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PSPH antibody (AA 1-225)

PSPH Reactivity: Human WB, ELISA, ICC, IF Host: Mouse Monoclonal 3G12 unconjugated
Catalog No. ABIN165446
  • Target See all PSPH Antibodies
    PSPH (Phosphoserine Phosphatase (PSPH))
    Binding Specificity
    • 14
    • 9
    • 2
    • 2
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    AA 1-225
    Reactivity
    • 37
    • 17
    • 6
    • 3
    • 3
    • 3
    • 3
    • 3
    • 3
    • 3
    • 1
    • 1
    Human
    Host
    • 28
    • 9
    • 1
    Mouse
    Clonality
    • 31
    • 7
    Monoclonal
    Conjugate
    • 28
    • 2
    • 2
    • 2
    • 2
    • 1
    • 1
    This PSPH antibody is un-conjugated
    Application
    • 31
    • 17
    • 10
    • 6
    • 6
    • 4
    • 3
    • 2
    • 2
    • 2
    • 2
    Western Blotting (WB), ELISA, Immunocytochemistry (ICC), Immunofluorescence (IF)
    Purification
    The antibody was purified from mouse ascitic fluids by protein-G affinity chromatography
    Immunogen
    Recombinant human PSP (1-225aa) purified from E. coli
    Clone
    3G12
    Isotype
    IgG1 kappa
    Top Product
    Discover our top product PSPH Primary Antibody
  • Application Notes
    Recommended dilution 1:1000
    Restrictions
    For Research Use only
  • Format
    Liquid
    Concentration
    1 mg/mL
    Buffer
    In Phosphate-Buffered Saline (pH7.4) with 0.1% Sodium Azide
    Preservative
    Sodium azide
    Precaution of Use
    This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
    Storage
    4 °C,-20 °C,-80 °C
    Storage Comment
    Can be stored at +2°C to +8°C for 1 week. For long term storage, aliquot and store at -20°C to -80°C. Avoid repeated freezing and thawing cycles.
  • Target
    PSPH (Phosphoserine Phosphatase (PSPH))
    Alternative Name
    Phosphoserine phosphatase/PSPH (PSPH Products)
    Background
    Human phosphoserine phosphatase (HPSP), specific for D- and L- phosphoserine, has been identified in all human tissues. HPSP is a Mg (2+) -dependent phosphoserine phosphatase. The three dimensional structure of HPSP reveals the structural and functional role of the divalent cation in the active site of phosphatases. In particular, the complex structures reveal that the open-closed environmental change of the active site, generated by local rearrangement of the alpha-helical bundle domain, is important for the substrate recognition and hydrolysis.
    NCBI Accession
    NP_004568
    Pathways
    Warburg Effect
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