IFITM3 (D8E8G) XP® Rabbit mAb (BSA and Azide Free) #74766
- WB
- IHC
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 15 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
Formulation
Storage
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val5 of human IFITM3 protein.
Background
Interferon-induced transmembrane protein (IFITM) family members are composed of short amino- and carboxy-termini, two transmembrane domains, and a cytoplasmic domain (1). There are four family members in humans: IFITM1, IFITM2, IFITM3, and IFITM5 (2,3). Mice have two additional family members, IFITM6 and IFITM7 (2,3). Basal expression of IFITM proteins is observed in some cells and expression can also be induced by type I and type II interferons (4-6). The primary function of IFITM family proteins appears to be viral restriction, as IFITM proteins inhibit cytosolic entry of viruses by preventing fusion of viral and host membranes (7,8). The mechanism by which IFITM proteins inhibit fusion is unclear. Although IFITM proteins are present on both the plasma membrane and intracellular membranes, they most effectively restrict viral fusion in late endosomes and lysosomes (8,9). In addition, different family members exhibit specific viral preferences (9). For example, IFITM3 is most effective at restricting influenza A infection, while IFITM1 is more successful in controlling filoviruses and SARS (9,10).
- Diamond, M.S. and Farzan, M. (2013) Nat Rev Immunol 13, 46-57.
- Lange, U.C. et al. (2003) BMC Dev Biol 3, 1.
- Hickford, D. et al. (2012) BMC Genomics 13, 155.
- Reid, L.E. et al. (1989) Proc Natl Acad Sci U S A 86, 840-4.
- Lewin, A.R. et al. (1991) Eur J Biochem 199, 417-23.
- Friedman, R.L. et al. (1984) Cell 38, 745-55.
- Brass, A.L. et al. (2009) Cell 139, 1243-54.
- Feeley, E.M. et al. (2011) PLoS Pathog 7, e1002337.
- Huang, I.C. et al. (2011) PLoS Pathog 7, e1001258.
- Everitt, A.R. et al. (2012) Nature 484, 519-23.
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