Recombinant Mouse ASGR1/ASGPR1 Protein


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Product Details

Reactivity MuSpecies Glossary
Applications Binding Activity

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Recombinant Mouse ASGR1/ASGPR1 Protein Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. rmASGPR1 immobilized at 2.5 µg/mL (100 µL/well) on a Mouse Anti-polyHistidine Monoclonal Antibody (Catalog # MAB050) coated plate can bind biotinylated beta -Gal-NAc-PAA with a linear range of 2-150 ng/mL.
Mouse myeloma cell line, NS0-derived mouse ASGR1/ASGPR1 protein
Ser60-Asn284, with an N-terminal 9-His tag
Accession #
N-terminal Sequence
Structure / Form
Protein/Peptide Type
Recombinant Proteins
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.


Theoretical MW
27 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
38-40 kDa, reducing conditions

Packaging, Storage & Formulations

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 250 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse ASGR1/ASGPR1 Protein

  • ASGPR 1
  • ASGP-R 1
  • ASGPR1
  • ASGR1
  • asialoglycoprotein receptor 1
  • CLEC4H1
  • C-type lectin domain family 4 member H1
  • Hepatic lectin H1
  • HL-1
  • MHL1
  • RHL1


The mouse asialoglycoprotein receptor (ASGP-R) is an endocytic recycling receptor that belongs to the long-form subfamily of the C-type/Ca++-dependent lectin family (1 - 3). It is a complex of two noncovalently-linked subunits, a major 42 kDa glycoprotein (ASGPR1) and a minor 51 kDa glycoprotein (ASGR2). The major mouse ASGP-R subunit, ASGPR1, is synthesized as a 284 amino acid (aa) type II transmembrane (TM) protein that contains a 39 aa cytoplasmic region, a 21 aa TM segment, and a 224 aa extracellular domain (ECD) (4 - 6). The ECD contains two important structural regions. The first is a stalk region of 56 aa (aa’s # 59 - 117) that contributes to noncovalent oligomerization. The second is a 118 aa, carbohydrate-binding, Ca++-dependent C-type lectin domain (aa’s 160 - 277) that is unusually stabilized by three Ca++ ions (3, 5). There are two potential alternate splice forms for ASGPR1. Both are TM and show a deletion of the C-type lectin domain. One is 113 aa in length and shows a deletion of aa’s # 114 - 284 (7). The second is 132 aa in length and shows a deletion of aa’s 118 - 146 and aa’s 162 - 284 (8). Mouse ASGPR1 ECD is 89% and 79% aa identical to the ASGPR1 ECD in rat and human, respectively. The minor mouse ASGP-R subunit, ASGR2, is also a C-type lectin that shares the same structural organization as ASGR-1. It is 301 aa in length and has two 45 kDa and 51 kDa differentially-glycosylated isoforms (4, 6, 9). The ECD of ASGR2 is 50% aa identical to the ECD of ASGPR1. Although ASGPR1 and 2 can be expressed individually, a fully functional and stable ASGP-R requires simultaneous expression of both subunits (10 - 12). The stoichiometry of a functional ASGP-R is suggested to be either a 2:2, 3:1 or 3:2 ratio of ASGPR1:ASGR2 (13, 14). ASGPR1 is reported to bind Gal (nonreducing), GalNAc, and sialic acid alpha 2,6GalNAc (3, 15, 16). This is generally in the context of triantennary or tetraantennary configurations (2).

  1. Stockert, R. J. (1995) Physiol. Rev. 75:591.
  2. Weigel, P.H. and J.H.N. Yik (2002) Biochim. Biophys. Acta 1572:341.
  3. Meier, M. et al. (2000) J. Mol. Biol. 300:857.
  4. Takezawa, R. et al. (1993) Biochim. Biophys. Acta 1172 :220.
  5. Monroe, R.S. and B.E. Huber (1994) Gene 148:237.
  6. Sanford, J.P. et al. (1988) DNA 7:721.
  7. Heath, P. (2005) GenBank Accession #:Q5NCV2
  8. Heath, P. (2005) GenBank Accession #:Q5NCV1.
  9. Sanford, J.P. and D. Doyle (1990) Biochim. Biophys. Acta 1087:259.
  10. Braun, J.R. et al. (1996) J. Biol. Chem. 271:21160.
  11. Ishibashi, S. et al. (1994) J. Biol. Chem. 269:27803.
  12. Tozawa, R. et al. (2001) J. Biol. Chem. 276:12624.
  13. Bider, M.D. et al. (1996) J. Biol. Chem. 271:31996.
  14. Lodish, H. (1991) Trends Biochem. Sci. 16:374.
  15. Westerlind, U. et al. (2004) Glyconj. J. 21:227.
  16. Park, E.I. et al. (2005) Proc. Natl. Acad. Sci. USA 102:17125.

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Gene Symbol Asgr1