CLEC4M Antibody - #DF15512
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Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
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C type lectin domain family 4, member M; C-type lectin domain family 4 member M; CD209 antigen like; CD209 antigen like protein 1; CD209 antigen-like protein 1; CD209L; CD209L1; CD299; CD299 antigen; CLC4M_HUMAN; CLEC4M; DC SIGN related protein; DC SIGN2; DC SIGNR; DC-SIGN-related protein; DC-SIGN2; DC-SIGNR; DCSIGN related protein; DCSIGNR; Dendritic cell-specific ICAM-3-grabbing non-integrin 2; HP10347; L SIGN; L-SIGN; Liver/lymph node specific ICAM3 grabbing nonintegrin; Liver/lymph node-specific ICAM-3-grabbing non-integrin; LSIGN; Mannose binding C type lectin DC SIGNR; MGC129964; MGC47866;
Immunogens
A synthesized peptide derived from human CLEC4M.
Predominantly highly expressed in liver sinusoidal endothelial cells and in lymph node. Found in placental endothelium but not in macrophages. Expressed in type II alveolar cells and lung endothelial cells.
- Q9H2X3 CLC4M_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MSDSKEPRVQQLGLLEEDPTTSGIRLFPRDFQFQQIHGHKSSTGCLGHGALVLQLLSFMLLAGVLVAILVQVSKVPSSLSQEQSEQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELPEKSKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTELKAAVGELPEKSKLQEIYQELTQLKAAVGELPDQSKQQQIYQELTDLKTAFERLCRHCPKDWTFFQGNCYFMSNSQRNWHDSVTACQEVRAQLVVIKTAEEQNFLQLQTSRSNRFSWMGLSDLNQEGTWQWVDGSPLSPSFQRYWNSGEPNNSGNEDCAEFSGSGWNDNRCDVDNYWICKKPAACFRDE
Research Backgrounds
Probable pathogen-recognition receptor involved in peripheral immune surveillance in liver. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. Is a receptor for ICAM3, probably by binding to mannose-like carbohydrates.
(Microbial infection) Acts as an attachment receptor for Ebolavirus.
(Microbial infection) Acts as an attachment receptor for Hepatitis C virus.
(Microbial infection) Acts as an attachment receptor for HIV-1.
(Microbial infection) Acts as an attachment receptor for Human coronavirus 229E.
(Microbial infection) Acts as an attachment receptor for Human cytomegalovirus/HHV-5.
(Microbial infection) Acts as an attachment receptor for Influenzavirus.
(Microbial infection) Acts as an attachment receptor for SARS coronavirus.
(Microbial infection) Acts as an attachment receptor for West-nile virus.
(Microbial infection) Acts as an attachment receptor for Japanese encephalitis virus.
(Microbial infection) Acts as an attachment receptor for Marburg virus glycoprotein.
(Microbial infection) Recognition of M.bovis by dendritic cells may occur partially via this molecule.
Cell membrane>Single-pass type II membrane protein.
Cell membrane>Single-pass type II membrane protein.
Cell membrane>Single-pass type II membrane protein.
Secreted.
Secreted.
Secreted.
Secreted.
Predominantly highly expressed in liver sinusoidal endothelial cells and in lymph node. Found in placental endothelium but not in macrophages. Expressed in type II alveolar cells and lung endothelial cells.
Homotetramer.
(Microbial infection) Interacts with ebola virus glycoprotein.
(Microbial infection) Interacts with hepatitis C virus E1 and E2 protein.
(Microbial infection) Interacts with HIV-1 gp120.
(Microbial infection) Interacts with human coronavirus 229E spike glycoprotein.
(Microbial infection) Interacts with human cytomegalovirus/HHV-5 gB protein.
(Microbial infection) Interacts with influenzavirus hemagglutinin.
(Microbial infection) Interacts with SARS coronavirus spike glycoprotein.
(Microbial infection) Interacts with west-nile virus envelope protein E.
(Microbial infection) Interacts with Japanese encephalitis virus E protein.
(Microbial infection) Interacts with Marburg virus glycoprotein.
(Microbial infection) Interacts with M.bovis LprG.
The tandem repeat domain, also called neck domain, mediates oligomerization.
Research Fields
· Cellular Processes > Transport and catabolism > Phagosome. (View pathway)
· Human Diseases > Infectious diseases: Bacterial > Tuberculosis.
· Human Diseases > Infectious diseases: Viral > Measles.
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