CLEC4D Protein, Rat (HEK293, Fc)

CLEC4D, a calcium-dependent lectin, detects DAMPs and PAMPs from bacteria and fungi. It interacts with FCER1G in myeloid cells, forming a functional complex that activates signaling pathways and promotes antigen-presenting cell maturation and T-cell priming. CLEC4D also combats fungal infections and contributes to antigen uptake for clearance or presentation to T-cells. Its interaction with CLEC4E strengthens the interaction with FCER1G. CLEC4D Protein, Rat (HEK293, Fc) is the recombinant rat-derived CLEC4D protein, expressed by HEK293 , with N-hFc labeled tag. The total length of CLEC4D Protein, Rat (HEK293, Fc) is 171 a.a., with molecular weight of ~53 kDa.

CLEC4D, a calcium-dependent lectin, serves as a pivotal pattern recognition receptor (PRR) within the innate immune system, identifying damage-associated molecular patterns (DAMPs) and pathogen-associated molecular patterns (PAMPs) from bacteria and fungi. Notably, it recognizes alpha-mannans on C.albicans hyphae and mycobacterial trehalose 6,6'-dimycolate (TDM). In myeloid cells, CLEC4D interacts with the signaling adapter Fc receptor gamma chain/FCER1G, likely facilitated by CLEC4E, forming a functional complex. Binding of mycobacterial TDM or C.albicans alpha-mannans to this receptor complex triggers phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G, activating SYK, CARD9, and NF-kappa-B. This activation cascade drives maturation of antigen-presenting cells, shaping antigen-specific priming of T-cells towards effector T-helper 1 and T-helper 17 cell subtypes. Additionally, the CLEC4D-CLEC6A heterodimer actively combats fungal infections, while CLEC4D, functioning as an endocytic receptor, may contribute to antigen uptake at infection sites for either antigen clearance or processing and subsequent presentation to T-cells. The disulfide-linked heterodimer with CLEC4E reinforces interaction with FCER1G, forming a functional complex.

Rat

HEK293

N-hFc

Q69FH1 (W48-K218)

362432  [NCBI]

Approximately 53 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.