|Calculated MW||This protein is fused with a C-terminal 6×His tag, has a calculated MW of 24.9 kDa expressed. The predicted N-terminus is Leu 20. Protein migrates as 35 kDa in reduced SDS-PAGE due to glycosylation.|
|Other Names||CXADR, CAR, CAR4/6, HCAR|
|Results||Measured by the ability of the immobilized protein to support the adhesion of mouse neutrophils. When 50000 cells/well are added to CXADR coated plates (4 µg/mL and 100 µL/well), approximately 20% - 50% will adhere specifically after 60 minutes at 37℃.|
|Application Notes||Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 µg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.|
|Storage||-20°C; Lyophilized from 0.22 µm filtered solution in PBS, pH 7.4. Normally Mannitol or Trehalose is added as protectants before lyophilization.|
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Provided below are standard protocols that you may find useful for product applications.
Coxsackie virus and adenovirus receptor (CXADR) also known as CAR, is a type I transmembrane glycoprotein for group B coxsackie viruses and subgroup C adenoviruses, and belongs to the CTX family of the Ig superfamily. CAR is strongly expressed in the developing central nervous system. It functions as a homophilic and also as a heterophilic cell adhesion molecule through its interactions with extracellular matrix glycoproteins such as: fibronectin, agrin, laminin-1 and tenascin-R. Human CXADR protein contains a signal sequence, a extracellular domain (ECD) with a V type (D1) and a C2 type (D2) Iglike domain, a transmembrane segment and a intracellular domain. D1 is thought to be responsible for homodimer formation in trans within tight junctions, and is necessary and sufficient for adenovirus binding. Variants of CXADR are attached to the cell membrane by a GPI- anchor.
Tomko R.P.,et al.Proc. Natl. Acad. Sci. U.S.A. 94:3352-3356(1997).
Bergelson J.M.,et al.Science 275:1320-1323(1997).
Bowles K.R.,et al.Hum. Genet. 105:354-359(1999).
He Y.,et al.Nat. Struct. Biol. 8:874-878(2001).
Doerner A.,et al.J. Biol. Chem. 279:18497-18503(2004).
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