M6PR Antibody [J18A13] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat

Usage Information

Dilution
WB1:1000 IHC1:50

Application
WB, IHC

Reactivity
Human, Mouse, Rat

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
275 kDa

Positive Control	Human colon carcinoma; Human liver; Human placenta; Human testes; SK-OV-3 cells; SK-MEL-28 cells; NIH/3T3 cells
Negative Control	A549 cells

Datasheet & SDS

Biological Description

Specificity
M6PR Antibody [J18A13] detects endogenous levels of total M6PR protein.

Clone
J18A13

Synonym(s)
Cation-independent mannose-6-phosphate receptor; CI Man-6-P receptor; CI-MPR; M6PR; MPR 300; Insulin-like growth factor 2 receptor; IGF-II receptor; M6P/IGF2 receptor (M6P/IGF2R); CD222; IGF2R; MPRI

Background
M6PR, also known as the Cation-Dependent Mannose 6-Phosphate Receptor or CD-MPR, is a type I transmembrane glycoprotein belonging to the P-type lectin family and is essential for the sorting of mannose 6-phosphate-tagged lysosomal hydrolases from the trans-Golgi network to endosomes and lysosomes. It consists of a luminal M6P receptor homology domain, which is a flattened beta-barrel composed of six beta-strands and stabilized by four disulfide bonds; loop D, spanning residues 134 to 141, forms one wall of the binding pocket. The receptor also has a single transmembrane domain and a short cytoplasmic tail containing dileucine and tyrosine motifs responsible for intracellular sorting. The M6P binding pocket coordinates the phosphate group via axial 2-hydroxyl hydrogen bonds to conserved residues such as arginine 111, tyrosine 143, and glutamic acid 133, with manganese ions acting as cofactors. CD-MPR binds high-mannose oligosaccharides with M6P tags at neutral pH in the trans-Golgi, clusters with GGA adaptors and clathrin at sorting stations, and packages enzymes into clathrin-coated vesicles for transport to endosomes. In the acidic pH of endosomes, it releases its cargo and is recycled to the Golgi via the retromer complex. CD-MPR recognizes about ten percent of lysosomal hydrolases, while the cation-independent counterpart handles the remainder. M6PR ensures a full complement of lysosomal hydrolases for degradation and recycling, maintains cellular homeostasis, and supports autophagy. The receptor forms constitutive dimers stabilized by inter-subunit salt bridges, which are weakened by ligand binding to facilitate cargo release. Loss-of-function mutations in M6PR cause I-cell disease or mucolipidosis II due to mis-sorting of hydrolases to the extracellular space and substrate accumulation.

Background

M6PR, also known as the Cation-Dependent Mannose 6-Phosphate Receptor or CD-MPR, is a type I transmembrane glycoprotein belonging to the P-type lectin family and is essential for the sorting of mannose 6-phosphate-tagged lysosomal hydrolases from the trans-Golgi network to endosomes and lysosomes. It consists of a luminal M6P receptor homology domain, which is a flattened beta-barrel composed of six beta-strands and stabilized by four disulfide bonds; loop D, spanning residues 134 to 141, forms one wall of the binding pocket. The receptor also has a single transmembrane domain and a short cytoplasmic tail containing dileucine and tyrosine motifs responsible for intracellular sorting. The M6P binding pocket coordinates the phosphate group via axial 2-hydroxyl hydrogen bonds to conserved residues such as arginine 111, tyrosine 143, and glutamic acid 133, with manganese ions acting as cofactors. CD-MPR binds high-mannose oligosaccharides with M6P tags at neutral pH in the trans-Golgi, clusters with GGA adaptors and clathrin at sorting stations, and packages enzymes into clathrin-coated vesicles for transport to endosomes. In the acidic pH of endosomes, it releases its cargo and is recycled to the Golgi via the retromer complex. CD-MPR recognizes about ten percent of lysosomal hydrolases, while the cation-independent counterpart handles the remainder. M6PR ensures a full complement of lysosomal hydrolases for degradation and recycling, maintains cellular homeostasis, and supports autophagy. The receptor forms constitutive dimers stabilized by inter-subunit salt bridges, which are weakened by ligand binding to facilitate cargo release. Loss-of-function mutations in M6PR cause I-cell disease or mucolipidosis II due to mis-sorting of hydrolases to the extracellular space and substrate accumulation.

References
https://pubmed.ncbi.nlm.nih.gov/18272523/ https://pubmed.ncbi.nlm.nih.gov/19928875/

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%