FITC-Labeled CEACAM5 Protein, Human (HEK293, Fc)

CEACAM5 protein is a cell surface glycoprotein that cooperates with carcinoembryonic antigen-related molecules (such as CEACAM6) to participate in cell adhesion, intracellular signaling, and tumor progression. FITC-Labeled CEACAM5 Protein, Human (HEK293, Fc) is the recombinant human-derived FITC-Labeled CEACAM5 protein, expressed by HEK293 , with Fc labeled tag.

CEACAM5 protein, a cell surface glycoprotein, assumes a multifaceted role in cell adhesion, intracellular signaling, and tumor progression. Functioning as a mediator of both homophilic and heterophilic cell adhesion, CEACAM5 interacts with other carcinoembryonic antigen-related cell adhesion molecules, such as CEACAM6. In the context of tumor progression, CEACAM5 acts as an oncogene, promoting tumor advancement and inducing resistance to anoikis in colorectal carcinoma cells. Additionally, during microbial infection, CEACAM5 serves as a receptor for E. coli Dr adhesins, and the binding of these adhesins results in the dissociation of the CEACAM5 homodimer. These diverse functions underscore the versatility of CEACAM5 in regulating cellular processes and highlight its significance in both physiological and pathological contexts.

Human

HEK293

Fc

P06731-1 (K35-A685)

1048

Full Length of Mature Protein

KLTIESTPFNVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNRQIIGYVIGTQQATPGPAYSGREIIYPNASLLIQNIIQNDTGFYTLHVIKSDLVNEEATGQFRVYPELPKPSISSNNSKPVEDKDAVAFTCEPETQDATYLWWVNNQSLPVSPRLQLSNGNRTLTLFNVTRNDTASYKCETQNPVSARRSDSVILNVLYGPDAPTISPLNTSYRSGENLNLSCHAASNPPAQYSWFVNGTFQQSTQELFIPNITVNNSGSYTCQAHNSDTGLNRTTVTTITVYAEPPKPFITSNNSNPVEDEDAVALTCEPEIQNTTYLWWVNNQSLPVSPRLQLSNDNRTLTLLSVTRNDVGPYECGIQNELSVDHSDPVILNVLYGPDDPTISPSYTYYRPGVNLSLSCHAASNPPAQYSWLIDGNIQQHTQELFISNITEKNSGLYTCQANNSASGHSRTTVKTITVSAELPKPSISSNNSKPVEDKDAVAFTCEPEAQNTTYLWWVNGQSLPVSPRLQLSNGNRTLTLFNVTRNDARAYVCGIQNSVSANRSDPVTLDVLYGPDTPIISPPDSSYLSGANLNLSCHSASNPSPQYSWRINGIPQQHTQVLFIAKITPNNNGTYACFVSNLATGRNNSIVKSITVSASGTSPGLSA

Approximately 140-160 kDa,based on SDS-PAGE under reducing conditions,due to the glycosylation.

≥ 95%, as determined by reducing SDS-PAGE.