Alpha-Fetoprotein Protein, Cynomolgus (HEK293, His)

Alpha-Fetoprotein binds copper, nickel, and fatty acids, displaying particular affinity for bilirubin, albeit less efficiently than serum albumin. Its structural variations, including dimeric and trimeric forms, alongside the monomeric state, contribute to the protein's versatile functionality. This complexity in molecular interactions with diverse ligands underscores Alpha-Fetoprotein's significance in various physiological processes. Alpha-Fetoprotein Protein, Cynomolgus (HEK293, His) is the recombinant cynomolgus-derived Alpha-Fetoprotein protein, expressed by HEK293 , with C-His labeled tag.

The Alpha-Fetoprotein Protein exhibits diverse binding capabilities, including the ability to bind copper, nickel, and fatty acids. Notably, it demonstrates affinity for bilirubin, although less efficiently than serum albumin. The protein exists in various forms, with dimeric and trimeric structures identified in addition to the monomeric form. These structural variations likely contribute to the functional versatility of Alpha-Fetoprotein, suggesting a complex interplay in its molecular interactions with different ligands and emphasizing its significance in various physiological processes.

Cynomolgus

HEK293

C-8*His

A0A2K5U7U0 (R19-V609)

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Full Length of Mature Protein

RTLHRNEYGIASILDSYQCTAEINLPDLATIFFAQFVQEATYKEVSKMVKDVLTAIEKPTGDEQSAGCLENQLPAFLEELCHEKDILEKYGLSDCCSQSEEGRHNCFLAHKKPTPASIPVFQVPEPVTSCEAYEEDRETFMNRFIYEIARRHPFLYAPTILLLAARYDKIIPSCCKAENAVECFQTKAASITKELRESSLLNQHACAVMKNFGTRTFHAITVTKLSQKFTKVNFTEIQKLVLDVAHVHEHCCRGDVLDCLQDGEKIMSYICSQQDTLSNKITECCKLTTLERGQCIIHAENDEKPEGLSPNLNRFLGDRDFNQFSSGEKNIFLASFVHEYSRRHPQLAVSVILRVAKGYQELLEKCFQTENPLECQEKGEEELQKYIQESQALAKRSCGLFQKLGEYYLQNAFLVAYTKKAPQLTSSELMAITRKMAATAATCCQLSEDKLLACGEGAADIIIGHLCIRHETTPVNPGVGQCCTSSYANRRPCFSSLVVDETYVPPAFSDDKFIFHKDLCQAQGVALQTMKQEFLINLVKQKPQITEEQLEAVIADFSGLLEKCCQGQEQEVCFAEEGQKLISKTRAALGV

Approximately 68-75 kDa,based on SDS-PAGE under reducing conditions,due to the glycosylation.

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

<1 EU/μg, determined by LAL method.