Western blot shows lysates of D3 mouse embryonic stem cell line. PVDF membrane was probed with 1 µg/mL of Sheep Anti-Mouse LRPAP Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4480) followed by ...read more
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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Preservative
No Preservative
Concentration
LYOPH
Reconstitution Instructions
Reconstitute at 0.2 mg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for LRPAP Antibody
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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Bu, G. (2001) Int. Rev. Cytol. 209:79.
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.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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