Recombinant Human Toll-Interleukin 1 Receptor (TIR) Domain Containing Adaptor Protein

Recombinant Human Toll-Interleukin 1 Receptor (TIR) Domain Containing Adaptor Protein

Catalog Number:
P001414306ABE
Mfr. No.:
Abe32-5092
Price:
  • Size:
    10 µg
    Quantity:
    Add to Cart:
      • Overview
        • TIRAP Human Recombinant produced in E. coli is a single polypeptide chain containing 244 amino acids (1-221) and having a molecular mass of 26.3 kDa. TIRAP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. Toll-interleukin1 receptor (TIR) domain containing adaptor protein (TIRAP) contains 1 TIR domain. TIRAP is an adapter molecule linked with toll-like receptors. TIRAP is required in TLR2 and TLR4 signaling pathways in the innate immune response. TIRAP activates NF-kappa-B, MAPK1, MAPK3 and JNK, which subsequently results in cytokine secretion and the inflammatory response. TIRAP is highly expressed in the liver, kidney, spleen, skeletal muscle and heart. TIRAP is also found in peripheral blood leukocytes, lung, placenta, small intestine, thymus, colon and brain.

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      • Properties
        • Protein Name
          Toll-interleukin 1 receptor (TIR) domain containing adaptor protein, adapter protein wyatt, BACTS1, Mal, wyatt, Toll-like receptor adaptor protein, TIR domain-containing adapter protein, MyD88 adapter-like protein.
          Source
          E. coli
          Type
          Recombinant Proteins
          Purification
          Greater than 90% as determined by SDS-PAGE.
          Formulation
          The TIRAP solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 20% glycerol.
          Storage
          Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

          * For Research Use Only. Not for use in diagnostic/therapeutics procedures.

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