Antibody data
- Antibody Data
- Antigen structure
- References [1]
- Comments [0]
- Validations
- Immunocytochemistry [1]
- Chromatin Immunoprecipitation [1]
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Validation data
Reference
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- Product number
- HPA068802 - Provider product page
- Provider
- Atlas Antibodies
- Proper citation
- Atlas Antibodies Cat#HPA068802, RRID:AB_2686039
- Product name
- Anti-MED25
- Antibody type
- Polyclonal
- Description
- Polyclonal Antibody against Human MED25, Gene description: mediator complex subunit 25, Alternative Gene Names: ACID1, ARC92, DKFZp434K0512, TCBAP0758, Validated applications: ICC, ChIP, WB, Uniprot ID: Q71SY5, Storage: Store at +4°C for short term storage. Long time storage is recommended at -20°C.
- Reactivity
- Human
- Host
- Rabbit
- Conjugate
- Unconjugated
- Isotype
- IgG
- Vial size
- 100 µl
- Concentration
- 0.2 mg/ml
- Storage
- Store at +4°C for short term storage. Long time storage is recommended at -20°C.
- Handling
- The antibody solution should be gently mixed before use.
Submitted references An Unexpected Encounter: Respiratory Syncytial Virus Nonstructural Protein 1 Interacts with Mediator Subunit MED25
Van Royen T, Sedeyn K, Moschonas G, Toussaint W, Vuylsteke M, Van Haver D, Impens F, Eyckerman S, Lemmens I, Tavernier J, Schepens B, Saelens X, Dutch R
Journal of Virology 2022;96(19)
Journal of Virology 2022;96(19)
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Supportive validation
- Submitted by
- Atlas Antibodies (provider)
- Main image
- Experimental details
- Immunofluorescent staining of human cell line A549 shows localization to nucleoplasm.
- Sample type
- Human
Supportive validation
- Submitted by
- Atlas Antibodies (provider)
- Main image
- Experimental details
- ChIP-Exo-Seq composite graph for Anti-MED25 (HPA068802, Lot 000018373) tested in K562 cells. Strand-specific reads (blue: forward, red: reverse) and IgG controls (black: forward, grey: reverse) are plotted against the distance from a composite set of reference binding sites. The antibody exhibits robust target enrichment compared to a non-specific IgG control and precisely reveals its structural organization around the binding site. Data generated by Prof. B. F. Pugh´s Lab at Cornell University.