Recombinant Human ASGR1/ASGPR1 Fc Chimera Protein, CF Summary
Accession # P07306-1
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
2 μg/lane of Recombinant Human ASGR1/ASGPR1 Fc Chimera (Catalog # 10255-AS) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 59-71 kDa and 120-140 kDa, respectively.
Immobilized Recombinant Human ASGR-1/ASGPR1 Fc Chimera (Catalog # 10255-AS) binds human plasma von Willebrand Factor with an ED50 of 150-900 ng/mL.
The human asialoglycoprotein receptor (ASGPR) is an endocytic recycling receptor that belongs to the long-form subfamily of the C-type/Ca+2-dependent lectin family (1, 2, 3). It is a complex of two noncovalently-linked subunits, a major 46 kDa glycoprotein (ASGR1) and a minor 50 kDa glycoprotein (ASGR2). The major human ASGPR subunit, ASGR1 (also H1), is synthesized as a 291 amino acid (aa) type II transmembrane (TM) glycoprotein. It contains a 40 aa cytoplasmic region, a 21 aa TM segment, and a 230 aa extracellular domain (ECD) (4 - 6). The cytoplasmic region contains one palmitoylation site at Cys36 that is essential for ligand endocytosis and dissociation (7). The ECD contains two important structural regions. The first is a stalk region of 62 aa (aa 61-123) that contributes to noncovalent oligomerization. The second is a 118 aa, carbohydrate-binding, Ca+2-dependent C-type lectin domain (aa 161-278) that is stabilized by three Ca+2 ions (3, 8). Human ASGR1 ECD is 79% aa identical to mouse ASGR1 ECD. There are two minor (ASGR2) subunits that interact with ASGR1/H1 in a mutually exclusive manner to generate a functional ASGPR (9). They represent alternate splice forms of a type II TM protein. Termed H2b and H2c, H2b differs from H2c only by the presence of a 19 aa insert in its cytoplasmic region. This insert is significant because it allows serine phosphorylation of the cytoplasmic tail and provides for the majority of ASGPR ligand internalization (9). The stoichiometry of a functional ASGPR is unclear, but is suggested to be either a 2:2, 3:1 or 3:2 ratio of ASGR1/H1:ASGR2/H2 (9, 10, 11). ASGPR is found on hepatocytes and a subset of T cells (6, 12). ASGPR is reported to bind Gal (nonreducing), GalNAc, and sialic acid alpha 2,6Gal and GalNAc (3, 13, 14, 15). This is generally within the context of triantennary or tetraantennary configurations (2). The sialic acid terminations are of particular interest because molecules with these motifs most likely represent the endogenous ligands for ASGPR (14).
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