• Product name
    Recombinant Human p53R2 protein
  • Protein length
    Protein fragment


  • Nature
  • Source
    Wheat germ
  • Amino Acid Sequence
    • Species
    • Sequence
    • Amino acids
      3 to 84
    • Tags
      GST tag N-Terminus


Our Abpromise guarantee covers the use of ab153320 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    Western blot


  • Form
  • Additional notes
    Protein concentration is above or equal to 0.05 mg/ml.
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    pH: 8.00
    Constituents: 0.31% Glutathione, 0.79% Tris HCl

General Info

  • Alternative names
    • DKFZp686M05248
    • MGC102856
    • MGC42116
    • MTDPS8A
    • MTDPS8B
    • p53 inducible ribonucleotide reductase small subunit 2 homolog
    • p53 inducible ribonucleotide reductase small subunit 2 like protein
    • P53 inducible ribonucleotide reductase small subunit 2 short form beta
    • p53 R2
    • p53-inducible ribonucleotide reductase small subunit 2-like protein
    • p53R2
    • Ribonucleoside diphosphate reductase M2 subunit B
    • Ribonucleoside-diphosphate reductase subunit M2 B
    • Ribonucleotide reductase M2 B
    • Ribonucleotide reductase M2 B (TP53 inducible)
    • Ribonucleotide reductase small subunit like 2 p53 inducible
    • RRM 2B
    • RRM2B
    • TP53 inducible ribonucleotide reductase M2 B
    • TP53-inducible ribonucleotide reductase M2 B
    see all
  • Function
    Plays a pivotal role in cell survival by repairing damaged DNA in a p53/TP53-dependent manner. Supplies deoxyribonucleotides for DNA repair in cells arrested at G1 or G2. Contains an iron-tyrosyl free radical center required for catalysis. Forms an active ribonucleotide reductase (RNR) complex with RRM1 which is expressed both in resting and proliferating cells in response to DNA damage.
  • Tissue specificity
    Widely expressed at a high level in skeletal muscle and at a weak level in thymus. Expressed in epithelial dysplasias and squamous cell carcinoma.
  • Pathway
    Genetic information processing; DNA replication.
  • Involvement in disease
    Defects in RRM2B are the cause of mitochondrial DNA depletion syndrome type 8A (MTDPS8A) [MIM:612075]. A disorder due to mitochondrial dysfunction characterized by various combinations of neonatal hypotonia, neurological deterioration, respiratory distress, lactic acidosis, and renal tubulopathy.
    Defects in RRM2B are the cause of mitochondrial DNA depletion syndrome type 8B (MTDPS8B) [MIM:612075]. A disease due to mitochondrial dysfunction and characterized by ophthalmoplegia, ptosis, gastrointestinal dysmotility, cachexia, peripheral neuropathy.
    Defects in RRM2B are the cause of progressive external ophthalmoplegia with mitochondrial DNA deletions autosomal dominant type 5 (PEOA5) [MIM:613077]. A disorder characterized by progressive weakness of ocular muscles and levator muscle of the upper eyelid. In a minority of cases, it is associated with skeletal myopathy, which predominantly involves axial or proximal muscles and which causes abnormal fatigability and even permanent muscle weakness. Ragged-red fibers and atrophy are found on muscle biopsy. A large proportion of chronic ophthalmoplegias are associated with other symptoms, leading to a multisystemic pattern of this disease. Additional symptoms are variable, and may include cataracts, hearing loss, sensory axonal neuropathy, ataxia, depression, hypogonadism, and parkinsonism.
  • Sequence similarities
    Belongs to the ribonucleoside diphosphate reductase small chain family.
  • Cellular localization
    Cytoplasm. Nucleus. Translocates from cytoplasm to nucleus in response to DNA damage.
  • Information by UniProt


  • ab153320 on a 12.5% SDS-PAGE stained with Coomassie Blue.


ab153320 has not yet been referenced specifically in any publications.

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