Recombinant Human CLEC4A protein, N-His-tagged

• Cat.No.: CLEC4A-3353H
• Product Overview: Recombinant Human CLEC4A protein(NP_001128530.1)(Gln 70-Leu 237) was expressed in HEK293, with a polyhistidine tag at the N-terminus.

Specification

• Species: Human
• Source: HEK293
• Tag: His
• Protein Length: 70-237 aa
• Form: Lyophilized from sterile PBS, pH 7.4.
• Molecular Mass: The recombinant human CLEC4A consists of 184 amino acids and has a calculated molecular mass of 22 kDa. In SDS-PAGE under reducing conditions, rhCLEC4A migrates as an approximately 28 kDa band due to glycosylation.
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.
• Purity: > 95 % as determined by SDS-PAGE
• Storage: Store it under sterile conditions at -20°C to -80°C upon receiving. Recommend to aliquot the protein into smaller quantities for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 ug/ul. Centrifuge the vial at 4°C before opening to recover the entire contents.

Gene Information

• Gene Name: CLEC4A C-type lectin domain family 4, member A [ Homo sapiens ]
• Official Symbol: CLEC4A
• Synonyms: CLEC4A; C-type lectin domain family 4, member A; C type (calcium dependent, carbohydrate recognition domain) lectin, superfamily member 6, CLECSF6; C-type lectin domain family 4 member A; DCIR; DDB27; C-type lectin DDB27; lectin-like immunoreceptor; dendritic cell immunoreceptor; C-type lectin superfamily member 6; C-type (calcium dependent, carbohydrate-recognition domain) lectin, superfamily member 6; LLIR; CLECSF6; HDCGC13P
• Gene ID: 50856
• mRNA Refseq: NM_016184
• Protein Refseq: NP_057268
• MIM: 605306
• UniProt ID: Q9UMR7

Case Study

Case 1: Nasu J, et al. Int Immunol. 2020

CLEC4A, a receptor in the immune system, has a unique way of sending "stop" signals to cells but needs to interact with itself to work effectively. It plays a major role in certain immune cells like cDC2 and monocytes. Missing parts of the receptor reduce its ability to stop cell activation. An antibody that blocks this self-interaction can even enhance immune responses. Essentially, CLEC4A's self-interaction is key to its ability to regulate these immune cells.

Fig1. The binding of mIgFc or CLEC4A-mIgFc to DC2.4 expressing mock-GFP, CLEC4A-GFP, CLEC4AN185Q-GFP or CLEC4AΔE195-S197-GFP was analyzed by flow cytometry.

Fig2. The expression of GFP and CLEC4A was analyzed by flow cytometry.

Case 2: Kaifu T, et al. J Exp Med. 2021

DCIR, found on dendritic cells and osteoclasts, helps regulate immunity and bone health. In Dcir-/- mice, autoimmune and bone issues arise due to deficient DCIR function. DCIR binds to an N-glycan on cells, and without it, there's increased osteoclast production. Neuraminidase treatment, which enhances this glycan visibility, can suppress cell activity and alleviate symptoms of autoimmune diseases by affecting how dendritic cells present antigens. Modifying cell glycans is crucial for DCIR's regulation of these diseases.

Fig1. Binding of DCIR-Fc to NA2-BSA in a glycan microarray assay.

Fig2. DCIR-Fc binding to BMCs was analyzed at 48 h after neuraminidase administration.

Application

Recombinant CLEC4A protein is making strides in both research and therapeutic areas because of its role in immune regulation. Researchers use it to gain insights into immune cell functions, which is fundamental in finding treatments for autoimmune diseases, where the immune system wrongly attacks the body. Understanding how CLEC4A works could help create therapies that effectively calm these overreactions. In drug development, recombinant CLEC4A is key for testing how new drugs might affect immune cells. It aids in crafting medications that can adjust immune responses, aiming for greater effectiveness and fewer side effects. This is crucial for conditions where it's important to manage the immune system, like allergies and inflammatory disorders. By harnessing recombinant CLEC4A, scientists are working on therapies that are more accurate and beneficial, driving progress in treating immune-related health issues.

Fig1. Proposed working models for DCIR involvement in HIV-1 infection. (Alexandra A Lambert, 2010)