Anti-CLM-9 (CD300c), clone ZAQ5

Anti-CLM-9 (CD300c), clone ZAQ5, Cat. No. MABT1511, is a rat monoclonal antibody that detects murine CMRF35-like molecule 9 (CLM-9) and has been tested for use in ELISA, Electron Microscopy, and Immunohistochemistry (Paraffin).

ELISA Electron Microscopy Immunohistochemistry (Paraffin)

Immunohistochemistry (Paraffin) Analysis: A 1:50 dilution from a representative lot detected CLM-9 (CD300c) in mouse spleen tissue sections.

ELISA Analysis: A representative lot detected CLM-9 (CD300c) in ELISA applications (Umemoto, E., et. al. (2006). J Exp Med. 203(6):1603-14).

Immunohistochemistry (Paraffin) Analysis: A representative lot detected CLM-9 (CD300c) in Immunohistochemistry applications (Umemoto, E., et. al. (2013). PLoS One. 8(12):e83681).

Electron Microscopy Analysis: A representative lot of this antibody displayed immunoreactivity in luminal microvillous processes near the intracellular junctions by immunoelectron microscopic analysis.(Umemoto, E., et. al. (2006). J Exp Med. 203(6):1603-14).

Clone ZAQ5 is a rat monoclonal antibody that detects murine CMRF35-like molecule 9 (CLM-9).

Extracellular domain of mouse CMRF35-like molecule 9 (CLM-9; Nepmucin) protein fused with the Fc portion of human IgG

Stable for 1 year at 2-8°C from date of receipt.

Purified rat monoclonal antibody IgG2a in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

CMRF35-like molecule 9 (UniProt: Q1ERP8; also known as CLM-9, CD300 antigen-like family member G, Nepmucin, CD300g) is encoded by the Cd300lg (also known as Clm9, D11Ertd736e) gene (Gene ID: 52685) in murine species. CLM-9 is a single-pass type I membrane protein that serves as a receptor to mediate L-selectin-dependent lymphocyte rollings. It is expressed in monocyte cell lines and in certain types of endothelial and myeloid lineage cells. Higher expression of CLM-9 is observed in endothelial venules and in peripheral and mesenteric lymph nodes. Under physiological conditions, it is constitutively and selectively expressed at the luminal surface of the small arterioles, venules, and capillaries of most tissues. However, in microvessels of the splenic red pulp and thymic medulla it is only weakly expressed. Its expression is shown to diminish in lymph nodes under inflammatory signals believed to be mediated partly by TNF-alpha. In tumors and tumor-draining lymph nodes its levels are reported to be down-regulated. CLM-9 is synthesized with a signal peptide (aa 1-18), which is subsequently cleaved off to generate the mature form that contains an extracellular domain (aa 19-204), a transmembrane domain (aa 205-225), and a cytoplasmic domain (aa 226-331). Its Ig-like domain (aa 19-120) is shown to mediate its binding to lymphocytes. Five isoforms of CCLM-9 have been described that are produced by alternative splicing. Isoform 5 is preferentially expressed in the heart tissue and isoform 1 in kidney and liver. (Ref.: Umemoto, E., et al. (2013) PLoS One 8(12); e83681; Umemoto, E., et al. (2006). J. Exp. Med. 203(6); 1603-1614).

Evaluated by Immunohistochemistry (Paraffin) in mouse kidney tissue sections.

Immunohistochemistry (Paraffin) Analysis: A 1:50 dilution of this antibody detected CLM-9 (CD300c) in mouse kidney tissue sections.

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