CLEC10A antibody

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935106861
info@markelab.com
name
CLEC10A antibody
category
Primary Antibodies
provider
FineTest
reference
FNab01745
tested applications
ELISA, WB
Documents del producto
Product specifications
Category | Primary Antibodies |
Immunogen Target | C-type lectin domain family 10, member A (CLEC10A) |
Host | Rabbit |
Reactivity | Human |
Recommended Dilution | WB: 1:500-1:1000 |
Clonality | polyclonal |
Conjugation | Unconjugated |
Isotype | IgG |
Observed MW | 32 kDa |
Purity | ≥95% as determined by SDS-PAGE |
Purification | Immunogen affinity purified |
Size 1 | 100µg |
Form | liquid |
Tested Applications | ELISA, WB |
Storage | PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months(Avoid repeated freeze / thaw cycles.) |
UniProt ID | Q8IUN9 |
Alias | C-type lectin domain family 10 member A,HML,MGL,HML2,CD301,CLECSF13,CLECSF14,C-type lectin superfamily member 14,Macrophage lectin 2 |
Background | Antibody anti-CLEC10A |
Status | RUO |
Note | Mol. Weight 32 kDa |
CLEC10A (C-type lectin domain containing 10A), also known as CD301 or MGL (Macrophage Galactose-Type Lectin), is a transmembrane protein in the C-type lectin receptor (CLR) family primarily expressed on antigen-presenting cells such as dendritic cells, macrophages, and certain monocytes. CLEC10A is part of the innate immune system, specializing in recognizing carbohydrate structures on the surfaces of cells and pathogens. Specifically, it binds to terminal galactose and N-acetylgalactosamine (GalNAc) residues, making it essential for identifying certain pathogens and interacting with glycoproteins on cellular surfaces. CLEC10A’s specificity for galactose-containing glycans allows it to function in immune surveillance, pathogen clearance, and immunomodulation, making it a focal point in immune-related research. Its expression on dendritic cells and macrophages positions it to play a key role in the innate immune system's interactions with the adaptive immune response, particularly in tissue immune environments. CLEC10A’s involvement in recognizing glycosylated antigens has implications for disease processes, including infections, cancer, and autoimmune conditions.
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