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货号： bs-12412R-PE-Cy7 基本售价： 2980.0 元 规格： 100ul
产品信息
- 产品编号
- bs-12412R-PE-Cy7
- 英文名称
- Anti-phospho-SP1 (Thr453)/PE-Cy7
- 中文名称
- PE-Cy7标记的磷酸化转录生长因子SP1抗体
- 别 名
- SP1 (phospho T453); p-SP1 (phospho T453); SP1 (phospho-Thr453); SP1 (phospho-T453); p-SP1 (phospho T453); p-TSFP1 (phospho T453); Sp1 transcription factor isoform a; TSFP1; TSFP 1; Specificity protein 1; Transcription factor Sp1; SP 1; SP1; Sp1 transcription factor; SP1_HUMAN.
- 规格价格
- 100ul/2980元购买 大包装/询价
- 说 明 书
- 100ul
- 产品类型
- 磷酸化抗体
- 研究领域
- 肿瘤 细胞生物 发育生物学 神经生物学 信号转导 干细胞 转录调节因子 锌指蛋白 表观遗传学
- 抗体来源
- Rabbit
- 克隆类型
- Polyclonal
- 交叉反应
- Human, Mouse, Rat,
- 产品应用
- ICC=1:50-200 IF=1:50-200
not yet tested in other applications.
optimal dilutions/concentrations should be determined by the end user.
- 分 子 量
- 81kDa
- 性 状
- Lyophilized or Liquid
- 浓 度
- 1mg/ml
- 免 疫 原
- KLH conjugated synthesised phosphopeptide derived from human TSFP1 around the phosphorylation site of Thr453
- 亚 型
- IgG
- 纯化方法
- affinity purified by Protein A
- 储 存 液
- 0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.
- 保存条件
- Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. The lyophilized antibody is stable at room temperature for at least one month and for greater than a year when kept at -20°C. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C.
- 产品介绍
- background:
Sp1 is a sequence-specific transcription factor that recognizes GGGGCGGGGC and closely related sequences, which are often referred to as GC boxes. Sp1 was initially identified as a HeLa cell-derived factor that selectively activates in vitro transcription from the SV40 promoter and binds to the multiple GC boxes in the 21-bp repeated elements in SV40. The sequence specificity of DNA binding is conferred by Zn (II) fingers, whereas a different region of Sp1 appears to regulate the affinity of DNA binding. Sp1 belongs to a subgroup of transcription factors that are phosphorylated upon binding to promoter sequences. Evidence suggests that the early growth response gene, Erg-1 (also known as Zif268 or NGF1-A) (7), may downregulate certain mammalian gene promoters by competing with Sp1 for binding to an overlapping binding motif. The gene encoding human Sp1 maps to chromosome 12q13.1.
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.
Subunit:
Interacts with ATF7IP, ATF7IP2, BAHD1, POGZ, HCFC1, AATF and PHC2. Interacts with varicella-zoster virus IE62 protein. Interacts with HIV-1 Vpr; the interaction is inhibited by SP1 O-glycosylation. Interacts with SV40 VP2/3 proteins. Interacts with SV40 major capsid protein VP1; this interaction leads to a cooperativity between the 2 proteins in DNA binding. Interacts with HLTF; the interaction may be required for basal transcriptional activity of HLTF. Interacts (deacetylated form) with EP300; the interaction enhances gene expression. Interacts with HDAC1 and JUN. Interacts with ELF1; the interaction is inhibited by glycosylation of SP1. Interaction with NFYA; the interaction is inhibited by glycosylation of SP1. Interacts with SMARCA4/BRG1. Interacts with ATF7IP and TBP. Interacts with MEIS2 isoform 4 and PBX1 isoform PBX1a.
Subcellular Location:
Nucleus. Cytoplasm. Nuclear location is governed by glycosylated/phosphorylated states. Insulin promotes nuclear location, while glucagon favors cytoplasmic location.
Tissue Specificity:
Up-regulated in adenocarcinomas of the stomach (at protein level).
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-101 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, p107.
Phosphorylation on Thr-668, Ser-670 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 p300 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).
Similarity:
Belongs to the Sp1 C2H2-type zinc-finger protein family.
Contains 3 C2H2-type zinc fingers.
Database links:Entrez Gene: 6667Human
Entrez Gene: 20683Mouse
Entrez Gene: 24790Rat
Omim: 189906Human
SwissProt: P08047Human
SwissProt: O89090Mouse
SwissProt: Q01714Rat
Unigene: 620754Human
Unigene: 649191Human
Unigene: 4618Mouse
Unigene: 44609Rat
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.