1-832-868-1888
order@swbio.com
Catalog Number: |
58014 |
other_names: | |
Amount: |
100μg/100μ |
calculated_mw: | |
host_species: | |
Price: |
$390 |
Swiss-Prot No: |
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Form of Antibody: |
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl,0.02% sodium azide and 50% glycerol. |
Storage/Stability: |
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Immunogen: |
synthetic phosphopeptide corresponding to residues surrounding Ser170 of human FBP1 |
Purification: |
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phospholation site. |
Specificity/Sensitivity: |
FBP1 (Phospho-Ser170 )antibody detects endogenous levels of FBP1 only when phospholated at Serine170 . |
Applications: |
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Background: |
Compared with normal cells, tumour cells possess greater metabolic plasticity, which provides them with a selective advantage for survival and proliferation under harsh microenvironmental conditions, including nutrient stress. Glucose deprivation in normal hepatocytes induced PERK-dependent FBP1 S170 phosphorylation, which converted the FBP1 tetramer to monomers and exposed the NLS for binding to importin α3 and subsequent FBP1-nuclear translocation. In the nucleus, S170-phosphorylated FBP1 interacted with PPARα and translocated to the promoter regions of PPARα-mediated β-oxidation genes, where FBP1 bound to histone H3[1] . |
References: |
[1] Wang Z.et al. Fructose-1,6-bisphosphatase 1 functions as a protein phosphatase to dephosphorylate histone H3 and suppresses PPARα-regulated gene transcription and tumour growth. Nat Cell Biol. 2022 Nov;24(11):1655-1665. doi: 10.1038/s41556-022-01009-4. |
appl_detail: |
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