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
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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)
Related Categories
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 Code
10 - Combustible liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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N T Ktistakis et al.
The Journal of cell biology, 113(5), 1009-1023 (1991-06-01)
Brefeldin A (BFA) was shown in earlier studies of numerous cell types to inhibit secretion, induce enzymes of the Golgi stacks to redistribute into the ER, and to cause the Golgi cisternae to disappear. Here, we demonstrate that the PtK1
D Kondo et al.
Journal of the American Society of Nephrology : JASN, 11(5), 803-813 (2000-04-20)
Agene encoding olfactomedin-related glycoprotein was isolated from rat glomerulus despite its prior identification as a neuron-specific gene. The mRNA expression was remarkably intense in renal glomerulus and brain and faint in the lung and eye among rat systemic organs. Although
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)
B Maranda et al.
The Journal of biological chemistry, 276(21), 18540-18550 (2001-03-30)
Kidney proximal tubule epithelial cells have an extensive apical endocytotic apparatus that is critical for the reabsorption and degradation of proteins that traverse the glomerular filtration barrier and that is also involved in the extensive recycling of functionally important apical
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