Anti-SP1 antibody produced in goat

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.

Peptide with sequence CSRIESPNENSNNSQ from the internal region of the protein sequence according to NP_612482.2.

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.

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Supplied at 0.5 mg/mL in Tris saline with 0.02% sodium azide and 0.5% bovine serum albumin.