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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human KLRG1/CLEC15A Protein, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 15.34 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
Form | Liquid |
Delivery condition | Dry Ice |
Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
Storage condition | 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection) |
Brand | Arovia |
Host species | Escherichia coli (E.coli) |
Fragment Type | Ser74-Lys186 |
Aliases /Synonyms | Killer cell lectin-like receptor subfamily G member 1, C-type lectin domain family 15 member A, ITIM-containing receptor MAFA-L, MAFA-like receptor, Mast cell function-associated antigen, KLRG1, CLEC15A, MAFA, MAFAL |
Reference | ARO-P10842 |
Note | For research use only. |
Recombinant Human KLRG1/CLEC15A Protein is a type I transmembrane glycoprotein that belongs to the C-type lectin family. It is also known as killer cell lectin-like receptor G1 (KLRG1) or C-type lectin domain family 15 member A (CLEC15A). This protein is encoded by the KLRG1 gene and is primarily expressed on natural killer (NK) cells, T cells, and subsets of B cells and myeloid cells.
The recombinant form of KLRG1/CLEC15A protein is produced through genetic engineering techniques, where the gene encoding for the protein is inserted into a suitable expression system. The resulting protein is a homodimer with a molecular weight of approximately 30 kDa. It contains an extracellular C-type lectin-like domain, a transmembrane domain, and a cytoplasmic tail. The extracellular domain is responsible for binding to its ligand, while the cytoplasmic tail contains signaling motifs that regulate the activity of the protein.
KLRG1/CLEC15A protein is a type II transmembrane receptor that plays a crucial role in the regulation of immune responses. It acts as an inhibitory receptor and is involved in the modulation of NK cell and T cell cytotoxicity. The binding of KLRG1/CLEC15A to its ligand results in the recruitment of phosphatases, which inhibit the signaling pathways involved in cell activation. This ultimately leads to the suppression of immune responses, which is important for maintaining immune homeostasis and preventing autoimmunity.
The ligand for KLRG1/CLEC15A protein is not yet fully identified, but it is believed to be a carbohydrate or glycoprotein present on the surface of target cells. Studies have shown that KLRG1/CLEC15A can interact with several ligands, including E-cadherin, Galectin-3, and MHC class I molecules. The binding of KLRG1/CLEC15A to its ligand results in the inhibition of NK cell and T cell cytotoxicity, as well as the downregulation of cytokine production.
Recombinant Human KLRG1/CLEC15A Protein has various applications in scientific research and potential therapeutic uses. Some of the key applications include:
Due to its role in regulating immune responses, recombinant KLRG1/CLEC15A protein is widely used in studies related to the immune system. It is used to investigate the mechanisms of immune tolerance and the role of inhibitory receptors in immune regulation. It is also used to study the interactions between immune cells and their targets, as well as the signaling pathways involved in these interactions.
The inhibitory activity of KLRG1/CLEC15A protein makes it a potential target for cancer immunotherapy. It has been shown to play a role in the suppression of anti-tumor immune responses, and targeting this protein may enhance the efficacy of cancer immunotherapies. Recombinant KLRG1/CLEC15A protein can be used in preclinical studies to evaluate its potential as a therapeutic target for cancer treatment.
KLRG1/CLEC15A protein has been implicated in the development of autoimmune diseases, such as multiple sclerosis and rheumatoid arthritis. Recombinant KLRG1/CLEC15A protein can be used
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