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G2279

Sigma-Aldrich

Monoclonal Anti-β-COP antibody produced in mouse

clone M3A5, ascites fluid

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Synonym(s):
Anti-BARMACS, Anti-COPB
MDL number:
NACRES:
NA.41

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)

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This Item
G6160C7082M7443
species reactivity

monkey, human, chicken, goose, rabbit, canine, bovine, kangaroo rat, rat, hamster

species reactivity

human, rat, hamster, monkey

species reactivity

human, chicken, canine, bovine

species reactivity

mouse, human, rat, monkey

biological source

mouse

biological source

mouse

biological source

mouse

biological source

mouse

conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

clone

M3A5, monoclonal

clone

maD, monoclonal

clone

6F9, monoclonal

clone

Men-8, monoclonal

antibody form

ascites fluid

antibody form

ascites fluid

antibody form

ascites fluid

antibody form

purified from hybridoma cell culture

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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.

Storage Class

10 - Combustible liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


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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
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
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
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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