Sp1 protein was the first transcription factor to be cloned and characterized. It was first detected in HeLa cells on the basis of its ability to activate the SV40 early promoter transcription. Analysis of structure and function has revealed that Sp1 can be separated into discrete functional domains. The DNA-binding domain consists of three zinc fingers that specifically bind to the GC-box element. Anti-SP1 Antibody detects endogenous levels of total SP1 protein.
Immunogen
The antiserum was produced against synthesized peptide derived from human SP1.
Immunogen Range: 706-755
Biochem/physiol Actions
Sp1 protein was shown to recognize and bind selectively to a GC-rich consensus sequence (GC-box: GGGCGG or CACCC) that presents in the promoter of several important cellular genes, including Simian vacuolating virus 40 (SV40) early, human immunodeficiency virus-1 (HIV-1), platelet-derived growth factor subunit B (PDGF-B), Myc, c-Src etc. In addition to transcription, Sp1 function has been linked to cell growth, cancer and Huntington disease.
Features and Benefits
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Physical form
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
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Mithramycin is a gene-selective Sp1 inhibitor that identifies a biological intersection between cancer and neurodegeneration.
Sleiman SF
The Journal of Neuroscience, 31(18), 6858-6870 (2011)
Decreased association of the transcription factor Sp1 with genes downregulated in Huntington's disease.
Chen-Plotkin AS
Neurobiology of Disease, 22(2), 233-241 (2006)
Structures of zinc finger domains from transcription factor Sp1. Insights into sequence-specific protein-DNA recognition.
Narayan VA
The Journal of Biological Chemistry, 272(12), 7801-7809 (1997)
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