Analytical Data
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Gene name
hspX
- Application
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Alternative Names
hspX；acr；Alpha-crystallin
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Species
E.coli
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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
P0A5B8
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Expression Region
2-144aa
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AA Sequence
ATTLPVQRHPRSLFPEFSELFAAFPSFAGLRPTFDTRLMRLEDEMKEGRYEVRAELPGVDPDKDVDIMVRDGQLTIKAERTEQKDFDGRSEFAYGSFVRTVSLPVGADEDDIKATYDKGILTVSVAVSEGKPTEKHIQIRSTN
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Molecular Weight
18.1 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
HspX, also known as HSPX or Hsp16.3, is a member of the heat shock protein family, specifically associated with the stress response in various organisms, including mycobacteria. Primarily studied in Mycobacterium tuberculosis, HspX plays a crucial role in protecting bacterial cells from heat shock and other environmental stresses, thereby contributing to pathogen survival within the hostile environment of a host. Its expression is tightly regulated and increases significantly during stationary phase and under stress conditions, highlighting its role in mycobacterial adaptation and virulence. The study of recombinant HspX protein is pivotal for understanding its structure, function, and immunogenic properties. Research on HspX can provide insights into potential vaccine development and therapeutic targets for tuberculosis, particularly given that the current vaccine, Bacillus Calmette-Guérin (BCG), has limitations in providing long-lasting immunity. Recombinant HspX can also aid in elucidating the molecular mechanisms by which mycobacteria evade the host immune response, as it may interact with immune cells and modulate their functions. Overall, the exploration of recombinant HspX not only advances our understanding of bacterial stress responses but also holds promise for innovative strategies in combating mycobacterial infections.
