This fast track antibody is not yet fully characterized. It is subject to these terms and conditions

Overview

Properties

Applications

  • Application notesThis antibody gave a positive result in ELISA against the immunizing peptide (ab39287).
    Not yet tested in other applications.

    Optimal dilutions/concentrations should be determined by the end user.
  • Target

    • FunctionInduces the collapse and paralysis of neuronal growth cones. Could potentially act as repulsive cues toward specific neuronal populations. Binds to neuropilin.
    • Sequence similaritiesBelongs to the semaphorin family.
      Contains 1 Ig-like C2-type (immunoglobulin-like) domain.
      Contains 1 PSI domain.
      Contains 1 Sema domain.
    • DomainStrong binding to neuropilin is mediated by the carboxy third of the protein.
    • Cellular localizationSecreted.
    • Information by UniProt
    • Database links
    • Alternative names
      • Coll 2 antibody
      • Coll2 antibody
      • Collapsin 2 antibody
      • SEM3D_HUMAN antibody
      • Sema domain immunoglobulin domain (Ig) short basic domain secreted (semaphorin) 3D antibody
      • Sema Z2 antibody
      • Sema3d antibody
      • Semaphorin-3D antibody
      • Semaphorin3D antibody
      see all

    Anti-Semaphorin 3D antibody images

    This Fast-Track antibody is not yet fully characterised. These images represent inconclusive preliminary data.

    • All lanes : Anti-Semaphorin 3D antibody (ab39288) at 1 µg/ml

      Lane 1 : Mouse brain tissue lysate - total protein (0 days) (ab7188)
      Lane 2 : Brain (Mouse) Tissue Lysate
      Lane 3 : Human brain tissue lysate - total protein (ab29466)

      Lysates/proteins at 10 µg per lane.

      Secondary
      Goat polyclonal to Rabbit IgG - H&L - Pre-Adsorbed (HRP) at 1/3000 dilution

      Performed under reducing conditions.

      Observed band size : 45 kDa (why is the actual band size different from the predicted?)

    References for Anti-Semaphorin 3D antibody (ab39288)

    ab39288 has not yet been referenced specifically in any publications.

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