MRC2 Protein, Canine (HEK293, His)

The MRC2 protein may function as an endocytic lectin receptor with calcium-dependent lectin activity. It internalizes glycosylated ligands via clathrin-mediated endocytosis and releases them in endosomes. MRC2 Protein, Canine (HEK293, His) is the recombinant canine-derived MRC2 protein, expressed by HEK293 , with C-His labeled tag.

The MRC2 protein is implicated in potentially playing a role as an endocytotic lectin receptor with calcium-dependent lectin activity. It functions by internalizing glycosylated ligands from the extracellular space, releasing them in an endosomal compartment through clathrin-mediated endocytosis. MRC2 may be involved in the plasminogen activation system, controlling the extracellular levels of PLAUR/PLAU and thus regulating protease activity at the cell surface. Additionally, it is suggested to contribute to the cellular uptake, remodeling, and degradation of extracellular collagen matrices, potentially influencing collagen turnover during cancer progression and other chronic tissue destructive diseases. MRC2's involvement in the remodeling of the extracellular matrix is proposed to collaborate with matrix metalloproteinases (MMPs). It interacts with the C-terminal region of type I collagen/COL1A1, forms a tri-molecular complex with PLAUR/UPAR and PLAU/pro-UPA, and directly interacts with collagen V, highlighting its versatile role in cellular processes related to extracellular matrix dynamics.

Canine

HEK293

C-8*His

A0A8I3NWU4 (G31-P533)

/

Partial

GAPGDAAAAALPEPNVFVIFSHGLQGCLEAQGGQVRVSSSCNASLPAQRWKWVSRNRLFNLGTMQCLGTGWPGTNTTASLGMYECDREALNLRWHCRTLGDQLSLLLGGRTGNSSKAGGLERGDQTRSGQWRIYGSDEDLCARPYYEVYTIQGNSHGKPCTIPFKYDNQWFHSCTSTGREDGHLWCATTQDYGKDERWGFCPIKSNDCETFWDKDQLTDSCYQFNFQSTLSWREAWASCEQQGADLLSITEIHEQTYINGLLTGYSSTLWIGLNDLDTSGGWQWSDNSPLKYLNWESDQPDNPSEENCGVIRTESSGGWQNRDCSIALPYVCKKKPNATAERPPPDVWANVKVECEPSWQPFQGHCYRLQAEKRSWQESKKACLRGGGDLLSIHSMAELEFITKQIKQEVEELWIGLNDLKLQMNFEWSDGSLVSFTHWHPFEPNNFRDSLEDCVTIWGPEGRWNDSPCNQSLPSICKKAGQLSQGAAEEDHGCRKGWTWHSP

Approximately 60-70 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.