Names
HSPF3；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
Related Products
Protein Description
HSPF3, or Heat Shock Protein Family F Member 3, is a member of the heat shock protein family known for its role in cellular stress responses and protein folding. As a molecular chaperone, HSPF3 assists in preventing the aggregation of misfolded proteins, thereby playing a crucial role in maintaining cellular homeostasis, particularly under conditions of stress such as elevated temperatures or toxic environments. Recent research has highlighted the significance of HSPF3 in various cellular processes, including apoptosis, cell differentiation, and immune responses. Understanding the structure and function of HSPF3 is vital given its implications in various diseases, notably cancer and neurodegenerative disorders where protein misfolding is a common hallmark. The recombinant production of HSPF3 protein allows researchers to study its biochemical properties and potential therapeutic applications in greater detail. This research is particularly important as it may lead to the development of novel strategies for disease treatment or prevention by targeting the mechanisms by which HSPF3 operates. Furthermore, the ability to generate HSPF3 in a controlled laboratory setting opens avenues for exploring its interactions with other biomolecules and its role in complex biological systems. Thus, the study of recombinant HSPF3 not only enhances our understanding of cellular stress responses but also contributes to the broader field of protein homeostasis and its implications for human health.
