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Recombinant Human LRPAP Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 4296-LR

R&D Systems, part of Bio-Techne
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4296-LR-050

Key Product Details

Source

E. coli

Accession #

Conjugate

Unconjugated

Applications

Binding Activity

Product Specifications

Source

E. coli-derived human LRPAP protein
Tyr35-Leu357, with an N-terminal Met and a C-terminal 6-His tag

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.

N-terminal Sequence Analysis

Met

Predicted Molecular Mass

38.7 kDa

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.

Formulation, Preparation and Storage

4296-LR
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution
Reconstitute at 100 μg/mL in sterile PBS.

Reconstitution Buffer Available:
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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.

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 alpha2-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

Alternate Names

A2MRAP, A2RAP, HBP44, LRPAP1, RAP

Entrez Gene IDs

4043 (Human); 16976 (Mouse); 116565 (Rat)

Gene Symbol

LRPAP1

UniProt

Additional LRPAP Products

Product Documents for Recombinant Human LRPAP Protein, CF

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human LRPAP Protein, CF

For research use only

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