R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
TAF-Iα (F3E2E) Rabbit mAb #97411
Filter:
- WB
- IP
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 45 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Simple Western™ | 1:10 - 1:50 |
| Immunoprecipitation | 1:50 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
TAF-Iα (F3E2E) Rabbit mAb recognizes endogenous levels of total TAF-Iα protein. This antibody does not cross-react with TAF-Iβ protein.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro8 of human TAF-Iα protein.
Background
Templated activating factor I (TAF-I), also known as SET, is a histone chaperone protein first discovered to play a role in adenovirus chromatin replication (1,2). TAF-I is an acidic protein capable of binding histone cores and remodeling nucleosomes (3). TAF-I is part of the inhibitor of acetyltransferases (INHAT) complex, which sharply represses histone acetylation by PCAF and P300/CBP (4). INHAT complex binding to histone tails is affected by certain histone marks (5). TAF-I has two predominant isoforms, TAF-Iα and TAF-Iβ, which only differ in the N-terminus. TAF-Iα is the predominant isoform in embryonic stem cells, and its expression is regulated by pluripotent factors. Upon differentiation, an isoform shift takes place as the alternative promoter is upregulated, generating TAF-Iβ (6-8). TAF-I uniquely exhibits histone chaperone activity toward linker histone H1, regulating higher-order chromatin structure. TAF-Iα has less activity than TAF-Iβ due to its inhibitory interaction between its unique N-terminus and the C-terminus (9,10). TAF-I has been implicated in oncogenic transformation by inhibiting apoptosis (11).
- Matsumoto, K. et al. (1993) J Biol Chem 268, 10582-7.
- Nagata, K. et al. (1995) Proc Natl Acad Sci USA 92, 4279-83.
- Kato, K. et al. (2007) Nucleic Acids Res 35, 705-15.
- Seo, S.B. et al. (2001) Cell 104, 119-30.
- Schneider, R. et al. (2004) J Biol Chem 279, 23859-62.
- Nagata, K. et al. (1998) Exp Cell Res 240, 274-81.
- Edupuganti, R.R. et al. (2017) Stem Cell Reports 9, 1291-1303.
- Asaka, M.N. et al. (2008) Biochem Biophys Res Commun 376, 665-70.
- Kato, K. et al. (2011) J Cell Sci 124, 3254-65.
- Kajitani, K. et al. (2017) Genes Cells 22, 334-347.
- Nenasheva, V.V. et al. (2021) In Vitro Cell Dev Biol Anim 57, 531-538.
限制使用
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