CL-L1/COLEC10 Protein, Cynomolgus (HEK293, Fc)

CL-L1/COLEC10, operating as a lectin, displays distinct sugar-binding preferences, with a hierarchy of galactose > mannose = fucose > N-acetylglucosamine > N-acetylgalactosamine. Apart from its sugar-binding role, CL-L1/COLEC10 functions as a chemoattractant, suggesting potential engagement in the modulation of cell migration. CL-L1/COLEC10 Protein, Cynomolgus (HEK293, Fc) is the recombinant cynomolgus-derived CL-L1/COLEC10 protein, expressed by HEK293 , with N-hFc labeled tag. The total length of CL-L1/COLEC10 Protein, Cynomolgus (HEK293, Fc) is 165 a.a., with molecular weight of ~56.3 kDa.

CL-L1 (COLEC10) is a lectin protein with a high binding affinity for various sugars, displaying specificity in the following order: galactose > mannose = fucose > N-acetylglucosamine > N-acetylgalactosamine. As a lectin, CL-L1 likely plays a role in sugar recognition and binding, and its diverse sugar specificity suggests potential involvement in various cellular processes. Notably, CL-L1 acts as a chemoattractant, implying a probable role in the regulation of cell migration. The ability of CL-L1 to attract cells suggests its participation in the modulation of cellular movements, possibly influencing processes such as immune cell trafficking or tissue repair. The sugar-binding specificity and chemoattractant properties of CL-L1 highlight its potential significance in mediating interactions between cells and their microenvironment, emphasizing its role in cellular responses and migration regulation (adapted from the provided passage).

Cynomolgus

HEK293

N-hFc

XP_005564031 (G113-K277)

102117541  [NCBI]

Approximately 56.3 kDa

Greater than 90% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.