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PSPH antibody (AA 1-225)

The Mouse Monoclonal anti-PSPH antibody has been validated for WB, ELISA, ICC and IF. It is suitable to detect PSPH in samples from Human.
Catalog No. ABIN165446

Quick Overview for PSPH antibody (AA 1-225) (ABIN165446)

Target

See all PSPH Antibodies
PSPH (Phosphoserine Phosphatase (PSPH))

Reactivity

  • 35
  • 17
  • 6
  • 3
  • 3
  • 3
  • 3
  • 3
  • 3
  • 3
  • 1
  • 1
Human

Host

  • 27
  • 8
  • 1
Mouse

Clonality

  • 30
  • 6
Monoclonal

Conjugate

  • 26
  • 2
  • 2
  • 2
  • 2
  • 1
  • 1
This PSPH antibody is un-conjugated

Application

  • 29
  • 15
  • 9
  • 8
  • 6
  • 4
  • 2
  • 2
  • 2
  • 2
  • 1
Western Blotting (WB), ELISA, Immunocytochemistry (ICC), Immunofluorescence (IF)

Clone

3G12
  • Binding Specificity

    • 12
    • 9
    • 2
    • 2
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    AA 1-225

    Purification

    The antibody was purified from mouse ascitic fluids by protein-G affinity chromatography

    Immunogen

    Recombinant human PSP (1-225aa) purified from E. coli

    Isotype

    IgG1 kappa
  • 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

    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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