Recombinant Mouse JAML protein (His tag) is a Mouse Fragment protein, in the 1 to 281 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
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Transmembrane protein of the plasma membrane of leukocytes that control their migration and activation through interaction with CXADR, a plasma membrane receptor found on adjacent epithelial and endothelial cells. The interaction between both receptors mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML induces downstream cell signaling events in gamma-delta T-cells through PI3-kinase and MAP kinases. It results in proliferation and production of cytokines and growth factors by T-cells that in turn stimulate epithelial tissues repair. It also controls the transmigration of leukocytes within epithelial and endothelial tissues through adhesive interactions with epithelial and endothelial CXADR.
Amica1, Gm638, Jaml, Junctional adhesion molecule-like, Dendritic cell-specific protein CREA7, mCrea7
Recombinant Mouse JAML protein (His tag) is a Mouse Fragment protein, in the 1 to 281 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
pH: 7.4
Constituents: 100% PBS
Transmembrane protein of the plasma membrane of leukocytes that control their migration and activation through interaction with CXADR, a plasma membrane receptor found on adjacent epithelial and endothelial cells. The interaction between both receptors mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML induces downstream cell signaling events in gamma-delta T-cells through PI3-kinase and MAP kinases. It results in proliferation and production of cytokines and growth factors by T-cells that in turn stimulate epithelial tissues repair. It also controls the transmigration of leukocytes within epithelial and endothelial tissues through adhesive interactions with epithelial and endothelial CXADR.
Belongs to the immunoglobulin superfamily.
The protein JAML also referred to as Junctional Adhesion Molecule-Like is an important transmembrane protein with a molecular mass of approximately 36 kDa. It belongs to the immunoglobulin superfamily and functions in the immune response. JAML is widely expressed in epithelial cells and various immune cells particularly in neutrophils and some subsets of T cells. On a cellular level JAML is involved in cell-cell adhesion processes functioning at interfaces where immune cells interact with epithelial layers.
Beyond serving as a simple structural component JAML establishes interactions critical for immune surveillance and cell movement. It pairs with other immune receptors to promote the transmigration of leukocytes across endothelial and epithelial barriers. This interaction is notably important since JAML mediates adhesion through its engagement with the Coxsackievirus and Adenovirus Receptor (CAR) forming dynamic complexes that facilitate immune cell trafficking.
Many cellular processes engage JAML in key signaling pathways responsible for immune responses. The protein takes part in the integrin signaling pathway affecting cellular adhesion and migration. Additionally JAML interacts with LFA-1 (Lymphocyte Function-associated Antigen 1) an integrin involved in leukocyte function modulating pathways that govern immune cell behavior and inflammation responses.
The functional role of JAML becomes particularly significant in contexts of inflammatory conditions and cancer. Inflammatory diseases such as inflammatory bowel disease (IBD) show considerable involvement of JAML as its regulatory influence on leukocyte transmigration exacerbates inflammation. Similarly changes in JAML expression have implications in cancer metastasis mechanisms as they relate to immune evasion in tumors. In these conditions JAML interacts closely with proteins like CAR and LFA-1 linking its expression and activity directly to disease progression and immune response modulation.
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SDS-PAGE analysis of ab276987
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