Anti-VLDLR Antibody, clone 4C4G5

Very low-density lipoprotein receptor (UniProt P98156; also known as VLDL receptor, VLDL-R) is encoded by the Vldlr gene (Gene ID 22359) in murine species. Murine very-low-density lipoprotein (VLDL) receptor (VLDLR) is an 110-kDa type I membrane receptor initially produced with a signal peptide sequence (a.a.1-27). The mature receptor has a large extracellular region (a.a. 28-797), a transmembrane domain (a.a. 798-819), and a cytoplasmic tail (a.a. 820-873). VLDLR belongs to the LDLR family of membrane glycoproteins whose members also inculde the low-density lipoprotein receptor (LDLR), the LDLR-related protein (LRP), ApoER2 (LRP-8), and Megalin (LRP-2). The overall extracellular structural features are similar among all LDLR family members. VLDLR contains a cluster of eight cysteine-rich Complement-type/LDLR Class A repeats that mediate ligand-binding and a cluster of six cysteine-poor LDLR Class B repeats (a.a. 495-714) that contains YWTD motifs involved in the pH-dependent ligands dissociation in endosomal compartments. The Class A and B clusters are separated by two EGF-like repeats (a.a. 356-391 and 396-431) and the Class B cluster is followed by an additional EGF-like repeat (a.a. 702-750). VLDLR and ApoER2 both function as receptor for reelin, a glycoprotein that is mainly secreted by Cajal Retzius neurons in the marginal zone and plays an essential role in the formation of the layered neocortex. Immunohistochemical staining reveals differential localization of VLDLR and ApoER2 in the developing mouse cerebral cortex, with VLDLR being localized to the distal portion of leading processes in the marginal zone (MZ) and ApoER2 mainly localized to neuronal processes and the cell membranes of multipolar cells in the multipolar cell accumulation zone (MAZ). The differential expression pattern may therefore allow distinct reelin actions on migrating neurons during both the early and late migratory stages in the developing cerebral cortex.

Clone 4C4G5 (4G) detected VLDLR expression in embryonic and neonatal brain tissues from wild-type, but not Vldlr-knockout mice (Hirota, Y., et al. (2015). J. Comp. Neurol. 523(3):463-478).

Epitope: cytoplasmic domain

GST-tagged recombinant mouse VLDLR cytoplasmic tail (Hirota, Y., et al. (2015). J. Comp. Neurol. 523(3):463-478).

Detect VLDLR using this rat monoclonal Anti-VLDLR, clone 4C4G5 Antibody, Cat. No. MABS1288, validated for use in Immunofluorescence and Western Blotting.

Immunofluorescence Analysis: A 1:500 dilution from a representative lot detected VLDLR expression in 4% paraformaldehyde-fixed, OCT-embedded frozen embryonic E17.5 mouse neocortex tissue section (Courtesy of Yuki Hirota, Ph.D., Keio University, Japan).

Immunofluorescence Analysis: A representative lot detected developmental stage-dependent VLDLR expression patterns among 4% paraformaldehyde-fixed, OCT-embedded frozen embryonic (E14.0 to E17.5) and neonatal (P0) brain tissues from wild-type, but not Vldlr-knockout mice (Hirota, Y., et al. (2015). J. Comp. Neurol. 523(3):463-478).

Western Blotting Analysis: A representative lot detected HA-tagged full-length mouse VLDLR exogenously expressed in HEK293T cells (Hirota, Y., et al. (2015). J. Comp. Neurol. 523(3):463-478).

Research Category
Signaling

Evaluated by Western Blotting in embryonic E16 mouse brain tissue lysate.

Western Blotting Analysis: A 1:1,000 dilution of this antibody detected VLDLR in 10 µg of embryonic E16 mouse brain tissue lysate.

~110 kDa observed. 93.49/96.37 kDa (mature/pro-form) calculated. The larger-than-calculated band size is consistent with that reported in the literature (Hirota, Y., et al. (2015). J. Comp. Neurol. 523(3):463-478). Uncharacterized bands may be observed in some lysate(s).

Protein G purified.

Format: Purified

Purified rat IgG2b 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.

Concentration: Please refer to lot specific datasheet.

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