Anti-LDL Receptor Antibody, clone 2H7.1

Epitope: Extracellular class A domains 1-3.

GST-tagged recombinant human LDL receptor extracellular fragment corresponding to class A domains 1-3.

Concentration: Please refer to lot specific datasheet.

Format: Purified

Protein G Purified

Purified mouse monoclonal IgG2bκ antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.

Evaluated by Western Blotting in human adrenal gland tissue lysate.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected LDL receptor in 10 µg of human adrenal gland tissue lysate.

Anti-LDL Receptor Antibody, clone 2H7.1 is an antibody against LDL Receptor for use in Western Blotting, Immunohistochemistry (Paraffin), Flow Cytometry.

Immunohistochemistry Analysis: A 1:250 dilution from a representative lot detected LDL receptor immunoreactivity in human adrenal gland tissue.
Flow Cytometry Analysis: 1.0 µg of this antibody from a representative lot detected LDL receptor expression in one million HepG2 cells.

Research Category
Signaling

Research Sub Category
Lipid Metabolism & Weight Regulation

Expected to react with spliced isoforms 1 and 5 reported by UniProt P01130). Reactivity toward spliced isoforms 2, 3, 4, and 6 has not been determined.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Low-density lipoprotein receptor (UniProt P01130; also known as LDL receptor) is encoded by the LDLR (also known as FH, FHC) gene (Gene ID 3949) in human. Low-density lipoprotein (LDL) receptor recognizes the apoprotein B100 embedded in the outer phospholipid layer of cholesterol-rich LDL particles and mediates their remval by endocytosis via clathrin-coated pits. LDL receptor also recognizes the apoE protein found in chylomicron remnants and VLDL remnants (IDL). LDLR gene mutations are known causes of familial hypercholesterolaemia (FH). LDL receptor is initially produced with a signal peptide sequence (a.a. 1-21), the removal of which yields the mature single transmembrane (a.a. 789-810) protein with a C-terminal cytoplasmic tail (a.a. 811-860) and a large N-terminal extracellular region (a.a. 22-788) that contains seven class A (a.a. 25-313) and six class B (a.a. 397-658) LDLR repeats, as well as three EGF-like domains (a.a. 314-353, 354-393, 663-712). LDL-A repeats mediate LDL binding, repeats 2-7 are required for ApoB binding, while only repeat 5 is required for ApoE binding. The class B (LDL-B) repeats region adopts a beta-propeller conformation and is believed to be responsible for the pH-dependent release of LDL in the endosome. The cytoplasmic tail contains a signal sequence important for localizing the receptors to clathrin-coated pits and for triggering receptor-mediated endocytosis upon LDL binding.

~150 kDa observed. Target band size appears larger than the calculated molecular weights of 95.38 kDa (isoform 1), 75.85 kDa (isoform 2), 76.86 kDa (isoform 3), 90.94 kDa (isoform 4), 95.09 kDa (isoform 5), and 82.25 kDa (isoform 6) due to glycosylation. Uncharacterized band(s) may appear in some lysates.