Anti-TRIM25/EFP antibody (ab245487)
- Datasheet
- References
- Protocols
Overview
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Product name
Anti-TRIM25/EFP antibody
See all TRIM25/EFP primary antibodies -
Description
Rabbit polyclonal to TRIM25/EFP -
Host species
Rabbit -
Tested applications
Suitable for: IP, WBmore details -
Species reactivity
Reacts with: Human -
Immunogen
Synthetic peptide within Human TRIM25/EFP aa 375-425. The exact sequence is proprietary. NP_005073.2
Database link: Q14258 -
Positive control
- WB: HeLa and HEK-293T whole cell lysates. IP: HeLa whole cell lysate.
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General notes
This product was previously labelled as TRIM25
Properties
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Form
Liquid -
Storage instructions
Shipped 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 buffer
Preservative: 0.09% Sodium azide
Constituents: Tris buffered saline, 0.1% BSA -
Concentration information loading... -
Purity
Immunogen affinity purified -
Purification notes
ab245487 was affinity purified using an epitope specific to TRIM25/EFP immobilized on solid support. -
Clonality
Polyclonal -
Isotype
IgG -
Research areas
Associated products
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Compatible Secondaries
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Positive Controls
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Recombinant Protein
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Related Products
Applications
Our Abpromise guarantee covers the use of ab245487 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
| Application | Abreviews | Notes |
|---|---|---|
| IP | Use at 2-5 µg/mg of lysate. | |
| WB | 1/2000 - 1/10000. Predicted molecular weight: 71 kDa. |
Target
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Function
Functions as an ubiquitin E3 ligase and as an ISG15 E3 ligase. Involved in innate immune defense against viruses by mediating ubiquitination of DDX58. Mediates 'Lys-63'-linked polyubiquitination of the DDX58 N-terminal CARD-like region which is crucial for triggering the cytosolic signal transduction that leads to the production of interferons in response to viral infection. Promotes ISGylation of 14-3-3 sigma (SFN), an adapter protein implicated in the regulation of a large spectrum signaling pathway. Mediates estrogen action in various target organs. -
Tissue specificity
Ubiquitous. -
Pathway
Protein modification; protein ubiquitination. -
Sequence similarities
Contains 1 B30.2/SPRY domain.
Contains 1 RING-type zinc finger. -
Domain
The RING-type zinc finger is important for ISG15 E3 ligase activity and autoISGylation. AutoISGylation negatively regulates ISG15 E3 ligase activity.
The C-terminal B30.2/SPRY domain interacts with the first N-terminal CARD domain of DDX58. -
Post-translational
modificationsAuto-ISGylated. -
Cellular localization
Cytoplasm. Colocalized with DDX58 at cytoplasmic perinuclear bodies. - Information by UniProt
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Database links
- Entrez Gene: 7706 Human
- Omim: 600453 Human
- SwissProt: Q14258 Human
- Unigene: 528952 Human
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Alternative names
- E3 ubiquitin/ISG15 ligase TRIM25 antibody
- EFP antibody
- Estrogen responsive finger protein antibody
see all
Images
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Western blot - Anti-TRIM25/EFP antibody (ab245487)All lanes : Anti-TRIM25/EFP antibody (ab245487) at 0.04 µg/ml
Lane 1 : HeLa (human epithelial cell line from cervix adenocarcinoma) whole cell lysate at 50 µg
Lane 2 : HeLa whole cell lysate at 15 µg
Lane 3 : HeLa whole cell lysate at 5 µg
Lane 4 : HEK-293T (human epithelial cell line from embryonic kidney transformed with large T antigen) whole cell lysate at 50 µg
Developed using the ECL technique.
Predicted band size: 71 kDa
Exposure time: 30 seconds -
Immunoprecipitation - Anti-TRIM25/EFP antibody (ab245487)TRIM25/EFP was immunoprecipitated from HeLa (human epithelial cell line from cervix adenocarcinoma) whole cell lysate (1 mg for IP, 20% of IP loaded) with ab245487 at 3 µg/mg lysate. Western blot was performed from the immunoprecipitate using ab245487 at 1 µg/ml.
Lane 1: ab245487 IP in HeLa whole cell lysate.
Lane 2: Control IgG IP in HeLa whole cell lysate.Detection: Chemiluminescence with exposure time of 3 seconds.
Datasheets and documents
References
ab245487 has not yet been referenced specifically in any publications.
