Name :
Recombinant Human CXADR/CAR Protein (His & hFc Tag)

Biological Activity :

Background :
CXADR (coxsackie virus and adenovirus receptor), also known as CAR, is a type I transmembrane glycoprotein belonging to the CTX family of the Ig superfamily, and is essential for normal cardiac development in the mouse. Proposed as a homophilic cell adhesion molecule, CXADR is a component of the epithelial apical junction complex that is essential for the tight junction integrity, and probably involved in transepithelial migration of polymorphonuclear leukocytes (PMN). Mature mouse CXADR structrually comprises a 218 aa extracellular domain (ECD) with a V-type (D1) and a C2-type (D2) Ig-like domain, a 21 aa transmembrane segment and a 17 aa intracellular domain, among which,D1 is thought to be responsible for homodimer formation in trans within tight junctions. The ECD of mouse CXADR shares 97%, 9% sequence identity with the corresponding regions of rat, human CXADR.

Biological Activity :
Testing in progress

Expression Host :
Human

Source :
HEK293 Cells

Tag :

Protein Accession No. :
NP_001329.1

NCBI Gene ID :

Synonyms :

Synonyms :
coxsackie virus and adenovirus receptor

Amino Acid Sequence :

Molecular Weight :
The recombinant human CXADR/Fc is a disulfide-linked homodimer. The reduced monomer consists of 466 amino acids and has a predicted molecular mass of 52 kDa. As a result of glycosylation, the apparent molecular mass of rh CXADR/Fc monomer migrates with an apparent molecular mass of 60-65 kDa in SDS-PAGE under reducing conditions.

Purity :
> 92 % as determined by SDS-PAGE

State of Matter :

Product Concentration :

Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Endotoxin Level :
< 1.0 EU per μg of the protein as determined by the LAL method

Protein Construction :
A DNA sequence encoding the human CXADR (NP_001329.1) extracellular domain (Met 1-Gly 237) was fused with the C-terminal polyhistidine-tagged Fc region of human IgG1 at the C-terminus.

Buffer Solution :
Lyophilized from sterile PBS, pH 7.4.Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.

Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.

Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.

Synonyms :
CAR Protein, Human; CAR4/6 Protein, Human; CXADR Protein, Human; HCAR Protein, Human CXADR/CAR 背景信息 CXADR (coxsackie virus and adenovirus receptor), also known as CAR, is a type I transmembrane glycoprotein belonging to the CTX family of the Ig superfamily, and is essential for normal cardiac development in the mouse. Proposed as a homophilic cell adhesion molecule, CXADR is a component of the epithelial apical junction complex that is essential for the tight junction integrity, and probably involved in transepithelial migration of polymorphonuclear leukocytes (PMN). Mature mouse CXADR structrually comprises a 218 aa extracellular domain (ECD) with a V-type (D1) and a C2-type (D2) Ig-like domain, a 21 aa transmembrane segment and a 17 aa intracellular domain, among which,D1 is thought to be responsible for homodimer formation in trans within tight junctions. The ECD of mouse CXADR shares 97%, 9% sequence identity with the corresponding regions of rat, human CXADR.

References & Citations :
Tomko, R.P. et al., 1997, Proc. Natl. Acad. Sci. U.S.A. 94 (7): 3352–3356. van Raaij , M.J. et al., 2001, Structure. 8 (11): 1147–1155. Cohen, C.J. et al., 2001, J. Biol. Chem. 276 (27): 25392–25398. Carson, S.D. et al., 2002, Rev. Med. Virol. 11 (4): 219–226. Selinka, H.C. et al., 2004, Med. Microbiol. Immunol. 193 (2-3): 127–131. Philipson, L. et al., 2004, Curr. Top. Microbiol. Immunol. 273:87-111. Raschperger, E. et al., 2006, Exp. Cell Res. 312: 1566-1580.

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