SIGLEC5 antibody

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935106861
info@markelab.com
name
SIGLEC5 antibody
category
Primary Antibodies
provider
FineTest
reference
FNab07860
tested applications
ELISA, WB
Description
Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
Documents del producto
Product specifications
Category | Primary Antibodies |
Immunogen Target | sialic acid binding Ig-like lectin 5 (SIGLEC5) |
Host | Rabbit |
Reactivity | Human |
Recommended Dilution | WB: 1:500-1:2000 |
Clonality | polyclonal |
Conjugation | Unconjugated |
Isotype | IgG |
Observed MW | 70 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 | O15389 |
Gene ID | 8778 |
Alias | CD170,OBBP2,CD33L2,OB-BP2,SIGLEC-5,Obesity-binding protein 2,CD33 antigen-like 2 |
Background | Antibody anti-SIGLEC5 |
Status | RUO |
Note | Mol. Weight 70 kDa |
Descripción
SIGLEC5 is an inhibitory receptor expressed on monocytes, neutrophils, and B cells. It binds to sialic acid-containing glycans on host and microbial surfaces, modulating immune responses to avoid excessive inflammation. Through its immunoreceptor tyrosine-based inhibitory motifs (ITIMs), SIGLEC5 dampens activation signals and helps maintain immune tolerance. This protein also plays a role in preventing inappropriate immune responses during pregnancy and infection. Genetic fusion events between SIGLEC5 and SIGLEC14 have been noted, affecting the functional balance between activation and inhibition. SIGLEC5 is studied for its involvement in autoimmune diseases and infections.
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Human SIGLEC5 (Sialic acid-binding Ig-like lectin 5) ELISA Kit
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SIGLEC5 antibody
Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
Ver Producto