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Recombinant Human ASGR2/ASGPR2 Fc Chimera Protein, CF

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Immobilized Recombinant Human ASGR2 Fc Chimera binds humanplasma von Willebrand Factor with an ED50 of 0.15-0.9 μg/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human ASGR2/ASGPR2 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized Recombinant Human ASGR2 Fc Chimer binds human plasma von Willebrand Factor with an ED50 of 0.15-0.9 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human ASGR2 protein
MDHuman IgG1
(Pro100-Lys330)
IEGRHuman ASGR2/ASGPR2
(Gln80-Ala311)
Accession # NP_001172
N-terminusC-terminus
Accession #
N-terminal Sequence
Met
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
53 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.
SDS-PAGE
60-74 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Human ASGR2/ASGPR2 Fc Chimera Protein, CF

  • ASGPR 2
  • ASGP-R 2
  • ASGPR2
  • ASGP-R2
  • ASGR2
  • asialoglycoprotein receptor 2
  • CLEC4H2
  • CLEC4H2FLJ60040
  • C-type lectin domain family 4 member H2
  • HBxAg-binding protein
  • HBXBP
  • Hepatic lectin H2
  • HL-2

Background

Asialoglycoprotein receptor 2 (ASGR-2), also known as C-type lectin domain family 4 member H2 (CLEC4H2) and hepatic lectin H2 (HL-2), is an approximately 48 kDa member of the C-type lectin receptor family (1, 2). ASGR-2 is a single-pass type II transmembrane protein that plays a role in the endocytosis of desialylated glycoproteins and hepatic thrombopoietin production (3). ASGR-2 is closely related to ASGR-1 which is about 2 kDa smaller and is encoded by distinct but closely linked genes. Variations in ASGR-2 structure due to alternative splicing have been reported (4-6). Mature ASGR-2 consists of a 5 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane segment and a 232 aa extracellular domain (ECD). Within the ECD, human ASGR-2 shares 66% and 62% aa sequence identity with mouse and rat ASGR-2, respectively. Both ASGR-2 and ASGR-1 compose the asialoglycoprotein receptor (ASGPR) which mediates removal of potentially hazardous glycoconjugates from blood in health and disease (7). ASGPR, also known as the Ashwell receptor, can modulate von Willebrand factor (vWF) and platelet homeostasis in part through clearance of platelets that are first desialylated during sepsis caused by pathogens including S. pneumoniae. The ASGR-1 chain of the Ashwell receptor can also participate in plasma vWF clearance independently of sialylation and sepsis, ASGR-2 colocalization with plasma vWF was increased in ASGR-1 deficient mice (8). In addition, ASGR-2 expression was shown to be associated with malignant phenotypes in gastric cancer and may represent a specific biomarker for recurrence of some gastric cancers (9).
  1. Spiess, M. and H.F. Lodish. (1985) Proc Natl Acad Sci U.S.A. 19: 6465.
  2. Grewal, P.K. (2010) Methods Enzymol. 479:223.
  3. Grozovsky, R. et al. (2015) Nat Med. 1:47.
  4. Drickamer, K. et al. (1984) J. Biol. Chem. 259:770.
  5. Halberg, D.F. et al. (1987) J. Biol. Chem. 262:9828.
  6. Paietta, E. et al. (1992) J. Biol. Chem. 267:11078.
  7. Harris R.L. et al. (2012) Mol Biol Int. 2012:283974.
  8. Grewal, P. et al. (2008) Nature Medicine. 14:6.
  9. Tanaka H. et al. (2018) Mol Cancer Res. doi: 10.1158/1541. MCR-17-0467. [Epub ahead of print].

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