Recombinant Mouse LDLR Protein Summary
Product Specifications
Ala22-Arg790 (Ala23Val and Cys27Gly), with a C-terminal 10-His tag
Analysis
Product Datasheets
Carrier Free
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.
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.
2255-LD
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
Reconstitution | Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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2255-LD/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute at 200 μg/mL in sterile PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Scientific Data
When Human LDL is immobilized at 5 μg/mL (100 μL/well), Recombinant Mouse LDLR (Catalog # 2255-LD) binds with an ED50 of 0.4-4 μg/mL.
Reconstitution Calculator
Background: LDLR
The low density lipoprotein receptor (LDL R) is the founding member of the LDL R family of widely expressed cell surface scavenger receptors (1-5). Members of the family are endocytic receptors, but can also co-regulate adjacent cell-surface signaling molecules (3, 4). Many proteins in the LDL R family are cleaved by extracellular proteases to release soluble forms to the circulation, and many of these soluble forms are active (1, 6). Mature LDL R is a 120-160 kDa (depending on glycosylation) type I transmembrane glycoprotein that contains cysteine-rich complement-like repeats (class A LDL domains), calcium-binding EGF repeats, and
beta -propeller structures (class B LDL repeats) in the extracellular domain (ECD) (1-7). A membrane-proximal Ser/Thr-rich region shows extensive O-linked glycosylation (4, 8). A cytoplasmic NPxY motif links the LDL R to clathrin pits for endocytosis, and binds to select adaptor proteins (1, 4, 8). The mouse LDL R ECD shares 78%, 86%, 76% and 76% aa sequence identity with human, rat, bovine, and porcine LDL R, respectively. LDL R is constitutively and widely expressed. Its class A LDL domains near the N-terminus bind apoB and apoE, the apolipoproteins of low- and very low-density lipoproteins (LDL and VLDL), respectively (1, 2, 4, 9). Hepatocyte LDL R is responsible for endocytosis and clearing of most plasma LDL cholesterol (2, 9). At the low pH of the endocytic vesicle, it dissociates, allowing degradation of LDL and recycling of LDL R to the cell surface (1, 4). Lack of LDL R expression or function causes familial hypercholesterolemia (FH) (4, 9, 10). The protease PCSK9 (proprotein convertase subtilisin/kexin type 9) can also cause increased plasma cholesterol by promoting LDL R degradation rather than recycling to the cell surface (10-12). Soluble forms of approximately 140 kDa and 28 kDa are reported to be released by phorbol esters or interferons, respectively (6, 7).
- 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.
- Polvino, W.J. et al. (1992) Somat. Cell Mol. Genet. 18:443.
- Begg, M.J. et al. (2004) Eur. J. Biochem. 271:524.
- Fischer, D.G. et al. (1993) Science 262:250.
- 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. USA 105:13045.
- Tavori, H. et al. (2013) Circulation 127:2403.
Citation for Recombinant Mouse LDLR Protein
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.
1 Citation: Showing 1 - 1
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Identification of lamprey variable lymphocyte receptors that target the brain vasculature
Authors: JM Lajoie, ME Katt, EA Waters, BR Herrin, EV Shusta
Scientific Reports, 2022-04-11;12(1):6044.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay
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