M3694
Anti-α1,2-Mannosidase IA antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Synonym(s):
Anti-HUMM3, Anti-HUMM9, Anti-MAN9
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About This Item
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biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~73 kDa
species reactivity
human, rat, mouse
technique(s)
indirect immunofluorescence: 5-10 μg/mL using human HepG2 cells or rat NRK cells
western blot (chemiluminescent): 0.5-1 μg/mL using whole extract of mouse NIH3T3 cells
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... MAN1A1(4121)
mouse ... Man1a(17155)
rat ... Man1a1(294410)
Related Categories
General description
α1,2-Mannosidase IA is a type II transmembrane Golgi-resident enzyme that belongs to class I α1,2-Mannosidases (glycosylhydrolase family 47). The highly conserved Class I α1,2-Mannosidases classified into three subgroups according to their enzymatic activities. α1,2-Mannosidase IA is predominantly detected in the juxtanuclear Golgi region. The three subgroups differ in their expression pattern, subcellular localization, and substrate specificity.
Immunogen
synthetic peptide corresponding to amino acids 138-154 of human α1,2-mannosidase IA with N-terminal added cysteine, conjugated to KLH. The corresponding sequence is identical in mouse.
Application
Anti-α1,2-Mannosidase IA antibody produced in rabbit has been used in:
- immunohistochemistry
- immunoblotting
- immunofluorescence
Biochem/physiol Actions
α1,2-Mannosidase IA belongs to the first subgroup out of the three subgroups of class I α1,2-Mannosidases. The first subgroup consists of yeast and human α 1,2-mannosidases of the endoplasmic reticulum that convert Man9GlcNAc2 to Man8GlcNAc2 isomer B. The second subgroup comprising of mammalian Golgi α1,2-Mannosidases IA, IB, and IC cleave Man9GlcNAc2 to Man5GlcNAc2 via Man8GlcNAc2 isomer A and C. The third subgroup of yeast and mammalian proteins do not show any activity on Man9GlcNAc2. Proteins from subgroup 1 and 3 have been implicated in ER quality control and in proteasomal degradation of misfolded glycoproteins. The Golgi mannosidases from the second subgroup may play a role in the ERAD (endoplasmic reticulum-associated degradation) of defective glycoproteins. The three subgroups have been found to pariticipate in the maturation of Asn-linked glycoproteins in the endoplasmic reticulum (ER) and Golgi complex.
Physical form
Solution in 0.01 M phosphate buffered saline containing 1% bovine serum albumin and 15 mM sodium azide.
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
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Yuri D Lobsanov et al.
The Journal of biological chemistry, 277(7), 5620-5630 (2001-11-21)
Class I alpha1,2-mannosidases (glycosylhydrolase family 47) are key enzymes in the maturation of N-glycans. This protein family includes two distinct enzymatically active subgroups. Subgroup 1 includes the yeast and human endoplasmic reticulum (ER) alpha1,2-mannosidases that primarily trim Man(9)GlcNAc(2) to Man(8)GlcNAc(2)
Identification of cholinergic chemosensory cells in mouse tracheal and laryngeal glandular ducts
Krasteva-Christ G, et al.
International Immunopharmacology, 29(1), 158-165 (2015)
Shijiao Huang et al.
Cell reports, 41(8), 111679-111679 (2022-11-24)
N-glycans are processed mainly in the Golgi, and a well-organized Golgi structure is required for accurate glycosylation. However, during mitosis the Golgi undergoes severe fragmentation. The resulting trafficking block leads to an extended exposure of cargo molecules to Golgi enzymes.
O-GlcNAcylation mediates metastasis of cholangiocarcinoma through FOXO3 and MAN1A1
Phoomak C, et al.
Oncogene, 37(42), 5648-5648 (2018)
Jie Li et al.
Molecular biology of the cell, 30(4), 478-490 (2018-12-20)
In mammalian cells, the Golgi reassembly stacking protein of 65 kDa (GRASP65) has been implicated in both Golgi stacking and ribbon linking by forming trans-oligomers. To better understand its function and regulation, we used biochemical methods to identify the DnaJ
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