Recombinant Human LRPAP Protein, CF

Catalog # Availability Size / Price Qty
4296-LR-050
R&D Systems Recombinant Proteins and Enzymes
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Citations (3)
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Recombinant Human LRPAP Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its binding ability in a functional ELISA. Immobilized human LRPAP at 0.5 µg/mL can bind rmVLDLR (Catalog # 2258-VL) with an apparent KD <0.25 nM.
Source
E. coli-derived human LRPAP protein
Tyr35-Leu357, with an N-terminal Met and a C-terminal 6-His tag
Accession #
N-terminal Sequence
Analysis
Met
Predicted Molecular Mass
38.7 kDa

Product Datasheets

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4296-LR

Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.

4296-LR

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: 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.
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Background: LRPAP

LRPAP (LDL receptor-related protein-associated protein 1; also named RAP), is a ubiquitously expressed 39 kDa chaperone for LDL receptor family proteins (1, 2). Mature human LRPAP shares 77% amino acid sequence identity with mouse and rat LRPAP. It is organized into three domains of comparable length. Domains D2 and D3 interact with each other, while D1 is independent (3). The D1 domain contains a low affinity binding site for LRP, and the associated D2 and D3 domains bind LRP with high affinity (4). 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 coexpressed 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).

References
  1. Strickland, D.K. et al. (1991) J. Biol. Chem. 266:13364.
  2. Bu, G. (2001) Int. Rev. Cytol. 209:79.
  3. Lazic, A. et al. (2003) Biochemistry 42:14913.
  4. Lazic, A. et al. (2006) Arch. Biochem. Biophys. 450:167.
  5. Bu, G. et al. (1994) J. Biol. Chem. 269:29874.
  6. Willnow, T.E. et al. (1996) EMBO J. 15:2632.
  7. Bu, G. and S. Rennke (1996) J. Biol. Chem. 271:22218.
  8. Obermoeller, L.M. et al. (1997) J. Biol. Chem. 272:10761.
  9. Lee, D. et al. (2006) Mol. Cell 22:423.
  10. Williams, S.E. et al. (1992) J. Biol. Chem. 267:9035.
  11. Medh, J.D. et al. (1995) J. Biol. Chem. 270:536.
  12. Herz, J. et al. (1991) J. Biol. Chem. 266:21232.
  13. Mokuno, H. et al. (1994) J. Biol. Chem. 269:13238.
  14. Orth, K. et al. (1992) Proc. Natl. Acad. Sci. 89:7422.
Long Name
Low Density Lipoprotein-Related Protein-associated Protein
Entrez Gene IDs
4043 (Human); 16976 (Mouse); 116565 (Rat)
Alternate Names
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

Citations for Recombinant Human LRPAP Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

3 Citations: Showing 1 - 3
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  1. The amyloid-beta degradation intermediate Abeta34 is pericyte-associated and reduced in brain capillaries of patients with Alzheimer's disease
    Authors: T Kirabali, S Rigotti, A Siccoli, F Liebsch, A Shobo, C Hock, RM Nitsch, G Multhaup, L Kulic
    Acta Neuropathol Commun, 2019-12-03;7(1):194.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Mapping the binding region on the low density lipoprotein receptor for blood coagulation factor VIII.
    Authors: Kurasawa J, Shestopal S, Karnaukhova E, Struble E, Lee T, Sarafanov A
    J Biol Chem, 2013-06-10;288(30):22033-41.
    Species: Human
    Sample Types: Protein
    Applications: Binding Assay
  3. HIV-1 promotes intake of Leishmania parasites by enhancing phosphatidylserine-mediated, CD91/LRP-1-dependent phagocytosis in human macrophages.
    Authors: Lodge R, Ouellet M, Barat C, Andreani G, Kumar P, Tremblay MJ
    PLoS ONE, 2012-03-06;7(3):e32761.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay

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