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
origen biológico
mouse
Nivel de calidad
conjugado
unconjugated
forma del anticuerpo
ascites fluid
tipo de anticuerpo
primary antibodies
clon
M3A5, monoclonal
contiene
15 mM sodium azide
reactividad de especies
monkey, human, chicken, goose, rabbit, canine, bovine, kangaroo rat, rat, hamster
técnicas
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
indirect immunofluorescence: 1:20 using cultured Chinese hamster ovary (CHO) cells
isotipo
IgG1
Nº de acceso UniProt
Condiciones de envío
dry ice
temp. de almacenamiento
−20°C
modificación del objetivo postraduccional
unmodified
Información sobre el gen
human ... COPB1(1315)
rat ... Copb1(114023)
Categorías relacionadas
Descripción general
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.
Especificidad
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.
Inmunógeno
microtubule-associated protein from goose brain.
Aplicación
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
Acciones bioquímicas o fisiológicas
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.
Cláusula de descargo de responsabilidad
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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Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
nwg
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
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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)
Cristina Torres et al.
Molecular microbiology, 54(3), 632-646 (2004-10-20)
Protozoan parasites are responsible of important healthy problems, among others malaria, leishmaniasis and trypanosomiasis. The present work reports the characterization of the first mammalian ATP-binding cassette transporter, subfamily A (ABCA)-like in Trypanosoma cruzi. TcABC1 is a single copy gene differentially
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
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