CEACAM5; also known as CEA or D66e; belongs to the large CEACAM subfamily of immunoglobulin superfamily. CEACAM5 is expressed primarily by epithelial cells; and is synthesized as a glycoprotein with a MW of 180 kDa comprising 60% carbohydrate. CEACAM5 contains one Ig-like V-type domain at the N-terminus; followed by six Ig-like C2-type domain and a GPI anchor; and exists as a homodimer. CEACAM5 and CEACAM6 are overexpressed in many cancers and are associated with adhesion and invasion. CEACAM5 can mediate cell-cell adhesion through homotypic and heterotypic interactions. It functions as a homotypic intercellular adhesion molecule and serves as a widely used tumor marker; since it is expressed at higher levels in tumorous tissues than in corresponding normal tissues. CEACAM5 has also been shown to contribute to tumorigenicity by inhibiting cellular differentiation. In addition; CEACAM5 is identified as the host receptor for the Dr family of adhesins of E.Coli; and the binding of E.coli Dr adhesins leads to dissociation of the CEACAM5 homodimer.Immune Checkpoint Immunotherapy Cancer Immunotherapy Targeted Therapy
Product Name:
Human CEACAM5 Recombinant Protein (RPES2018)
Product Code:
RPES2018
Size:
50µg
Species:
Human
Expressed Host:
HEK293 Cells
Synonyms:
CD66e,CEA
Accession:
NP_004354.2
Sequence:
Met 1-Ala 685
Fusion tag:
C-His
Endotoxin:
<1.0 EU per µg as determined by the LAL method.
Protein Construction:
A DNA sequence encoding the mature form of human CEACAM5 (NP_004354.2) (Met 1-Ala 685) was fused with a polyhistidine tag at the C-terminus.
Purity:
> 95 % as determined by reducing SDS-PAGE.
Mol Mass:
72.8 kDa
AP Mol Mass:
100-110 kDa
Formulation:
Lyophilized from sterile PBS; pH 7.4
Shipping:
This product is provided as lyophilized powder which is shipped with ice packs.
Stability and Storage:
Lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
