Clone:
REAL553
Type of antibody:
Releasable fluorochromes, Primary antibodies, Recombinant antibodies
Applications:
MICS, IHC, IF
Alternative names:
CAT

Specifications for Catalase Antibody, anti-human, REAdye_lease™

Overview

Clone REAL553 is an antibody fragment derived from the full Catalase antibody molecule. It displays no binding to Fc receptors. The recombinantly engineered antibody fragments are multimerized to form the REAdye_lease Complex to bind markers with high avidity.
Clone REAL553 recognizes catalase, a key antioxidant enzyme against oxidative stress. Catalase catalyzes the decomposition of hydrogen peroxide to water and oxygen and is present in the peroxisome of nearly all aerobic cells. Oxidative stress is hypothesized to play a role in the development of many chronic or late-onset diseases such as diabetes, asthma, Alzheimer's disease, systemic lupus erythematosus, rheumatoid arthritis, and cancers. Catalase promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells.
For removal of REAdye_lease fluorochromes for optional relabeling with different fluorochrome-conjugated REAdye_lease antibodies use the REAlease Support Kit (130-120-675).

Alternative names

CAT

Detailed product information

Technical specifications

CloneREAL553
Clonalitymonoclonal
Isotype controlControl Antibody
Hostcell line
Type of antibodyReleasable fluorochromes, Primary antibodies, Recombinant antibodies
Specieshuman
AntigenCatalase
Alternative names of antigenCAT
Distribution of antigenubiquitous, kidney, bone marrow, liver
RRIDAB_2857591

References for Catalase Antibody, anti-human, REAdye_lease™

Publications

  1. Böhm, B. et al. (2015) Extracellular localization of catalase is associated with the transformed state of malignant cells. Biol. Chem. Hoppe-Seyler 396(12): 1339-1356
  2. Glorieux, C. et al. (2015) Regulation of catalase expression in healthy and cancerous cells. Free Radic. Biol. Med. 87: 84-97
  3. Glorieux, C. et al. (2017) Catalase, a remarkable enzyme: targeting the oldest antioxidant enzyme to find a new cancer treatment approach. Biol. Chem. Hoppe-Seyler 398(10): 1095-1108