Recombinant Human Dectin-1 protein (GST tag N-Terminus)
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Recombinant Human Dectin-1 protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 77 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
CD369, BGR, CLECSF12, DECTIN1, UNQ539/PRO1082, CLEC7A, C-type lectin domain family 7 member A, Beta-glucan receptor, C-type lectin superfamily member 12, Dendritic cell-associated C-type lectin 1, DC-associated C-type lectin 1, Dectin-1
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Dectin-1 protein (GST tag N-Terminus) (AB163849)
ab163849 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Specifications
Form
Liquid
General info
Function
Lectin that functions as a pattern recognizing receptor (PRR) specific for beta-1,3-linked and beta-1,6-linked glucans, which constitute cell wall constituents from pathogenic bacteria and fungi (PubMed : 11567029, PubMed : 12423684). Necessary for the TLR2-mediated inflammatory response and activation of NF-kappa-B : upon beta-glucan binding, recruits SYK via its ITAM motif and promotes a signaling cascade that activates some CARD domain-BCL10-MALT1 (CBM) signalosomes, leading to the activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines (By similarity). Enhances cytokine production in macrophages and dendritic cells (By similarity). Mediates production of reactive oxygen species in the cell (By similarity). Mediates phagocytosis of C.albicans conidia (PubMed : 17230442). Binds T-cells in a way that does not involve their surface glycans and plays a role in T-cell activation. Stimulates T-cell proliferation. Induces phosphorylation of SCIMP after binding beta-glucans (By similarity).
Post-translational modifications
Phosphorylated on tyrosine residues in response to beta-glucan binding.
Target data
Product promise
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