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Recombinant Human Inverted formin-2 (INF2), Truncated

ACP17679

Number
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High Purity LevelsPrecision and ReliabilityCustomization Options

Specifications


Cat.No ACP17679 Target NameINF2
FormLyophilized powderExpression SystemCustom Production. Please inquire and provide the desire expression system.
Protein LengthPartialPurity>85% (SDS-PAGE)
Storage Buffer5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0.

Immunogen Information


Target SpeciesHumanUniprot IDQ27J81
Background Information
  • Uniprot Id

    Q27J81

  • Target Species

    Human

  • Target Name

    INF2

  • Target Full Name

    Inverted formin-2

  • Target Function

    Severs actin filaments and accelerates their polymerization and depolymerization.

  • Target Involvement

    Focal segmental glomerulosclerosis 5 (FSGS5); Charcot-Marie-Tooth disease, dominant, intermediate type, E (CMTDIE)

  • Target Subcellular Location

    Cytoplasm, perinuclear region.

  • Target Protein Families

    Formin homology family

  • Target Tissue Specificity

    Widely expressed. In the kidney, expression is apparent in podocytes and some tubule cells.

  • Target Synonyms

    C14orf151; C14orf173; CMTDIE; DKFZp762A0214; FLJ22056; FSGS5; HBEAG binding protein 2 binding protein C; HBEBP2 binding protein C; HBEBP2-binding protein C; INF 2; inf2; INF2_HUMAN; Inverted formin 2; Inverted formin FH2 and WH2 domain containing; Inverted formin-2; MGC13251; pp9484

  • Target Background

    This gene represents a member of the formin family of proteins. It is considered a diaphanous formin due to the presence of a diaphanous inhibitory domain located at the N-terminus of the encoded protein. Studies of a similar mouse protein indicate that the protein encoded by this locus may function in polymerization and depolymerization of actin filaments. Mutations at this locus have been associated with focal segmental glomerulosclerosis 5.

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