Anti-SP1 Antibody - ChIP Grade (RMAB-0251100)
Cat. No.: RMAB-0251100
Category: Primary Antibodies
INQUIRY
100 μL
Customer Size
Rabbit monoclonal to SP1 - ChIP Grade
Product Features
| Isotype | IgG |
|---|---|
| Clonality | Monoclonal |
| Host Species | Rabbit |
| Clone Number | EPR22648-50 |
| Form | Liquid |
| Purity | Protein A purified |
| Species Reactivity | Human |
| Immunogen | Recombinant fragment. |
| Applications | ChIP-seq, Flow Cyt (Intra), ChIC/CUT&RUN-seq, WB, IHC-P, ICC/IF, IP, ChIP |
| Key Features | Produced recombinantly (animal-free) for high batch-to-batch consistency and long term security of supply; Rabbit monoclonal to SP1 - ChIP Grade; Suitable for: ChIP-sequencing, Flow Cyt (Intra), ChIC/CUT&RUN-seq, WB, IHC-P, ICC/IF, IP, ChIP; Knockout validated; Reacts with: Human |
Target Information
| Target Symbol | SP1 |
|---|---|
| Target Name | Transcription factor Sp1 |
| UniProt ID | P08047 |
| Cellular Localization | Nucleus. Cytoplasm. Nuclear location is governed by glycosylated/phosphorylated states. Insulin promotes nuclear location, while glucagon favors cytoplasmic location. |
| Function | Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Binds also the PDGFR-alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. Plays an essential role in the regulation of FE65 gene expression. In complex with ATF7IP, maintains telomerase activity in cancer cells by inducing TERT and TERC gene expression. |
| Post-translational Modifications | Phosphorylated on multiple serine and threonine residues. Phosphorylation is coupled to ubiquitination, sumoylation and proteolytic processing. Phosphorylation on Ser-59 enhances proteolytic cleavage. Phosphorylation on Ser-7 enhances ubiquitination and protein degradation. Hyperphosphorylation on Ser-11 in response to DNA damage has no effect on transcriptional activity. MAPK1/MAPK3-mediated phosphorylation on Thr-453 and Thr-739 enhances VEGF transcription but, represses FGF2-triggered PDGFR-alpha transcription. Also implicated in the repression of RECK by ERBB2. Hyperphosphorylated on Thr-278 and Thr-739 during mitosis by MAPK8 shielding SP1 from degradation by the ubiquitin-dependent pathway. Phosphorylated in the zinc-finger domain by calmodulin-activated PKCzeta. Phosphorylation on Ser-641 by PKCzeta is critical for TSA-activated LHR gene expression through release of its repressor, p17. Phosphorylation on Thr-668, Ser-67 and Thr-681 is stimulated by angiotensin II via the AT1 receptor inducing increased binding to the PDGF-D promoter. This phosphorylation is increased in injured artey wall. Ser-59 and Thr-681 can both be dephosphorylated by PP2A during cell-cycle interphase. Dephosphorylation on Ser-59 leads to increased chromatin association during interphase and increases the transcriptional activity. On insulin stimulation, sequentially glycosylated and phosphorylated on several C-terminal serine and threonine residues. Acetylated. Acetylation/deacetylation events affect transcriptional activity. Deacetylation leads to an increase in the expression the 12(s)-lipooxygenase gene though recruitment of p3 to the promoter. Ubiquitinated. Ubiquitination occurs on the C-terminal proteolytically-cleaved peptide and is triggered by phosphorylation. Sumoylated by SUMO1. Sumoylation modulates proteolytic cleavage of the N-terminal repressor domain. Sumoylation levels are attenuated during tumorigenesis. Phosphorylation mediates SP1 desumoylation. Proteolytic cleavage in the N-terminal repressor domain is prevented by sumoylation. The C-terminal cleaved product is susceptible to degradation. O-glycosylated; contains at least 8 N-acetylglucosamine side chains. Levels are controlled by insulin and the SP1 phosphorylation states. Insulin-mediated O-glycosylation locates SP1 to the nucleus, where it is sequentially deglycosylated and phosphorylated. O-glycosylation affects transcriptional activity through disrupting the interaction with a number of transcription factors including ELF1 and NFYA. Also inhibits interaction with the HIV1 promoter. Inhibited by peroxisomome proliferator receptor gamma (PPARgamma). |
| Sequence Similarities | Belongs to the Sp1 C2H2-type zinc-finger protein family. Contains 3 C2H2-type zinc fingers. |
Storage & Shipping
| Storage Buffer | pH: 7.2; Preservative: 0.01% Sodium azide; Constituents: 40% Glycerol (glycerin, glycerine), 0.05% BSA, PBS |
|---|---|
| Storage & Shipping | Shipped at 4°C. Store at 4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle. |
For research use only. Not for clinical use.
