Recombinant Cynomolgus Monkey LDLR His-tag Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Human LDL is immobilized
at 4.00 µg/mL (100 µL/well), Recombinant Cynomolgus Monkey LDLR His-tag (Catalog # 111151-LD) binds with an ED50 of
30.0-300 ng/mL. |
Source |
Human embryonic kidney cell, HEK293-derived cynomolgus monkey LDLR protein Ala22-Gly788, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Ala22 |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
86 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. |
SDS-PAGE |
125-140 kDa, under reducing conditions. |
Packaging, Storage & Formulations
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.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 200 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Cynomolgus Monkey LDLR His-tag Protein, CF
Background
The low density lipoprotein receptor (LDLR) is
the founding member of the LDLR family, a group of widely expressed type I
transmembrane glycoprotein cell surface scavenger receptors (1-5). Members of
the family are endocytic receptors which bind and internalize extracellular
ligands, including lipoproteins, exotoxins, and lipid‑carrier complexes but can
also co-regulate adjacent cell-surface signaling molecules (3, 4). Mature LDLR
consists of an extracellular domain (ECD) with 7 cysteine‑rich complement-like
repeats (class A LDL domains), calcium-binding EGF repeats, and beta ‑propeller
structures (class B LDL repeats), a transmembrane domain and a cytoplasmic
domain with an NPxY-repeat motif. The ECD of cynomologus LDLR shares 94% amino
acid sequence identity with human LDLR. LDLR is constitutively and widely
expressed and plays a key role in regulating cholesterol homeostasis. The class
A LDL domains near the N-terminus of LDLR bind apoB and apoE, the
apolipoproteins of low- and very low-density lipoproteins (LDL and VLDL),
respectively (1, 2, 4, 7). Hepatocyte LDLR is responsible for
endocytosis and clearing of most plasma LDL cholesterol from circulation (2, 7).
At the low pH of the endocytic vesicle, it dissociates, allowing degradation of
LDL and recycling of LDLR to the cell surface (1, 4). Lack of LDLR
expression or function causes familial hypercholesterolemia (FH) and leads to premature
cardiovascular disease (4, 7, 8). The protease PCSK9 (proprotein
convertase subtilisin/kexin type 9) can also cause increased plasma cholesterol
by promoting LDLR degradation rather than recycling to the cell surface (8-10).
Additionally, soluble forms of LDLR are reported to be released by phorbol
esters or interferons and could serve as a disease marker (5, 11, 12). Several studies
have demonstrated a role for LDLR in cancer progression, including liver
cancer, leukemia, lung cancer, breast cancer, colorectal cancer, and prostate
cancer (13).
- Go, G.W. and A. Mani (2012) Yale J. Biol. Med. 85:19.
- Ren, G. et al. (2010) Proc. Natl. Acad. Sci. USA 107:1059.
- Bujo, H. and Y. Saito (2006) Arterioscler. Thromb. Vasc. Biol. 26:1246.
- Gent, J. and I. Braakman (2004) Cell. Mol. Life Sci. 61:2461.
- Begg, M.J. et al. (2004) Eur. J. Biochem. 271:524.
- Stolt, P.C. and H.H. Bock (2006) Cell. Signal. 18:1560.
- Defesche, J.C. (2004) Semin. Vasc. Med. 4:5.
- De Castro-Oros, I. et al. (2010) Appl. Clin Genet. 3:53.
- Zhang, D.W. et al. (2008) Proc. Natl. Acad. Sci. U.S.A. 105:13045.
- Tavori, H. et al. (2013) Circulation 127:2403.
- Fischer, D.G. et al. (1993) Science 262:250.
- Mbikay, M. et al. (2020) Lipids Health Dis 19:17
- Roslan, Z. et al. (2019) J. Oncol. 2019:536302.
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