Human C-Type Lectin Domain Family 4 Member D (CLEC4D) Protein
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Description
Human CLEC4D Protein is a recombinant protein from Human produced in HEK293 Cells. A DNA sequence encoding the human CLEC4D (NP_525126.2) extracellular domain (Gly 52-Asn 215) was expressed, with a polyhistidine tag at the N-terminus.
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Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | CLEC4D |
| Host | HEK293 cells |
| Origin | Human |
| Observed MW | Molecular Weight: 21.2 kDa Sequence Fragment: Gly52-Asn215 Tag: N-terminal His tag Validity: The validity for this protein is 12 months. |
| Expression | Recombinant |
| Purity | > 92% (SDS-PAGE) |
| Size 1 | 100 µg |
| Form | |
| Tested Applications | SDS-PAGE |
| Buffer | Lyophilized from sterile PBS, pH 7.4. |
| Availability | Shipped within 5-15 working days. |
| Storage | Aliquot and store at -20°C or -80°C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| NCBI Accession | NP_525126.2 |
| Alias | C-type lectin superfamily member 8,MCL,MPCL,CD368,CLEC6,CLEC-6,CLECSF8,Dectin-3,C-type lectin-like receptor 6,Dendritic cell-associated C-type lectin 3 |
| Background | Protein CLEC4D |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
CLEC4D, known as C-type lectin domain family 4 member D, also referred to as macrophage-inducible C-type lectin (Mincle), is a receptor primarily expressed on immune cells, particularly macrophages and neutrophils. CLEC4D is part of the C-type lectin receptor (CLR) family, which is involved in recognizing pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). These receptors play critical roles in the innate immune response by recognizing carbohydrate structures on pathogens or damaged cells, thus initiating immune responses to eliminate infections or maintain immune homeostasis. CLEC4D functions primarily as an activating receptor and is involved in inflammation and immune activation, particularly in response to microbial infections and tissue damage. Its role in recognizing non-self and modified-self molecules underscores its importance in immunity. CLEC4D’s interaction with mycobacterial glycolipids, fungal pathogens, and endogenous ligands positions it as an essential component of innate immune defenses, especially in fungal and bacterial infections. Furthermore, CLEC4D’s involvement in sterile inflammatory responses has expanded its relevance to non-infectious diseases, including tissue injury and autoimmune conditions.
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