CXADR Fc Chimera Protein, Mouse,specification,price,image-Bio-Equip in China

Product Detail
Company Profile

Product Specification

Species	Mouse
Synonyms	CAR10Coxsackievirus B-adenovirus receptor; CAR4/6; coxsackie virus and adenovirus receptor; coxsackie virus B receptor; coxsackievirus and adenovirus receptor; CVB3 binding protein; CVB3 BP; CVB3-binding protein; CXADR; HCAR; HCVADR
Accession	P97792
Amino Acid Sequence	Leu20-Gly237 with Human IgG1 Fc at C-Terminus
Expression System	HEK293
Molecular Weight	55-70kDa (Reducing)
Purity	＞95% by SDS-PAGE & SEC-HPLC
Endotoxin	<0.1EU/μg
Conjugation	Unconjugated
Tag	Human IgG1 Fc
Physical Appearance	Lyophilized Powder
Storage Buffer	PBS, PH7.4, 5% trehalose
Reconstitution	Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation.
Stability & Storage	· 12 months from date of receipt, lyophilized powder stored at -20 to -80℃. · 3 months, -20 to -80℃ under sterile conditions after reconstitution. · 1 week, 2 to 8℃ under sterile conditions after reconstitution. · Please avoid repeated freeze-thaw cycles.
Reference	1.Philipson, L. et al., 2004, Curr. Top. Microbiol. Immunol. 273:87-111. 2.Raschperger, E. et al., 2006, Exp. Cell Res. 312: 1566-1580.

Background

CXADR (coxsackie virus and adenovirus receptor), also known as CAR, is a type I transmembrane glycoprotein belonging to the CTX family within the immunoglobulin (Ig) superfamily. It plays a crucial role in normal cardiac development in mice. CXADR is proposed to function as a homophilic cell adhesion molecule and is a component of the epithelial apical junction complex, which is essential for maintaining tight junction integrity. It is also likely involved in the transepithelial migration of polymorphonuclear leukocytes (PMNs).
The mature mouse CXADR structure comprises a 218 amino acid (aa) extracellular domain (ECD), which includes a V-type (D1) and a C2-type (D2) Ig-like domain, a 21 aa transmembrane segment, and a 17 aa intracellular domain. Notably, D1 is believed to be responsible for homodimer formation within tight junctions. The ECD of mouse CXADR shares 97% sequence identity with the corresponding regions of human CXADR and 9% sequence identity with those of rat CXADR.