InVivoMAb anti-mouse/rat/bovine VLDL-R

Catalog #BE0345
Clone:
IgG-6A6
Reactivities:
Mouse, Rat, Bovine

$150.00 - $3,920.00

In stock
Only %1 left

Product Details

The IgG-6A6 monoclonal antibody reacts with the cytoplasmic tail of mouse, rat, and bovine very low-density lipoprotein receptor (VLDL-R). IgG-6A6 has also been reported to cross-react with human VLDL-R. VLDL-R is a member of the low-density lipoprotein (LDL) receptor family. The VLDL-R binds to triglyceride (TG)-rich lipoproteins but not LDL. VLDL-R is expressed in fatty acid-active tissues including heart, skeletal muscle, fat, and brain. Macrophages and dendritic cells also express VLDL-R. In contrast to the LDL receptor, VLDL-R binds apolipoprotein (apo) E2/2 VLDL particles as well as apoE3/3 VLDL. Various functions of the VLDL-R have been reported in lipoprotein metabolism, metabolic syndrome/atherosclerosis, cardiac fatty acid metabolism, neuronal migration, angiogenesis/tumor growth, and asthma.

Specifications

Isotype Mouse IgG1, λ
Recommended Isotype Control(s) InVivoMAb mouse IgG1 isotype control, unknown specificity
Recommended Dilution Buffer InVivoPure pH 7.0 Dilution Buffer
Immunogen A peptide corresponding to the 10 C-terminal AA’s (SVVSTDDDLA) of rat VLDL-R coupled to KLH.
Reported Applications Western blot
Formulation PBS, pH 7.0
Contains no stabilizers or preservatives
Endotoxin <2EU/mg (<0.002EU/μg)
Determined by LAL gel clotting assay
Purity >95%
Determined by SDS-PAGE
Sterility 0.2 μM filtered
Production Purified from tissue culture supernatant in an animal free facility
Purification Protein G
RRID AB_2894764
Molecular Weight 150 kDa
Storage The antibody solution should be stored at the stock concentration at 4°C. Do not freeze.
Western Blot
Roberts, C. K., et al. (2002). "Effect of diet on adipose tissue and skeletal muscle VLDL receptor and LPL: implications for obesity and hyperlipidemia" Atherosclerosis 161(1): 133-141. PubMed

This study was designed to examine the effect of a high-fat (primarily saturated), refined-carbohydrate (sucrose) diet (HFS), which is known to induce obesity and hyperlipidemia, on adipose tissue and skeletal muscle lipoprotein lipase (LPL) and very-low density lipoprotein receptor (VLDL-R) protein expressions. Female Fischer rats were placed on either a HFS or a low-fat, complex-carbohydrate (LFCC) diet for 22 months beginning at 2 months of age. After 20 months, a subgroup of the HFS rats were switched to the LFCC diet for 2 months (HFS/LFCC). Body weight, feed efficiency, plasma total cholesterol, VLDL-C, low-density lipoprotein cholesterol (LDL-C) and triglyceride (TG) concentrations and LDL-C to high-density lipoprotein cholesterol ratio were all significantly raised by the HFS diet and improved by conversion to the LFCC diet. Adipose tissue heparin-releasable, extractable and total LPL activity expressed per cell were significantly increased in the HFS-fed group. However, LPL protein abundance normalized against total cellular protein was unchanged in the HFS group. This observation is consistent with the presence of adipose tissue hypertrophy. Skeletal muscle LPL protein abundance and heparin-releasable activity were reduced by the HFS diet and improved after switching to the LFCC diet. Both adipose tissue and skeletal muscle VLDL-R protein levels were significantly reduced by the HFS diet and increased after conversion to the LFCC diet. We conclude that an HFS diet induces changes in LPL and VLDL-R in a manner which favors shunting of dietary fat from skeletal muscle to adipose tissue and decreases TG-rich lipoprotein clearance contributing to increased plasma lipids and obesity. Conversion to a LFCC diet can ameliorate the dyslipidemia and tissue changes induced by long-term HFS diet consumption.

Western Blot
Wyne, K. L., et al. (1996). "Expression of the VLDL receptor in endothelial cells" Arterioscler Thromb Vasc Biol 16(3): 407-415. PubMed

In this article we describe the cellular distribution of the very low density lipoprotein receptor (VLDLR), a transmembrane protein that is expressed at high concentrations in skeletal muscle, heart, adipose tissue, and brain but in only trace amounts in the liver. Indirect immunofluorescence localization studies were performed in murine and bovine tissues using a rabbit polyclonal anti-human VLDLR antibody. Immunoreactive VLDLR protein was detected in the endothelium of capillaries and small arterioles but not in veins or venules of bovine skeletal muscle, heart, ovary, and brain. In the liver, there was intense staining of the capillaries and arterioles that supply the capsule and hepatic vessels but no staining of the sinusoidal surfaces. We failed to detect any signal from nonendothelial cells in the liver or peripheral organs. The VLDLR was also expressed at high levels on the endothelial surface of bovine coronary arteries; in contrast, little or no staining was seen in aortic endothelium. Antibody staining of cultured bovine coronary artery endothelial cells demonstrated punctate cell-surface staining, as well as staining of large and small cytoplasmic vesicles. This tissue and cell pattern of expression suggests that the VLDLR plays a role in the transport of VLDL or another plasma constituent from the vascular compartment to adjacent tissues.

Western Blot
Frykman, P. K., et al. (1995). "Normal plasma lipoproteins and fertility in gene-targeted mice homozygous for a disruption in the gene encoding very low density lipoprotein receptor" Proc Natl Acad Sci U S A 92(18): 8453-8457. PubMed

The very low density lipoprotein (VLDL) receptor is a recently cloned member of the low density lipoprotein (LDL) receptor family that mediates the binding and uptake of VLDL when overexpressed in animal cells. Its sequence is 94% identical in humans and rabbits and 84% identical in humans and chickens, implying a conserved function. Its high level expression in muscle and adipose tissue suggests a role in VLDL triacylglycerol delivery. Mutations in the chicken homologue cause female sterility, owing to impaired VLDL and vitellogenin uptake during egg yolk formation. We used homologous recombination in mouse embryonic stem cells to produce homozygous knockout mice that lack immunodetectable VLDL receptors. Homozygous mice of both sexes were viable and normally fertile. Plasma levels of cholesterol, triacylglycerol, and lipoproteins were normal when the mice were fed normal, high-carbohydrate, or high-fat diets. The sole abnormality detected was a modest decrease in body weight, body mass index, and adipose tissue mass as determined by the weights of epididymal fat pads. We conclude that the VLDL receptor is not required for VLDL clearance from plasma or for ovulation in mice.

Western Blot
Jokinen, E. V., et al. (1994). "Regulation of the very low density lipoprotein receptor by thyroid hormone in rat skeletal muscle" J Biol Chem 269(42): 26411-26418. PubMed

A new member of the low density lipoprotein receptor gene family that binds and internalizes very low density lipoprotein (VLDL) particles was previously cloned and characterized from the rabbit and human. The physiological role of this putative VLDL receptor is not known, but its tissue distribution and ligand specificity suggest a possible role in the delivery of triglycerides to peripheral tissue. To learn more about the potential function of this receptor, we measured the changes in VLDL receptor mRNA and protein in various tissues following dietary or hormonal manipulation of rats. No significant changes in the VLDL receptor mRNA or protein were seen after a 48-h fast and subsequent to refeeding. A striking change in receptor mRNA and protein was observed in skeletal muscle of hypothyroid and hyperthyroid rats. In hypothyroid rats, the amount of immunodetectable VLDL receptor was reduced by 80%, while in the hyperthyroid animals it was increased by 300%. These maneuvers did not affect VLDL receptor mRNA or protein levels in adipose tissue or heart. The changes in VLDL receptor mRNA in muscle were opposite to those observed with lipoprotein lipase. These studies suggest that the VLDL receptor plays a role in a metabolic process in muscle that is regulated by thyroid hormone.