AV43519
Anti-M6PR antibody produced in rabbit
IgG fraction of antiserum
Synonym(s):
Anti-CD-MPR, Anti-FLJ32994, Anti-MPR46, Anti-Mannose-6-phosphate receptor (cation dependent), Anti-SMPR
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
28 kDa
species reactivity
mouse, human, rabbit, guinea pig, rat
concentration
0.5 mg - 1 mg/mL
technique(s)
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... M6PR(4074)
General description
Mannose-6-phosphate receptor (cation dependent) (M6PR) is a receptor for mannose-6-phosphate groups on lysosomal enzymes. It is an integral membrane protein that belongs to type I membrane-spanning glycoproteins. M6PR protein exists as a homodimer and localizes in the trans-Golgi reticulum, endosomes, and the plasma membrane. M6PR gene is mapped to human chromosome 12p13.31.
Immunogen
Synthetic peptide directed towards the N terminal region of human M6PR
Biochem/physiol Actions
Mannose-6-phosphate receptor (cation dependent) (M6PR) aids in intracellular targeting of lysosomal enzymes. It mediates the export of newly synthesized acid hydrolases from the trans-Golgi network (TGN) to endosomes for their subsequent transfer to lysosomes. The presence of a cytoplasmic tail in M6PR protects it from lysosomal degradation. in vitro studies suggest that M6PR favors the secretion of pro-cathepsin D in breast cancer cells.
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
Other Notes
Synthetic peptide located within the following region: RLKPLFNKSFESTVGQGSDTYIYIFRVCREAGNHTSGAGLVQINKSNGKE
Disclaimer
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.
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Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Balraj Doray et al.
The Journal of biological chemistry, 277(21), 18477-18482 (2002-03-12)
The GGAs (Golgi-localizing, gamma-adaptin ear homology domain, ARF-binding) are a multidomain family of proteins implicated in protein trafficking between the Golgi and endosomes. Recent evidence has established that the cation-independent (CI) and cation-dependent (CD) mannose 6-phosphate receptors (MPRs) bind specifically
A Schweizer et al.
Proceedings of the National Academy of Sciences of the United States of America, 94(26), 14471-14476 (1998-02-07)
The 67-amino acid cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor (CD-MPR) contains a signal(s) that prevents the receptor from entering lysosomes where it would be degraded. To identify the key residues required for proper endosomal sorting, we analyzed the
Pradipta Ghosh et al.
Nature reviews. Molecular cell biology, 4(3), 202-212 (2003-03-04)
The two mannose 6-phosphate (M6P) receptors were identified because of their ability to bind M6P-containing soluble acid hydrolases in the Golgi and transport them to the endosomal-lysosomal system. During the past decade, we have started to understand the structural features
Moutushy Mitra et al.
Molecular vision, 16, 828-842 (2010-05-13)
Previously we showed that epithelial cell adhesion molecule (Ep-CAM), a cell surface molecule, was highly expressed in primary retinoblastoma tumors. In the present study, we studied the genes regulated by Ep-CAM in a retinoblastoma Y79 cell line in vitro using
N Bannoud et al.
PloS one, 13(8), e0201844-e0201844 (2018-08-08)
Cancer cells secrete procathepsin D, and its secretion is enhanced by estradiol. Although alterations in the pro-enzyme intracellular transport have been reported, the mechanism by which it is secreted remains poorly understood. In this work, we have studied the influence
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