G6160
Monoclonal Anti-β-COP antibody produced in mouse
clone maD, 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
maD, monoclonal
contains
15 mM sodium azide
species reactivity
human, rat, hamster, monkey
technique(s)
indirect immunofluorescence: 1:80 using cultured Chinese hamster ovary (CHO) cells
microarray: suitable
western blot: 1:1,000 using a preparation of stacked Golgi membranes from rat liver
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
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 in the β-COP protein (110 kDa) and stains the periphery of the Golgi complex using immunocytochemical techniques.
Immunogen
synthetic peptide D1 of β-COP (a.a. 701-715) conjugated to KLH
Application
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunofluorescence (1 paper)
Immunofluorescence (1 paper)
Monoclonal Anti-β-COP antibody produced in mouse is suitable for use as a primary antibody in immunoblot:
It is suitable for immunostaining of β-coatomer, that is used as a intracellular, Golgi protein marker :
It is suitable for use in cell-surface ELISA of human aortic endothelial cells (HAEC)
It is also suitable for western blot analysis at a working dilution of 1:1000 using a preparation of stacked Golgi membranes from rat liver, for indirect immunofluorescence at a working dilution of 1:80 using cultured Chinese hamster ovary (CHO) cells and for microarray.
- analysis at a working dilution of 1:1000 using subcellular proteins from rat PC12 (pheochromocytoma) cells
- analysis of gradient fractions of cerebral microvessels to confirm the separation of plasma membrane lipid raft domains from intracellular membranous components
- detection of the Golgi marker protein β-COP in exosome-enriched extracellular microvesicles (eMV) preparations from untreated HeLa cells
It is suitable for immunostaining of β-coatomer, that is used as a intracellular, Golgi protein marker :
- to confirm that CD14 staining is localized to the cell surface of HAEC
- for examining the localization of Meltrin β in the Golgi apparatus and its vicinity in neurons prepared from developing dorsal root ganglia of mouse embryos
- in NB4 and NB4-LR1 cells to examine the colocalization of PKA regulatory subunits
- in CHO cells to examine colocalization of GFP-Rab24
It is suitable for use in cell-surface ELISA of human aortic endothelial cells (HAEC)
It is also suitable for western blot analysis at a working dilution of 1:1000 using a preparation of stacked Golgi membranes from rat liver, for indirect immunofluorescence at a working dilution of 1:80 using cultured Chinese hamster ovary (CHO) cells and for microarray.
Biochem/physiol Actions
COPs (coatomer proteins) contain adaptin-like, complex (8) and are transiently attached to the vesicles involved in transport within the Golgi complex and possibly between the rough ER and Golgi complex. β-COP has a molar mass of 110kDa and its primary structure is homologous to the β-adaptin component of clathrin-coated vesicles.
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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Product No.
Description
Pricing
Storage Class Code
10 - Combustible liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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J W Creemers et al.
The Journal of biological chemistry, 276(6), 4211-4217 (2000-11-10)
The amyloid peptide is the main constituent of the amyloid plaques in brain of Alzheimer's disease patients. This peptide is generated from the amyloid precursor protein by two consecutive cleavages. Cleavage at the N terminus is performed by the recently
Daniela B Munafó et al.
Traffic (Copenhagen, Denmark), 3(7), 472-482 (2002-06-06)
Rab GTPases comprises a large family of proteins, with more than 50 gene products localized in distinct subcellular compartments. Rab24 is a member of this family whose function is not presently known. In order to elucidate the role of this
Fumi Kano et al.
Journal of cell science, 122(Pt 13), 2218-2227 (2009-06-11)
Yip1A, a mammalian homologue of yeast Yip1p, is a multi-spanning membrane protein that is considered to be involved in transport between the endoplasmic reticulum (ER) and the Golgi. However, the precise role of Yip1A in mammalian cells remains unclear. We
Gwen McCaffrey et al.
Journal of neurochemistry, 106(6), 2395-2409 (2008-07-24)
Tight junctions (TJs) at the blood-brain barrier (BBB) dynamically alter paracellular diffusion of blood-borne substances from the peripheral circulation to the CNS in response to external stressors, such as pain, inflammation, and hypoxia. In this study, we investigated the effect
Seema Dalal et al.
Molecular biology of the cell, 15(2), 637-648 (2003-11-18)
NSF and p97 are related AAA proteins implicated in membrane trafficking and organelle biogenesis. p97 is also involved in pathways that lead to ubiquitin-dependent proteolysis, including ER-associated degradation (ERAD). In this study, we have used dominant interfering ATP-hydrolysis deficient mutants
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