Cat: PA1000-1846

Recombinant Human LTA Protein,His

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Analytical Data

  • Gene name

    LTA

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    LTA;TNFB;TNFSF1;Lymphotoxin-alpha

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P01374

  • Expression Region

    35-205aa

  • AA Sequence

    LPGVGLTPSAAQTARQHPKMHLAHSTLKPAAHLIGDPSKQNSLLWRANTD RAFLQDGFSLSNNSLLVPTSGIYFVYSQVVFSGKAYSPKATSSPLYLAHE VQLFSSQYPFHVPLLSSQKMVYPGLQEPWLHSMYHGAAFQLTQGDQLSTH TDGIPHLVLSPSTVFFGAFAL

  • Molecular Weight

    19 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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.

  • 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.

  • 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.

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Protein Description

LTA (Lipoteichoic Acid)-binding proteins, particularly those derived from bacterial sources, have gained increasing attention in recent years due to their significant roles in immune response and microbial pathogenesis. These proteins play a crucial role in the recognition and binding of LTA, a component of the Gram-positive bacterial cell wall, which is crucial for maintaining cell integrity and influencing the bacterial interaction with host tissues. Understanding LTA-binding proteins is vital as they participate in various biological processes, including bacterial adhesion, immune evasion, and modulation of inflammatory responses. Researchers have focused on characterizing these proteins to uncover their mechanisms of action, which could lead to novel therapeutic strategies against bacterial infections and inflammation-related diseases. Additionally, studies have demonstrated that LTA-binding proteins can be exploited in vaccine development or as potential antimicrobial agents aimed at targeting Gram-positive bacteria. Moreover, the ability of these proteins to modulate immune responses makes them of interest in the context of autoimmune diseases and cancer therapies. Thus, investigating the structural and functional aspects of LTA-binding proteins provides valuable insights into their potential applications in both basic and applied biomedical research.

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