G2279
Monoclonal Anti-β-COP antibody produced in mouse
clone M3A5, ascites fluid
Sinónimos:
Anti-BARMACS, Anti-COPB
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About This Item
Productos recomendados
biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
M3A5, monoclonal
contains
15 mM sodium azide
species reactivity
monkey, human, chicken, goose, rabbit, canine, bovine, kangaroo rat, rat, hamster
technique(s)
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
indirect immunofluorescence: 1:20 using cultured Chinese hamster ovary (CHO) cells
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... COPB1(1315)
rat ... Copb1(114023)
General description
Monoclonal Anti- β-COP (mouse IgG1 isotype) is derived from the M3A5 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse. COPs (coatomer proteins) have a molar mass of 110 kDa and its primary structure is homologous to the β-adaptin component of clathrin-coated vesicles.
The coatomer (approx. 550kDa) consists of proteins designated α-, β-, γ-, and δ-COP, together with substoichiometric amounts of several other proteins.
Specificity
The antibody recognizes an epitope shared by β-COP (110 kDa) found in most tissue culture lines, and by a doublet of brain microtubule-associated protein (MAP2, 270-300 kDa). The antibody stains a reticular structure in the perinuclear area of non-neuronal cells (the periphery of Golgi complex and a population of coatomers scattered throughout the cytoplasm) in tissues from different species and cell processes, as well as cell bodies in chicken brain neuronal cells. It has been used for studies on the effects of various agents that influence energy status, disrupt the Golgi complex, or alter the activity of G-proteins or small GTP-binding proteins on the cellular localization of β-COP. The antibody may be used for the immunoaffinity purification of the protein.
Immunogen
microtubule-associated protein from goose brain.
Application
Monoclonal Anti-β-COP antibody produced in mouse has been used:
- for the localization of β-COP using immunoprecipitation
- in immunocytochemistry
- in immunoblotting
- with other antibodies to Golgi proteins to study the role and relationships of this protein in the cell
Biochem/physiol Actions
COPs (coatomer proteins) are transiently attached to the vesicles involved in transport within the Golgi complex and possibly between the rough ER and Golgi complex.
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
10 - Combustible liquids
wgk_germany
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
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Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
T E Kreis et al.
Annual review of cell and developmental biology, 11, 677-706 (1995-01-01)
Cytosolic coat proteins (COPs) regulate membrane traffic in eukaryotic cells. Three classes of coat protein complexes have so far been identified: clathrin and its adaptor proteins, coatomer (COPI), and COPII. Coatomer (composed of seven different subunits) and ADP-ribosylation factor (ARF)
L Orci et al.
Nature, 362(6421), 648-652 (1993-04-15)
Do the coats on vesicles budded from the Golgi apparatus actually cause the budding, or do they simply coat buds (Fig. 1)? One view (the membrane-mediated budding hypothesis) is that budding is an intrinsic property of Golgi membranes not requiring
G J Choukroun et al.
The Journal of clinical investigation, 106(8), 983-993 (2000-10-18)
The Golgi complex and the trans-Golgi network are critical cellular organelles involved in the endocytic and biosynthetic pathways of protein trafficking. Lipids have been implicated in the regulation of membrane-protein trafficking, vesicular fusion, and targeting. We have explored the role
Y Sagiv et al.
The EMBO journal, 19(7), 1494-1504 (2000-04-04)
Membrane proteins located on vesicles (v-SNAREs) and on the target membrane (t-SNAREs) mediate specific recognition and, possibly, fusion between a transport vesicle and its target membrane. The activity of SNARE molecules is regulated by several soluble cytosolic proteins. We have
M A Stamnes et al.
Proceedings of the National Academy of Sciences of the United States of America, 92(17), 8011-8015 (1995-08-15)
We have isolated a major integral membrane protein from Golgi-derived coatomer-coated vesicles. This 24-kDa protein, p24, defines a family of integral membrane proteins with homologs present in yeast and humans. In addition to sequence similarity, all p24 family members contain
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