G2279
Monoclonal Anti-β-COP antibody produced in mouse
clone M3A5, ascites fluid
Synonym(s):
Anti-BARMACS, Anti-COPB
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About This Item
Conjugate:
unconjugated
Clone:
M3A5, monoclonal
Application:
ICC, IF, IP
Citations:
25
biological source
mouse
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
Quality Level
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.
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.
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.
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
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
常规特殊物品
动植物来源生物产品
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J S Li et al.
Journal of virology, 70(9), 6029-6035 (1996-09-01)
Infection by human and animal hepadnaviruses displays remarkable host and tissue tropism. The infection cycle probably initiates with binding of the pre-S domain of viral envelope protein to surface receptors present on the hepatocyte. Three types of neutralizing monoclonal antibodies
J G Donaldson et al.
Science (New York, N.Y.), 254(5035), 1197-1199 (1991-11-22)
The binding of cytosolic coat proteins to organelles may regulate membrane structure and traffic. Evidence is presented that a small guanosine triphosphate (GTP)-binding protein, the adenosine diphosphate ribosylation factor (ARF), reversibly associates with the Golgi apparatus in an energy, GTP
The ARF1 GTPase-activating protein: zinc finger motif and Golgi complex localization
Cukierman E, et al.
Science (New York, N.Y.), 270(5244), 1999-2002 (1995)
Binding of ARF and beta-COP to Golgi membranes: possible regulation by a trimeric G protein
Donaldson JG, et al.
Science (New York, N.Y.), 254(5035), 1197-1199 (1991)
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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