Key features and details
- Rabbit polyclonal to COPB2 - C-terminal
- Suitable for: WB, IP, IHC-P
- Reacts with: Mouse, Human
- Isotype: IgG
Product nameAnti-COPB2 antibody - C-terminal
See all COPB2 primary antibodies
DescriptionRabbit polyclonal to COPB2 - C-terminal
Tested applicationsSuitable for: WB, IP, IHC-Pmore details
Species reactivityReacts with: Mouse, Human
Predicted to work with: Rat, Sheep, Rabbit, Horse, Cow, Dog, Pig, Chimpanzee, Rhesus monkey, Orangutan
- HeLa, 293T, Jurkat, TCMK1 and NIH 3T3 whole cell lysates.
This product was previously labelled as beta COP I
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In preparation for this, we have started to update the applications & species that this product is Abpromise guaranteed for.
We are also updating the applications & species that this product has been “predicted to work with,” however this information is not covered by our Abpromise guarantee.
Applications & species from publications and Abreviews that have not been tested in our own labs or in those of our suppliers are not covered by the Abpromise guarantee.
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Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.
Storage bufferpH: 7
Preservative: 0.09% Sodium azide
Constituent: 99% Tris citrate/phosphate
Concentration information loading...
PurityImmunogen affinity purified
Purification notesab192924 was affinity purified using an epitope specific to COPB2 immobilized on solid support.
Our Abpromise guarantee covers the use of ab192924 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/2000 - 1/10000. Predicted molecular weight: 102 kDa.|
|IP||Use at 2-10 µg/mg of lysate.|
FunctionThe coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors.
This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-dependent manner.
Sequence similaritiesBelongs to the WD repeat COPB2 family.
Contains 9 WD repeats.
Cellular localizationCytoplasm. Golgi apparatus membrane. Cytoplasmic vesicle > COPI-coated vesicle membrane. The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it.
- Information by UniProt
- Beta'-coat protein antibody
- Beta'-COP antibody
- Coatomer subunit beta' antibody
Immunohistochemistry of human prostate carcinoma using ab192924 at 1/1000.
Immunohistochemistry of mouse renal cell carcinoma using ab192924 at 1/1000.
Detection of COPB2 by Western Blot of Immunprecipitate.
Lane 1: ab192924 at 0.1 µg/ml labeling COPB2 in 293T whole cell lysate (prepared using NETN lysis buffer) immunoprecipitated using ab192924 at 6µg/mg lysate (1 mg/IP; 20% of IP loaded/lane).
Lane 2: Control IgG.
Detection: Chemiluminescence with exposure time of 30 seconds.
All lanes : Anti-COPB2 antibody - C-terminal (ab192924) at 0.1 µg/ml
Lane 1 : HeLa whole cell lysate
Lane 2 : 293T whole cell lysate
Lane 3 : Jurkat whole cell lysate
Lane 4 : TCMK1 whole cell lysate
Lane 5 : NIH 3T3 whole cell lysate
Lysates/proteins at 50 µg per lane.
Developed using the ECL technique.
Predicted band size: 102 kDa
Exposure time: 30 seconds
Lysates were prepared using NETN lysis buffer.
ab192924 has not yet been referenced specifically in any publications.