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Sp1 protein (human), (recombinant) (HA-tag)

 
ALX-201-106-R050 50 µl 510.00 USD
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The protein may be employed in the following fields of research:
i) Promoter studies: Identification of Sp1 binding promoter elements by bandshift or DNase1 footprint assays.
ii) Detection of Sp1 interacting proteins.

Product Specification

Source:Produced in insect cells (Schneider SL2 cells). Human Sp1 is fused to a HA- and a FLAG®-tag (H. Braun and G. Suske; Biotechniques 26, 1038 (1999)).
 
UniProt ID:P08047
 
Quantity:Sufficient for performing at least 25 protein-DNA interaction experiments in 10mM HEPES, pH 7.9, 0.1mM EDTA, 8.5% glycerol, 170mM KCl, 1µM ZnSO4, 37.5µg/ml Poly dIdC, 10mM DTT and 1mg/ml BSA, analyzed by gel shift assay.
 
Formulation:Liquid. In 50mM TRIS-HCl, pH 7.9, containing 420mM KCl, 0.1% NP-40, 12.5mM MgCl2 and 20% glycerol.
 
Purity Detail:Nuclear extract.
 
Specific Activity:0.5BFU/µl (band forming units). 1BFU is sufficient to generate a strong band shift with a labelled oligonucleotide.
 
Application Notes:EMSA promoter characterization, analysis of nuclear extracts (oligonucleotides and recombinant protein serve as a positive control).
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-80°C
 
Handling:Avoid freeze/thaw cycles.
 
Scientific Background:The ubiquitously expressed Sp1 was the first identified and cloned member of the Sp-family of mammalian transcription factors. The 785 aa human protein contains an 81 aa DNA-binding domain consisting of three C2H2-type zinc fingers close to the C-terminus. Two glutamine-rich activation domains are present adjacent to serine/threonine stretches in the N-terminal part of the protein. Sp1 recognizes specifically G-rich elements such as the GC-box (GGGGCGGGG) and the GT/CACC-box (GGTGTGGGG) found in housekeeping as well as in many tissue-specific and viral genes.
 
Technical Info/Product Notes:Nuclear extract was prepared from HA/FLAG-Sp1 expressing SL2 cells. In EMSAs, DNA-protein complexes are separated from free (unbound) oligonucleotides by native gel-electrophoresis. The formation of a specific DNA-protein complex results in a lower mobility of this complex compared to the mobility of the free DNA.The specificity of the DNA-protein interaction can  be analyzed by competition or supershift experiments. An excess of unlabeled specific oligonucleotide interferes with the formation of a specific band, whereas unspecific or mutated oligonucleotides have no effect. The presence of a specific antibody leads to the formation of a very slow migrating antibody-protein-DNA complex.

FLAG is a registered trademark of Sigma-Aldrich Co.
 
201-106 1
Structure of Sp1 protein.
201-106 2
Bandshift with recombinant Sp1.
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201-106 1 201-106 2

Product Literature References

p53 coordinates base excision repair to prevent genomic instability: M. Poletto, et al.; Nucleic Acids Res. 44, 3165 (2016), Application(s): Cell culture, Abstract; Full Text
Bifurcated converging pathways for high Ca2+- and TGFbeta-induced inhibition of growth of normal human keratinocytes: M. Sakaguchi, et al.; PNAS 102, 13921 (2005), Abstract; Full Text
Induction of endoplasmic reticulum-induced stress genes in Panc-1 pancreatic cancer cells is dependent on Sp proteins: M. Abdelrahim, et al.; J. Biol. Chem. 280, 16508 (2005), Abstract; Full Text
The Sp-family of transcription factors: G. Suske; Gene 238, 291 (1999), (Review), Abstract;
Vectors for inducible expression of dual epitope-tagged proteins in insect cells: H. Braun & G. Suske; Biotechniques 26, 1038 (1999), Abstract;
Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain: J.T. Kadanoga, et al.; Cell 51, 1079 (1987), Abstract;

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