Human CEACAM1 (NP_001703.2, 35 a.a. - 428 a.a.) partial recombinant protein with a 6×His tag at the C-terminus expressed in HEK293 cells.
Host:
Human
Form:
Lyophilized
Preparation Method:
Mammalian cell (HEK293) expression system
Purification:
Ni-sepharose purification
Purity:
> 97% (determined by SDS-PAGE)
Activity:
Measured by its binding ability in a functional ELISA. Immobilized recombinant human CEACAM1 at 5 ug/mL (100 uL/well) can bind recombinant human CEACAM8 with a linear range of 0.5-3 ug/mL.
Quality Control Testing:
SDS-PAGE Stained with Coomassie Blue
Recommend Usage:
SDS-PAGE The optimal working dilution should be determined by the end user.
Storage Buffer:
Lyophilized from a 0.22 um filtered solution of PBS, pH 7.4.
Storage Instruction:
Store at -80°C on dry atmosphere, lyophilized antibodies are stable at least 2 years. After reconstitution with deionized water, store at -20°C or lower. Aliquot to avoid repeated freezing and thawing.
This gene encodes a member of the carcinoembryonic antigen (CEA) gene family, which belongs to the immunoglobulin superfamily. Two subgroups of the CEA family, the CEA cell adhesion molecules and the pregnancy-specific glycoproteins, are located within a 1.2 Mb cluster on the long arm of chromosome 19. Eleven pseudogenes of the CEA cell adhesion molecule subgroup are also found in the cluster. The encoded protein was originally described in bile ducts of liver as biliary glycoprotein. Subsequently, it was found to be a cell-cell adhesion molecule detected on leukocytes, epithelia, and endothelia. The encoded protein mediates cell adhesion via homophilic as well as heterophilic binding to other proteins of the subgroup. Multiple cellular activities have been attributed to the encoded protein, including roles in the differentiation and arrangement of tissue three-dimensional structure, angiogenesis, apoptosis, tumor suppression, metastasis, and the modulation of innate and adaptive immune responses. Multiple transcript variants encoding different isoforms have been reported, but the full-length nature of only two has been determined. [provided by RefSeq