Recombinant Mouse ASGR1/ASGPR1 Protein Summary
Product Specifications
Ser60-Asn284, with an N-terminal 9-His tag
Analysis
Product Datasheets
Carrier Free
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.
2755-AS
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
| Reconstitution | Reconstitute at 250 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
| 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.
|
2755-AS/CF
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 250 μg/mL in sterile 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.
|
Reconstitution Calculator
Background: ASGR1/ASGPR1
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).
- Stockert, R. J. (1995) Physiol. Rev. 75:591.
- Weigel, P.H. and J.H.N. Yik (2002) Biochim. Biophys. Acta 1572:341.
- Meier, M. et al. (2000) J. Mol. Biol. 300:857.
- Takezawa, R. et al. (1993) Biochim. Biophys. Acta 1172 :220.
- Monroe, R.S. and B.E. Huber (1994) Gene 148:237.
- Sanford, J.P. et al. (1988) DNA 7:721.
- Heath, P. (2005) GenBank Accession #:Q5NCV2
- Heath, P. (2005) GenBank Accession #:Q5NCV1.
- Sanford, J.P. and D. Doyle (1990) Biochim. Biophys. Acta 1087:259.
- Braun, J.R. et al. (1996) J. Biol. Chem. 271:21160.
- Ishibashi, S. et al. (1994) J. Biol. Chem. 269:27803.
- Tozawa, R. et al. (2001) J. Biol. Chem. 276:12624.
- Bider, M.D. et al. (1996) J. Biol. Chem. 271:31996.
- Lodish, H. (1991) Trends Biochem. Sci. 16:374.
- Westerlind, U. et al. (2004) Glyconj. J. 21:227.
- Park, E.I. et al. (2005) Proc. Natl. Acad. Sci. USA 102:17125.
FAQs
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This protein datasheet indicates I need to use a cross-linking antibody, Catalog # MAB050, for biological activity. What is this antibody and is it really necessary?
The antibody is directed against a 6x histidine repeat and is recommended for use as a cross-linker of proteins with 6x his-tag. Crosslinking is often used for proteins that require receptor trimerization and can result greater biological activity. R&D Systems Quality Control tests the performance of these proteins in the presence of the cross-linking antibody. Therefore, it is necessary to use this antibody when trying to achieve the same level of specific activity described in the datasheet.
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