The coxsackie virus and adenovirus receptor (CXADR, CAR) is a highly conserved, single-transmembrane glycoprotein and the primary receptor to mediate cellular attachment and infection of coxsackie B viruses and most adenoviruses. The CAR protein contains a pair of Ig-like domains within the amino-terminal extracellular domain and a carboxyl-terminal PDZ motif. Research studies indicate that CAR is a tight junction protein that associates with the ZO-1 scaffold protein and promotes both cell adhesion and restriction of solute and ion movement between cells. Endogenous CAR is targeted to the basolateral plasma membrane by a tyrosine-based basolateral sorting signal and clathrin adaptors AP-1A and AP-1B. CAR binds junctional adhesion molecule L (JAML) on epithelial cells and neutrophils where it activates PI3K and downstream MAPK kinases to stimulate epithelial γδ T cell proliferation and increase production of TNFα and keratinocyte growth factor. As a result, the CAR protein plays a potentially critical role in adenoviral gene therapy, immunity, wound repair, inflammation, and cancer therapy. Additional studies demonstrate that CAR is essential in regulating squamous carcinoma cell growth.

Coxsackievirus and adenovirus receptor; CAR; hCAR; CVB3-binding protein; Coxsackievirus B-adenovirus receptor; HCVADR; CXADR; CAR

p78310

Human,Pig

WB

WB 1:1000-1:2000

~ 50 kDa

Rabbit

This antibody detects endogenous levels of CAR protein.

Synthetic peptide, corresponding to Human CAR.

Polyclonal

Rabbit IgG

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

PBS with 0.02% sodium azide, 50% glycerol, pH7.2

1mg/ml

Store at 4℃ short term,and store at -20℃ long term. Avoid freeze-thaw cycles.