Key features and details
- Produced recombinantly (animal-free) for high batch-to-batch consistency and long term security of supply
- Rabbit monoclonal [EPSISR23] to MUC16 (APC)
- Suitable for: Flow Cyt
- Reacts with: Human
- Conjugation: APC. Ex: 645nm, Em: 660nm
Product nameAnti-MUC16 antibody [EPSISR23] (APC)
See all MUC16 primary antibodies
DescriptionRabbit monoclonal [EPSISR23] to MUC16 (APC)
ConjugationAPC. Ex: 645nm, Em: 660nm
Tested applicationsSuitable for: Flow Cytmore details
Species reactivityReacts with: Human
- Flow Cyt: SK-OV-3 cells
This product is a recombinant monoclonal antibody, which offers several advantages including:
- - High batch-to-batch consistency and reproducibility
- - Improved sensitivity and specificity
- - Long-term security of supply
- - Animal-free production
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at +4°C. Do Not Freeze. Store In the Dark.
Storage bufferpH: 7.40
Preservative: 0.02% Sodium azide
Constituents: 1% BSA, PBS
Concentration information loading...
PurityProtein A purified
Immunizing Peptide (Blocking)
Our Abpromise guarantee covers the use of ab221279 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
The cellular localisation of this product has been verified in ICC/IF.
FunctionThought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces.
Tissue specificityExpressed in corneal and conjunctival epithelia (at protein level). Overexpressed in ovarian carcinomas and ovarian low malignant potential (LMP) tumors as compared to the expression in normal ovarian tissue and ovarian adenomas.
Sequence similaritiesContains 2 ANK repeats.
Contains 56 SEA domains.
DomainComposed of three domains, a Ser-, Thr-rich N-terminal domain, a repeated domain containing more than 60 partially conserved tandem repeats of 156 amino acids each (AAs 12061-21862) and a C-terminal transmembrane contain domain with a short cytoplasmic tail.
modificationsHeavily O-glycosylated; expresses both type 1 and type 2 core glycans.
Heavily N-glycosylated; expresses primarily high mannose and complex bisecting type N-linked glycans.
May be phosphorylated. Phosphorylation of the intracellular C-terminal domain may induce proteolytic cleavage and the liberation of the extracellular domain into the extracellular space.
May contain numerous disulfide bridges. Association of several molecules of the secreted form may occur through interchain disulfide bridges providing an extraordinarily large gel-like matrix in the extracellular space or in the lumen of secretory ducts.
Cellular localizationCell membrane. Secreted > extracellular space. May be liberated into the extracellular space following the phosphorylation of the intracellular C-terminus which induces the proteolytic cleavage and liberation of the extracellular domain.
- Information by UniProt
- CA 125 antibody
- CA-125 antibody
- CA125 antibody
Overlay histogram showing SK-OV-3 cells stained with ab221279 (red line). The cells were fixed with 4% formaldehyde (10 min) and then permeabilized with 90% methanol. The cells were then incubated in 1x PBS / 10% normal goat serum to block non-specific protein-protein interactions followed by the antibody (ab221279, 1/500 dilution) for 30 min at 22°C.
Isotype control antibody (black line) was Rabbit IgG (monoclonal) Allophycocyanin used at the same concentration and conditions as the primary antibody. Unlabelled sample (blue line) was also used as a control.
Acquisition of >5,000 events were collected using a 17 mW red Helium-Neon laser (633nm) and 660/20 bandpass filter.
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab221279 has not yet been referenced specifically in any publications.