Anti-Mouse Ly6G Antibody – Purified in vivo GOLD™ Functional Grade

Mouse Ly-6G transfected EL-4J cell line

This monoclonal antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 - 7.4 with no carrier protein, potassium, calcium or preservatives added. Due to inherent biochemical properties of antibodies, certain products may be prone to precipitation over time. Precipitation may be removed by aseptic centrifugation and/or filtration.

Functional grade preclinical antibodies are manufactured in an animal free facility using in vitro cell culture techniques and are purified by a multi-step process including the use of protein A or G to assure extremely low levels of endotoxins, leachable protein A or aggregates.

Functional grade preclinical antibodies may be stored sterile as received at 2-8°C for up to one month. For longer term storage, aseptically aliquot in working volumes without diluting and store at -80°C. Avoid Repeated Freeze Thaw Cycles.

Next Day 2-8°C

Ly6G antibody (clone 1A8) recognizes an epitope on mouse Ly6G. Clone 1A8 does not cross react with Ly6C.

Ly6G is expressed by neutrophils.

Ly6G antibody (clone 1A8) recognizes lymphocyte antigen 6 complex locus G6D (Ly6G; also called Gr-1), a 21-25 kDa glycosylphosphatidylinositol (GPI)-anchored protein¹. Ly6G belongs to the lymphocyte antigen-6 (Ly6)/urokinase-type plasminogen activator receptor (uPAR) superfamily, characterized by a Ly6/uPAR (LU) domain-containing a three-fingered structural motif stabilized by disulfide bonds². Ly6G is expressed by murine neutrophils regardless of location and activation^1,4,5. Eosinophils may also express low levels of Ly6G⁵. There is no human ortholog for Ly6G; however, a structurally related L76/uPAR protein, CD177 (also known as HNA-2a, NB1, or PRV-1) is expressed in human neutrophils and is implicated in neutropenia⁶. Although the exact function and ligand of Ly6G remain unknown, Ly6G ligation may impair neutrophil migration to sites of inflammation via a β2-integrin-dependent mechanism⁷.

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2. Tsetlin VI. et al. (2015) Trends Pharmacol Sci. 36(2):109-23
3. Daley JM, et al. (2008) J Leukoc Biol. 83(1):64-70
4. Lee PY, et al. (2013) J Leukoc Biol. 94(4):585-594
5. Percopo CM, et al. (2017) J Leukoc Biol. 101(1):321-328.
6. Stroncek DF. et al. (2007) Curr Opin Hematol. 14(6):688-93
7. Wang JX, et al. (2012) Blood. 120(7):1489-1498
8. Gubin, M. et al. (2018) Cell. 175(4):1014–1030.e19 Journal Link
9. Lebratti, T.et al. (2021) eLife 10: e65762 Journal Link
10. 1. Tzetzo, S. L., Kramer, E. D., Mohammadpour, H., Kim, M., Rosario, S. R., Yu, H., Dolan, M., Oturkar, C. C., Morreale, B., Bogner, P. N., Stablewski, A., Benavides, F., Brackett, C. M., Ebos, J. M., Das, G. M., Opyrchal, M., Nemeth, M. J., Evans, S. S., & Abrams, S. I. (2024). Downregulation of IRF8 in alveolar macrophages by G-CSF promotes metastatic tumor progression. iScience, 109187. https://doi.org/10.1016/j.isci.2024.109187