Cubilin C-terminal Antibody [C16H20]

Application: Reactivity: Human

Usage Information

Dilution
WB1:10000 - 1:50000 IHC1:500

Application
WB, IHC

Reactivity
Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
399 kDa 399 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
Cubilin C-terminal Antibody [C16H20] detects endogenous levels of C-terminal region of total Cubilin protein.

Clone
C16H20

Synonym(s)
IFCR, CUBN, Cubilin, 460 kDa receptor, Intestinal intrinsic factor receptor, Intrinsic factor-cobalamin receptor, Intrinsic factor-vitamin B12 receptor

Background
Cubilin is a large multiligand endocytic receptor of the CUB‑domain–containing family that is expressed at the apical surface of absorptive epithelia in the small intestine, renal proximal tubule, visceral yolk sac, and placenta, where it partners with amnionless and megalin to mediate receptor‑driven uptake of carrier‑bound nutrients and filtered plasma proteins. The ectodomain is built from a series of EGF‑like modules followed by 27 CUB domains that form repeated Ca²⁺‑binding ligand‑interaction modules; the C‑terminal half of cubilin contains a large subset of these CUB domains and contributes substantially to ligand binding and receptor multivalency. Calcium‑coordinated CUB domains in this region bind the intrinsic factor–cobalamin complex, albumin, apolipoprotein A‑I, transferrin, hemoglobin, vitamin D–binding protein (GC), immunoglobulin light chains, and high‑density lipoprotein particles, and biochemical mapping indicates that discrete CUB‑domain clusters within the C‑terminal portion provide overlapping but distinct binding sites for IF–B12 and albumin, allowing simultaneous or competitive capture of these ligands at the brush border. Cubilin lacks a transmembrane segment and relies on its N‑terminal interaction with amnionless to form the cubam complex, which anchors the receptor in the membrane and couples ligand‑occupied cubilin to clathrin‑mediated endocytosis and downstream endosomal trafficking, while cooperation with megalin further expands ligand repertoires and endocytic capacity. The C‑terminal half of cubilin is critical for renal protein reabsorption, and human C‑terminal CUBN variants that alter surface expression or ligand binding associate with chronic isolated albuminuria in the presence of preserved glomerular filtration and normal renal function, with the region as a determinant of proximal tubular albumin uptake efficiency rather than glomerular barrier integrity.

Background

Cubilin is a large multiligand endocytic receptor of the CUB‑domain–containing family that is expressed at the apical surface of absorptive epithelia in the small intestine, renal proximal tubule, visceral yolk sac, and placenta, where it partners with amnionless and megalin to mediate receptor‑driven uptake of carrier‑bound nutrients and filtered plasma proteins. The ectodomain is built from a series of EGF‑like modules followed by 27 CUB domains that form repeated Ca²⁺‑binding ligand‑interaction modules; the C‑terminal half of cubilin contains a large subset of these CUB domains and contributes substantially to ligand binding and receptor multivalency. Calcium‑coordinated CUB domains in this region bind the intrinsic factor–cobalamin complex, albumin, apolipoprotein A‑I, transferrin, hemoglobin, vitamin D–binding protein (GC), immunoglobulin light chains, and high‑density lipoprotein particles, and biochemical mapping indicates that discrete CUB‑domain clusters within the C‑terminal portion provide overlapping but distinct binding sites for IF–B12 and albumin, allowing simultaneous or competitive capture of these ligands at the brush border. Cubilin lacks a transmembrane segment and relies on its N‑terminal interaction with amnionless to form the cubam complex, which anchors the receptor in the membrane and couples ligand‑occupied cubilin to clathrin‑mediated endocytosis and downstream endosomal trafficking, while cooperation with megalin further expands ligand repertoires and endocytic capacity. The C‑terminal half of cubilin is critical for renal protein reabsorption, and human C‑terminal CUBN variants that alter surface expression or ligand binding associate with chronic isolated albuminuria in the presence of preserved glomerular filtration and normal renal function, with the region as a determinant of proximal tubular albumin uptake efficiency rather than glomerular barrier integrity.

References
https://pubmed.ncbi.nlm.nih.gov/31613795/ https://pubmed.ncbi.nlm.nih.gov/23291372/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%