Monoclonal Anti-β-COP antibody produced in mouse

The coatomer (approx. 550kDa) consists of proteins designated α-, β-, γ-, and δ-COP, together with substoichiometric amounts of several other proteins.

synthetic peptide D1 of β-COP (a.a. 701-715) conjugated to KLH

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunofluorescence (1 paper)

Monoclonal Anti-β-COP antibody produced in mouse is suitable for use as a primary antibody in immunoblot:

• 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.

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.

The antibody recognizes an epitope in the β-COP protein (110 kDa) and stains the periphery of the Golgi complex using immunocytochemical techniques.

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