Recombinant Human Coxsackie Adenovirus Receptor/hCAR protein (ab151334)
Key features and details
- Expression system: HEK 293 cells
- Purity: > 95% SDS-PAGE
- Endotoxin level: < 1.000 Eu/µg
- Tags: His tag C-Terminus
- Suitable for: SDS-PAGE, HPLC
Description
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Product name
Recombinant Human Coxsackie Adenovirus Receptor/hCAR protein
See all Coxsackie Adenovirus Receptor/hCAR proteins and peptides -
Purity
> 95 % SDS-PAGE.
Purtiy is greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE. -
Endotoxin level
< 1.000 Eu/µg -
Expression system
HEK 293 cells -
Accession
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Protein length
Protein fragment -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Sequence
LSITTPEEMIEKAKGETAYLPCKFTLSPEDQGPLDIEWLISPADNQKVDQ VIILYSGDKIYDDYYPDLKGRVHFTSNDLKSGDASINVTNLQLSDIGTYQ CKVKKAPGVANKKIHLVVLVKPSGARCYVDGSEEIGSDFKIKCEPKEGSL PLQYEWQKLSDSQKMPTSWLAEMTSSVISVKNASSEYSGTYSCTVRNRVG SDQCLLRLNVVPPSNKAGVDHHHHHH -
Predicted molecular weight
25 kDa including tags -
Amino acids
20 to 237 -
Tags
His tag C-Terminus
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab151334 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
SDS-PAGE
HPLC
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Form
Lyophilized -
Additional notes
This product was previously labelled as Coxsackie Adenovirus Receptor
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. The lyophilized protein is stable for a few weeks at room temperature. Store at -20°C long term.
pH: 7.20
Constituents: 99% Phosphate Buffer, 0.88% Sodium chloride -
ReconstitutionDissolve the lyophilized protein in 1X PBS. It is not recommended to reconstitute to a concentration less than 100 µg/ml. Reconstituted protein solution can be stored at 4-7°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
General Info
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Alternative names
- 46 kD coxsackievirus and adenovirus receptor CAR protein
- 46 kD coxsackievirus and adenovirus receptor protein
- CAR
see all -
Function
Component of the epithelial apical junction complex that is essential for the tight junction integrity. Proposed to function as a homophilic cell adhesion molecule. Recruits MPDZ to intercellular contact sites. Probably involved in transepithelial migration of polymorphonuclear leukocytes (PMN) through adhesive interactions with AMICA1/JAML located in the plasma membrane of PMN. -
Tissue specificity
Expressed in pancreas, brain, heart, small intestine, testis, prostate and at a lower level in liver and lung. Isoform 5 is ubiquitously expressed. Isoform 3 is expressed in heart, lung and pancreas. In skeletal muscle, isoform 1 is found at the neuromuscular junction and isoform 2 is found in blood vessels. In cardiac muscle, isoform 1 and isoform 2 are found at intercalated disks. In heart expressed in subendothelial layers of the vessel wall but not in the luminal endothelial surface. Expression is elevated in hearts with dilated cardiomyopathy. -
Sequence similarities
Contains 2 Ig-like C2-type (immunoglobulin-like) domains. -
Domain
The Ig-like C2-type 1 domain probably mediates homodimerization and interaction with JAML.
The PDZ-binding motif mediates interaction with MPDZ and BAIAP1. -
Post-translational
modificationsN-glycosylated.
Palmitoylated on Cys-259 and/or Cys-260; required for proper localization to the plasma membrane. -
Cellular localization
Secreted and Cell membrane. Cell junction > tight junction. Cell junction > adherens junction. Basolateral cell membrane. In epithelial cells localizes to the apical junction complex composced of tight and adherens junctions. In airway epithelial cells localized to basolateral membrane but not to apical surface. - Information by UniProt
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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Datasheet download
References (0)
ab151334 has not yet been referenced specifically in any publications.