Siglec-8 Protein, Human (HEK293, Fc)

Siglec-8 protein is a putative adhesion molecule that mediates sialic acid-dependent binding to erythrocytes, preferring α-2,3-linked sialic acid and interacting with α-2,6-linked sialic acid . Its sialic acid recognition site may be hidden through cis interactions with sialic acid on the surface of the same cell. Siglec-8 Protein, Human (HEK293, Fc) is the recombinant human-derived Siglec-8 protein, expressed by HEK293 , with C-hFc labeled tag.

Siglec-8 protein, identified as a putative adhesion molecule, serves as a mediator for sialic-acid dependent binding to red blood cells. It exhibits a preference for binding to alpha-2,3-linked sialic acid and also interacts with alpha-2,6-linked sialic acid. Notably, the sialic acid recognition site of Siglec-8 may be concealed due to cis interactions with sialic acids present on the same cell surface. Furthermore, it has the ability to simultaneously recognize epitopes featuring a terminal N-acetylneuraminic acid (sialic acid) and an underlying 6-O-sulfated galactose, with a specific affinity for Gal-6-sulfated sialyl-Lewis X glycan epitopes.

Human

HEK293

C-hFc

Q9P0M4/NP_037410.1 (M17-A363)

27181  [NCBI]

MEGDRQYGDGYLLQVQELVTVQEGLCVHVPCSFSYPQDGWTDSDPVHGYWFRAGDRPYQDAPVATNNPDREVQAETQGRFQLLGDIWSNDCSLSIRDARKRDKGSYFFRLERGSMKWSYKSQLNYKTKQLSVFVTALTHRPDILILGTLESGHSRNLTCSVPWACKQGTPPMISWIGASVSSPGPTTARSSVLTLTPKPQDHGTSLTCQVTLPGTGVTTTSTVRLDVSYPPWNLTMTVFQGDATASTALGNGSSLSVLEGQSLRLVCAVNSNPPARLSWTRGSLTLCPSRSSNPGLLELPRVHVRDEGEFTCRAQNAQGSQHISLSLSLQNEGTGTSRPVSQVTLAA

80-100 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.