KLRF1 Human
HEK293 Cells.
NKp80, KLRF1, C-type lectin domain family 5 member C, CLEC5C, ML, Killer cell lectin-like receptor F1, Killer cell lectin-like receptor subfamily F member 1,Killer cell lectin-like receptor subfamily F member 1 isoform 1, Lectin-like receptor F1, Activating coreceptor NKp80, CLEC5CMGC119908, MGC119907, MGC119909.
Sterile filtered colorless solution.
Greater than 85.0% as determined by SDS-PAGE.
Description
KLRF1 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 414 amino acids (60-231a.a) and having a molecular mass of 47.1kDa.
KLRF1 is fused to a 242 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.
Product Specs
KLRF1, also known as Killer cell lectin-like receptor subfamily F member 1, belongs to the C-type lectin family. This activating homodimeric receptor is predominantly found on natural killer (NK) cells and plays a crucial role in enhancing their cytotoxic activity and cytokine production. KLRF1 interacts with its ligand, AICL (activation-induced C-type lectin), which is selectively expressed on myeloid cells. This interaction triggers the release of proinflammatory cytokines, thereby regulating immune responses at inflammatory sites. KLRF1 has been associated with certain medical conditions, including Developmental And Epileptic Encephalopathy 76.
Recombinant Human KLRF1, expressed in HEK293 cells, is a single, glycosylated polypeptide chain. It comprises 414 amino acids (60-231a.a) with a molecular weight of 47.1kDa. The protein includes a C-terminal fusion of a 242 amino acid hIgG-His-Tag and is purified using proprietary chromatographic techniques.
Sterile filtered, colorless solution.
The KLRF1 solution is provided at a concentration of 0.25mg/ml in phosphate buffered saline (pH 7.4) containing 10% glycerol.
For short-term storage (up to 2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Repeated freezing and thawing should be avoided.
Purity is determined to be greater than 85.0% by SDS-PAGE analysis.
Biological activity is assessed by measuring the ability of the immobilized protein to promote adhesion of U937 human histiocytic lymphoma cells. The assay involves adding cells to plates coated with human KLRF1 at a concentration of 2 ug/ml, which results in a significant adhesion effect exceeding 60%.
NKp80, KLRF1, C-type lectin domain family 5 member C, CLEC5C, ML, Killer cell lectin-like receptor F1, Killer cell lectin-like receptor subfamily F member 1,Killer cell lectin-like receptor subfamily F member 1 isoform 1, Lectin-like receptor F1, Activating coreceptor NKp80, CLEC5CMGC119908, MGC119907, MGC119909.
HEK293 Cells.
DGSLLVSQGV LLKCQKGSCS NATQYEDTGD LKVNNGTRRN ISNKDLCASR SADQTVLCQS EWLKYQGKCY WFSNEMKSWS DSYVYCLERK SHLLIIHDQL EMAFIQKNLR QLNYVWIGLN FTSLKMTWTW VDGSPIDSKI FFIKGPAKEN SCAAIKESKI FSETCSSVFK WICQYLEPKS CDRTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH HHHH
Product Science Overview
KLRF1 is an 80 kDa homodimeric protein characterized by an extracellular C-type lectin domain, a transmembrane domain, and a cytoplasmic domain. The extracellular domain is responsible for ligand binding, while the transmembrane domain anchors the protein to the cell membrane. The cytoplasmic domain contains signaling motifs that are essential for transmitting activation signals .
KLRF1 is involved in the activation of NK cells, which are critical components of the innate immune system. Upon binding to its ligand, CLEC2B, which is expressed on the surface of myeloid cells, KLRF1 stimulates NK cell cytotoxicity and cytokine production. This interaction leads to the destruction of malignant cells expressing CLEC2B . KLRF1 also plays a role in the immune response to infections and tumors by enhancing the cytolytic activity of NK cells .
The activation of KLRF1 involves the binding of its extracellular domain to ligands on target cells. This binding triggers a signaling cascade that results in the phosphorylation of downstream proteins, such as AKT and AMP-responsive protein kinase (AMPK). These signaling events lead to the activation and proliferation of NK cells, enhancing their ability to target and destroy infected or malignant cells .
KLRF1 has been studied for its potential therapeutic applications in cancer immunotherapy. By targeting KLRF1 and its ligands, researchers aim to enhance the cytotoxic activity of NK cells against tumors. Additionally, KLRF1 is being investigated as a biomarker for certain diseases, including autoimmune disorders and infectious diseases .
Recombinant KLRF1 is produced using genetic engineering techniques to express the protein in a host system, such as bacteria or mammalian cells. This recombinant protein is used in research to study the function and signaling pathways of KLRF1, as well as in the development of therapeutic agents targeting NK cell activation .
