Rabbit Polyclonal ACR antibody. Suitable for WB and reacts with Transfected cell lysate - Mycobacterium tuberculosis samples. Immunogen corresponding to Recombinant Fragment Protein within Mycobacterium tuberculosis H37Rv hspX.
pH: 7.4
Preservative: 0.0975% Sodium azide
Constituents: PBS
WB | |
---|---|
Mycobacterium tuberculosis | Predicted |
Transfected cell lysate - Mycobacterium tuberculosis | Tested |
Species | Dilution info | Notes |
---|---|---|
Species Transfected cell lysate - Mycobacterium tuberculosis | Dilution info 1 µg/mL | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Mycobacterium tuberculosis | Dilution info - | Notes - |
Acts as a chaperone, as it has a significant ability to suppress the thermal denaturation of alcohol dehydrogenase. Cells overexpressing this gene grow more slowly than wild-type cells, and are less susceptible to autolysis following saturation of the culture in vitro, suggesting this protein may slow down the growth rate of M.tuberculosis in culture and by extension during macrophage infection.
Alpha-crystallin hspX
acr, Rv2031c, MTV018.18c, hspX, Alpha-crystallin, Acr, 14 kDa antigen, 16 kDa antigen, HSP 16.3, Nox16
Rabbit Polyclonal ACR antibody. Suitable for WB and reacts with Transfected cell lysate - Mycobacterium tuberculosis samples. Immunogen corresponding to Recombinant Fragment Protein within Mycobacterium tuberculosis H37Rv hspX.
pH: 7.4
Preservative: 0.0975% Sodium azide
Constituents: PBS
Reacts with Mycobacterium tuberculosis Alpha-crystallin hspX.
Purity: > 95% (by SDS-PAGE).
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Alpha-crystallin hspX also known as heat shock protein X or Acr1 functions as a molecular chaperone within cells. It helps proteins maintain their proper folding under stress conditions preventing aggregation. With a molecular weight of approximately 16 kDa alpha-crystallin hspX is expressed in various tissues including the eye lens and certain types of bacteria like Mycobacterium tuberculosis. This protein plays a significant role in cellular defense against environmental stressors.
Alpha-crystallin hspX contributes to the stability and transparency of the eye lens by avoiding protein aggregation and maintaining lens crystallin clarity. In bacteria it forms part of a complex that assists in survival under hostile conditions such as heat shock or nutrient deprivation promoting bacterial persistence. This protein features small heat shock protein domains allowing it to interact with unstable proteins facilitating their refolding or marking them for degradation.
Alpha-crystallin hspX engages in the stress response pathway protecting cells under various stress scenarios. In the eye lens it relates to the maintenance of lens transparency through the interaction with other crystallins. In bacterial cells it connects to the dormancy survival programs aiding in the organism's ability to withstand prolonged periods in hostile environments. Alpha-crystallin hspX often associates with other heat shock proteins enhancing the cell's ability to survive stress.
Alpha-crystallin hspX links to cataract formation due to its role in maintaining lens transparency. A disruption in its function can lead to protein aggregation contributing to lens opacity. Another connection exists with tuberculosis where it influences the bacteria's ability to remain dormant in the host. The interaction between alpha-crystallin hspX and mycobacterial latency proteins is important as it aids in the pathogen's persistence within the host’s immune system complicating treatment and eradication strategies.
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This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
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All lanes: Western blot - Anti-Alpha-crystallin hspX antibody (ab231177) at 1 µg/mL
Lane 1: Non-transfected E.coli lysate
Lane 2: Mycobacterium tuberculosis Alpha-crystallin hspX transfected E.coli lysate
Predicted band size: 16 kDa
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