Arginase-1 (E4U1I) Mouse mAb (BSA and Azide Free) #41332
- WB
- IHC
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 40 |
| Source/Isotype | Mouse IgG2a |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
Formulation
Storage
Specificity / Sensitivity
Arginase-1 (E4U1I) Mouse mAb (BSA and Azide Free) recognizes endogenous levels of total arginase-1 protein. This antibody does not cross-react with arginase-2 protein.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val47 of human arginase-1 protein.
Background
L-arginine plays a critical role in regulating the immune system (1-3). In inflammation, cancer, and certain other pathological conditions, myeloid cell differentiation is inhibited leading to a heterogeneous population of immature myeloid cells, known as myeloid-derived suppressor cells (MDSCs). MDSCs are recruited to sites of cancer-associated inflammation and express high levels of arginase-1 (4). Arginase-1 catalyzes the final step of the urea cycle converting L-arginine to L-ornithine and urea (5). Thus, MDSCs increase the catabolism of L-arginine resulting in L-arginine depletion in the inflammatory microenvironment of cancer (4,6). The reduced availability of L-arginine suppresses T cell proliferation and function and thus contributes to tumor progression (4,6). Arginase-1 is of great interest to researchers looking for a therapeutic target to inhibit the function of MDSCs in the context of cancer immunotherapy (7). In addition, research studies have demonstrated that arginase-1 distinguishes primary hepatocellular carcinoma (HCC) from metastatic tumors in the liver, indicating its value as a potential biomarker in the diagnosis of HCC (8,9).
- Albina, J.E. et al. (1989) J Exp Med 169, 1021-9.
- Mills, C.D. (2001) Crit Rev Immunol 21, 399-425.
- Rodriguez, P.C. et al. (2004) Cancer Res 64, 5839-49.
- Gabrilovich, D.I. and Nagaraj, S. (2009) Nat Rev Immunol 9, 162-74.
- Wu, G. and Morris, S.M. (1998) Biochem J 336 (Pt 1), 1-17.
- Raber, P. et al. (2012) Immunol Invest 41, 614-34.
- Wesolowski, R. et al. (2013) J Immunother Cancer 1, 10.
- Sang, W. et al. (2015) Tumour Biol 36, 3881-6.
- Geramizadeh, B. and Seirfar, N. (2015) Hepat Mon 15, e30336.
Limited Uses
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