Human JAML/AMICA1 (His Tag) recombinant protein

Human JAML/AMICA1 (His Tag) recombinant protein

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Junctional adhesion molecules (JAMs) are endothelial and epithelial adhesion molecules involved in the recruitment of circulating leukocytes to inflammatory sites. JAML (Junctional adhesion molecule-like), also known as AMICA1 (Adhesion molecule interacting with CXADR antigen 1), a protein related to the JAM family, is restricted to leukocytes and promotes their adhesion to endothelial cells. It contains 2 extracellular immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic tail involved in activation signaling. Monocytic JAML/AMICA1 plays a critical role in regulating monocyte transendothelial migration (TEM) probably via binding to the endothelial coxsackie and adenovirus receptor (CAR) and other tight junction-associated adhesive molecules. The Expression of JAML/AMICA1 is restricted to the hematopoietic tissues with the exception of liver. JAML may function in transmigration of leukocytes through epithelial and endothelial tissues. Expressed at the plasma membrane of polymorphonuclear leukocytes, JAML/AMICA1 also enhances myeloid leukemia cell adhesion to endothelial cells.

cDNA FLJ39966 fis, clone SPLEN2027395, highly similar to Junctional adhesion molecule-like

ADHESION MOLECULE; ADHESION MOLECULE AMICA; MCREA7; DENDRITIC-CELL SPECIFIC PROTEIN CREA7-4; FLJ37080; JUNCTIONAL ADHESION MOLECULE; DENDRITIC CELL-SPECIFIC PROTEIN CREA7; CREA7-4; ADHESION MOLECULE INTERACTING WITH CXADR ANTIGEN 1; JAML; AMICA; DENDRITIC CELL-SPECIFIC PROTEIN CREA7-1; ADHESION MOLECULE THAT INTERACTS WITH CXADR ANTIGEN 1; CREA7; MGC118814; CREA7-1; UNQ722/PRO1387; MGC118815; GM638; INTERACTS WITH CXADR ANTIGEN 1; AMICA1; JUNCTIONAL ADHESION MOLECULE-LIKE

Q86YT9

Human Cells

A DNA sequence encoding the human JAML (NP_001091996.1) extracellular domain (Met 1-Leu 275) was fused with a polyhistidine tag at the C-terminus.

Human

The secreted recombinant human JAML consists of 267 amino acids with the predicted molecular mass of 30.5 kDa. As a result of glycosylation, rhJAML migrates as an approximately 43 kDa band in SDS-PAGE under reducing conditions.

> 90 % as determined by SDS-PAGE