Arginase-1 (E4U1I) Mouse mAb #43933
- 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
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| IHC Leica Bond | 1:50 - 1:200 |
| Immunohistochemistry (Paraffin) | 1:50 |
Storage
For a carrier free (BSA and azide free) version of this product see product #41332.
Protocol
Specificity / Sensitivity
Arginase-1 (E4U1I) Mouse mAb 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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