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Recombinant Mouse TNF Receptor I protein (ab185837)

Key features and details

  • Expression system: Escherichia coli
  • Purity: > 95% SDS-PAGE
  • Endotoxin level:
  • Suitable for: SDS-PAGE, HPLC

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Preparation and Storage

  • Alternative names

    • CD120a
    • FPF
    • MGC19588
    • p55
    • p55-R
    • p60
    • TBP1
    • TBPI
    • TNF R
    • TNF R55
    • TNF-R1
    • TNF-RI
    • TNFAR
    • TNFR-I
    • TNFR1
    • TNFR55
    • TNFR60
    • TNFRI
    • TNFRSF1a
    • TNR1A_HUMAN
    • Tumor necrosis factor receptor 1
    • Tumor necrosis factor receptor superfamily, member 1A
    • Tumor necrosis factor receptor type 1
    • Tumor necrosis factor receptor type I
    • Tumor necrosis factor-binding protein 1
    see all
  • Function

    Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase.
  • Involvement in disease

    Familial hibernian fever
    Multiple sclerosis 5
  • Sequence similarities

    Contains 1 death domain.
    Contains 4 TNFR-Cys repeats.
  • Domain

    The domain that induces A-SMASE is probably identical to the death domain. The N-SMASE activation domain (NSD) is both necessary and sufficient for activation of N-SMASE.
    Both the cytoplasmic membrane-proximal region and the C-terminal region containing the death domain are involved in the interaction with TRPC4AP.
  • Post-translational
    modifications

    The soluble form is produced from the membrane form by proteolytic processing.
  • Cellular localization

    Cell membrane. Golgi apparatus membrane. Secreted. A secreted form is produced through proteolytic processing and Secreted. Lacks a Golgi-retention motif, is not membrane bound and therefore is secreted.
  • Target information above from: UniProt accession P19438 The UniProt Consortium
    The Universal Protein Resource (UniProt) in 2010
    Nucleic Acids Res. 38:D142-D148 (2010) .

    Information by UniProt

Images

Please note: All products are "FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC PROCEDURES"
For licensing inquiries, please contact partnerships@abcam.com

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