Phospho-GLI1 (Thr1074) Antibody #35875
- WB
- IP
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 160 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
Storage
Protocol
Specificity / Sensitivity
Phospho-GLI1 (Thr1074) Antibody recognizes endogenous levels of GLI1 protein only when phosphorylated at Thr1074.
Species Reactivity:
Human
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Thr1074 of human GLI1 protein. Antibodies are purified by peptide affinity chromatography.
Background
GLI was first identified as a gene amplified in a malignant glioma (1) capable of transforming primary cells in cooperation with adenovirus E1A (2). GLI belongs to the Krüppel family of zinc finger proteins that includes three mammalian GLI proteins: GLI1, GLI2, and GLI3 (3). These GLI proteins are similar to the Drosophila homolog Cubitus interruptus (Ci) and function as transcription factors activated by the Hedgehog signaling pathway. Hedgehog signaling plays an important role in animal development, and research studies have shown that this pathway is aberrantly activated in many types of cancers (4,5).
GLI1 phosphorylation by upstream kinases can control its stability, localization, and transcriptional activity. AMPK phosphorylates GLI1 at three sites, Ser102, Ser408, and Thr1074, increasing GLI1 cytoplasmic localization and targeting it for degradation via the β-TrCP/SCF E3 ligase pathway (6,7). IKKβ promotes GLI1 stability by phosphorylating it at a cluster of serine residues (Ser543-Ser548) and Thr1071, inhibiting ITCH-mediated ubiquitination (8). MEKK3 phosphorylates GLI1 n-terminus (Ser201, Ser204, Ser243) and c-terminus (Ser968, Thr1074, Ser1078), preventing GLI1 nuclear accumulation, increasing GLI1 association with Hedgehog-regulator SUFU, and inhibiting GLI1 association with target promoters (9).
- Kinzler, K.W. et al. (1987) Science 236, 70-3.
- Ruppert, J.M. et al. (1991) Mol Cell Biol 11, 1724-8.
- Kinzler, K.W. et al. (1988) Nature 332, 371-4.
- Ingham, P.W. and McMahon, A.P. (2001) Genes Dev 15, 3059-87.
- McMahon, A.P. et al. (2003) Curr Top Dev Biol 53, 1-114.
- Li, Y.H. et al. (2015) Cell Rep 12, 599-609.
- Zhang, R. et al. (2017) Oncotarget 8, 49869-49881.
- Agarwal, N.K. et al. (2016) Blood 127, 605-15.
- Lu, J. et al. (2018) Oncogene 37, 3864-3878.
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