ILDR2/B7-2 Protein, Cynomolgus (HEK293, Fc)

The Ig-like domain of Ig-like domain-containing protein is a classic structure of tailed double-stranded (ds) DNA phage particles, which may be formed through weak interactions with carbohydrates on the surface of bacterial cells. Play an auxiliary role in phage infection. ILDR2/B7-2 Protein, Cynomolgus (HEK293, Fc) is the recombinant cynomolgus-derived ILDR2/B7-2 protein, expressed by HEK293 , with C-hFc labeled tag. The total length of ILDR2/B7-2 Protein, Cynomolgus (HEK293, Fc) is 222 a.a., with molecular weight of 90-120 kDa.

Ig-like domain-containing protein is a protein with an Ig-like domain. Immunoglobulins (Ig) often have folded structures, and a central feature of the Ig fold structure is a nonlocal trans-β structure connecting two β-sheets. Ig folding is an important functional structure that is inseparable from the immune response and cell adhesion processes of vertebrates. The Ig-like domain is the classical structure of the constituent proteins of tailed double-stranded (ds) DNA phage particles. Phage Ig-like domains can be divided into three distinct sequence families, resembling classical immunoglobulin domains (I-Set), fibronectin type 3 repeats (FN3), and bacterial Ig-like domains (Big2). Ig-like domains are deceptive, able to be added to larger proteins through programmed ribosomal frameshifting, and are therefore not easily detected. The Ig-like domain may play an auxiliary role in phage infection by weakly interacting with carbohydrates on the bacterial cell surface.

Cynomolgus

HEK293

C-hFc

G7NXR4 (A19-H240)

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APLKIQAYFNETADLPCQFANSQNRSLSELVVFWQNQENLVLNEVYLGKEKFDSVHSKYMGRTSFDPESWTLRLHNLQIKDKGLYQCIIHHKRPTGMIRIHQMNSELSVLANFSQPEIVPISNITENMYINLTCSSIHGYPEPEKMSVLLRTKNSTIEYDGVMQKSQDNVTELYDVSISLSVSFPDVTSNMTIFCVLETDKTQLLSSPFSIELEDPQPPPDH

90-120 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.