JAML/AMICA Protein, Mouse (HEK293, His)

JAML/AMICA protein is a transmembrane protein on leukocytes that regulates migration and activation by interacting with CXADR on adjacent epithelial/endothelial cells. It is essential for the activation of γ-δ T cells in the epithelium, signaling through PI3 kinase and MAP kinase to promote T cell proliferation, cytokine/growth factor production, and tissue repair. JAML/AMICA Protein, Mouse (HEK293, His) is the recombinant mouse-derived JAML/AMICA protein, expressed by HEK293 , with C-His labeled tag.

Junctional adhesion molecule-like (JAML), also known as AMICA, is a transmembrane protein located on the plasma membrane of leukocytes, governing their migration and activation by interacting with CXADR, a receptor present on adjacent epithelial and endothelial cells. This interaction plays a crucial role in activating gamma-delta T-cells, a T-cell subpopulation residing in epithelia, contributing to tissue homeostasis and repair. Upon binding to epithelial CXADR, JAML initiates downstream signaling in gamma-delta T-cells through PI3-kinase and MAP kinases, leading to T-cell proliferation and the production of cytokines and growth factors that stimulate tissue repair. JAML also regulates the transmigration of leukocytes within epithelial and endothelial tissues by engaging in adhesive interactions with epithelial and endothelial CXADR. In its homodimeric form, JAML is particularly active in mediating leukocyte-endothelial cell adhesion. Additionally, JAML interacts with integrin alpha-4/beta-1 (ITGA4 and ITGB1), suggesting a role in the regulation of leukocyte-endothelial cell adhesion by controlling JAML homodimerization.

Mouse

HEK293

C-His

Q80UL9 (Q21-L281)

270152  [NCBI]

Extracellular Domain

QGLPGLTVSSPQLRVHVGESVLMGCVVQRTEEKHVDRVDWLFSKDKDDASEYVLFYYSNLSVPTGRFQNRSHLVGDTFHNDGSLLLQDVQKADEGIYTCEIRLKNESMVMKKPVELWVLPEEPKDLRVRVGDTTQMRCSIQSTEEKRVTKVNWMFSSGSHTEEETVLSYDSNMRSGKFQSLGRFRNRVDLTGDISRNDGSIKLQTVKESDQGIYTCSIYVGKLESRKTIVLHVVQDEFQRTISPTPPTDKGQQGILNGNQL

Approximately 47.7 kDa,based on SDS-PAGE under reducing conditions.

≥ 95%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.