Sp1 transcription factor has been used as a standard in electrophoretic mobility shift assay.[1]
Azioni biochim/fisiol
Sp1 was first detected in HeLa cells on the basis of its ability to activate the SV40 early promoter transcription. Subsequently it 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 SV40 early, HIV-1, PDGF-B etc. Sp1 was the first transcription factor to be cloned and characterized. 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. Sp1 contains at least four separate transcriptional activation domains. Two of these domains are glutamine-rich, a well-characterized motif found in several other transcription factors. In addition to transcription, Sp1 function has been linked to cell growth, cancer, Huntington disease and other disorders through transcriptional regulation or specific protein-protein interactions. The function of Sp1 can be regulated by phosphorylation and glycosylation.
Stato fisico
Clear and colorless frozen liquid solution
Nota sulla preparazione
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
Science (New York, N.Y.), 234(4772), 47-52 (1986-10-03)
The biochemical analysis of cellular trans-activators involved in promoter recognition provides an important step toward understanding the mechanisms of gene expression in animal cells. The promoter selective transcription factor, Sp1, has been purified from human cells to more than 95
Fractionation of HeLa cell extracts reveals the presence of a promoter-specific transcription factor, Sp 1, which activates a class of promoters that includes the SV40 early promoter but not several others that have been tested. We analyzed SV40 early-promoter deletion
International journal of biological sciences, 11(9), 1006-1015 (2015-07-30)
The beta-2 adrenergic receptor (beta-2 AR) modulates metabolic processes in skeletal muscle, liver, and adipose tissue in response to catecholamine stimulation. We showed previously that expression of the porcine beta-2 AR gene (ADRB2) is affected by cis-regulatory polymorphisms. These are
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