>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
39.9 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.
Publications
Read Publications using 4480-LR in the following applications:
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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse LRPAP Protein, CF
A2MRAP
A2MRAPMRAP
A2RAP
alpha-2-macroglobulin receptor-associated protein 1
alpha-2-macroglobulin receptor-associated protein
alpha-2-MRAP
HBP44
lipoprotein receptor associated protein
low density lipoprotein receptor-related protein associated protein 1
Low density lipoprotein receptor-related protein-associated protein 1
low density lipoprotein-related protein-associated protein 1(alpha-2-macroglobulin receptor-associated protein 1)
LRPAP
LRPAP1
MGC138272
RAP
Background
LRPAP (LDL receptor-related protein-associated protein 1; also named RAP) is a ubiquitously expressed 39 kDa molecular chaperone for LDL receptor family proteins (1, 2). Mature mouse LRPAP is 332 amino acids (aa) in length and secreted into the ER/Golgi of the cell. It shares 77% and 97% aa sequence identity with human and rat LRPAP, respectively. LRPAP contains three approximately 100 aa alpha -helical domains (D1 - D3). The D1 domain contains a low affinity binding site for LRP, and the associated D2 and D3 domains bind LRP with high affinity (4). Domains D2 and D3 interact with each other, while D1 is independent (3). The majority of LRPAP is localized in the endoplasmic reticulum and Golgi (5). LRPAP prevents the premature interaction of LRP, LRP2/megalin, and VLDLR with their co-expressed ligands, thereby promoting proper receptor folding and export from the ER (6 - 8). Protonation of conserved histidine residues within the D3 domain induces the separation of LRPAP and LRP in the relatively acidic Golgi (9). LRPAP, which contains a C-terminal HNEL motif, can then recycle to the ER (9). A minor amount of LRPAP remains associated with LRP and can modulate receptor activity on the cell surface (5). Exogenously applied LRPAP competitively inhibits LDL receptor family binding and uptake of activated alpha 2-macroglobulin, apoB100- or apoE-enriched LDL and VLDL particles, cholesteryl esters, and complexes of PAI-1 with either tPA or uPA (10 - 14).
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Lazic, A. et al. (2003) Biochemistry 42:14913.
Lazic, A. et al. (2006) Arch. Biochem. Biophys. 450:167.
Bu, G. et al. (1994) J. Biol. Chem. 269:29874.
Willnow, T.E. et al. (1996) EMBO J. 15:2632.
Bu, G. and S. Rennke (1996) J. Biol. Chem. 271:22218.
Obermoeller, L.M. et al. (1997) J. Biol. Chem. 272:10761.
Lee, D. et al. (2006) Mol. Cell 22:423.
Williams, S.E. et al. (1992) J. Biol. Chem. 267:9035.
Medh, J.D. et al. (1995) J. Biol. Chem. 270:536.
Herz, J. et al. (1991) J. Biol. Chem. 266:21232.
Mokuno, H. et al. (1994) J. Biol. Chem. 269:13238.
Orth, K. et al. (1992) Proc. Natl. Acad. Sci. 89:7422.
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