Arginase-1 Antibody – 150Nd

Catalog: 715001                                        Clone: EPR6672(B)                                          Isotype: Rabbit IgG
Reactivity: Human*
Storage: Arginase-1 antibody is supplied in antibody stabilizer with 0.05% sodium azide. Store at 4°C
IHC: Arginase-1 antibody staining of  FFPE human liver
MIBI: Arginase-1 antibody staining  (cyan) of FFPE human liver, counterstained with Histone H3 (magenta)
IHC: Arginase-1 antibody staining of  FFPE human thymus
MIBI: Arginase-1 antibody staining
(cyan) of FFPE human thymus, counterstained with Histone H3 (magenta)
Background: Arginase-1 is expressed by liver cells, myeloid-derived suppressor cells (MDSCs), macrophages, and neutrophils.  In mammals, there are three enzymes that metabolise arginine: two arginase isoforms  (ARG1, ARG2) and inducible nitric oxide synthase (iNOS). Arginase-1 catalyzes the breakdown of L-arginine into L-ornithine and urea as the final step in the urea cycle.  L-arginine is a  necessary metabolite for T cell receptor signaling and T cell proliferation. Arginase is induced by inflammation. In cancer, MDSCs within the tumor microenvironment (TME) produce arginase-1 resulting in low levels of available L-arginine within the TME leading to attenuated T cell responsiveness.

Validation: Each lot of conjugated arginase-1 antibody is quality control tested by MIBIscope™ analysis of stained tissue microarray using the appropriate positive and negative tissue field of views and are pathologist verified.

Recommended Usage: 1 uL of Arginase-1 antibody per 100 uL staining volume using the MIBI™ Staining Protocol.
For optimal results, antibody should be titrated for each desired application.  Suggested starting range is 1:100.

MIBI technology: Learn more about MIBI Technology, a multiplex IHC technology with unmatched sensitivity and true subcellular resolution.

References

  • Rodríguez, P.C., Ochoa A.C. Arginine regulation by myeloid derived suppressor cells and tolerance in cancer:  mechanisms and therapeutic perspectives. Immunol Rev. 2008; 222:180-91.
  • McGaha T.L. et al. Amino acid catabolism: a pivotal regulator of innate and adaptive immunity. Immunol Rev. 2012;  249(1):135-57.

* Conjugate tested on human tissue.

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