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.

Contact Us

<p style="text-align: center; margin-top: 2em;">Let us know how we can help you.</p>


    Immuno-oncology/CancerNeuroscienceInfectious DiseaseImmunologyStem CellOther

    255

    Please contact me. I understand that I can choose to unsubscribe at any time by e-mailing marketing@ionpath.com.

    X
    Contact Us

    We are using cookies on our website

    Please confirm, if you accept our tracking cookies. You can also decline the tracking and continue to visit our website without any data sent to third-party services.