ECT2 Antibody (Center)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| IHC-P, WB, E |
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Primary Accession | Q9H8V3 |
Other Accession | Q07139, NP_060568.3 |
Reactivity | Human |
Predicted | Mouse |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 103505 Da |
Antigen Region | 597-625 aa |
Gene ID | 1894 |
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Other Names | Protein ECT2, Epithelial cell-transforming sequence 2 oncogene, ECT2 |
Target/Specificity | This ECT2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 597-625 amino acids from the Central region of human ECT2. |
Dilution | WB~~1:1000 IHC-P~~1:10~50 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | ECT2 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | ECT2 (HGNC:3155) |
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Function | Guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP. Promotes guanine nucleotide exchange on the Rho family members of small GTPases, like RHOA, RHOC, RAC1 and CDC42. Required for signal transduction pathways involved in the regulation of cytokinesis. Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Regulates the translocation of RHOA from the central spindle to the equatorial region. Plays a role in the control of mitotic spindle assembly; regulates the activation of CDC42 in metaphase for the process of spindle fibers attachment to kinetochores before chromosome congression. Involved in the regulation of epithelial cell polarity; participates in the formation of epithelial tight junctions in a polarity complex PARD3-PARD6-protein kinase PRKCQ-dependent manner. Plays a role in the regulation of neurite outgrowth. Inhibits phenobarbital (PB)-induced NR1I3 nuclear translocation. Stimulates the activity of RAC1 through its association with the oncogenic PARD6A- PRKCI complex in cancer cells, thereby acting to coordinately drive tumor cell proliferation and invasion. Also stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death. |
Cellular Location | Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, spindle. Cleavage furrow. Midbody. Cell junction. Cell junction, tight junction. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Sequestered within the nucleus during interphase (PubMed:10579713). Dispersed throughout the cytoplasm upon breakdown of the nuclear envelope during mitosis (PubMed:10579713). Colocalizes with the centralspindlin complex to the mitotic spindles during anaphase/metaphase, the cleavage furrow during telophase and at the midbody at the end of cytokinesis (PubMed:10579713). Colocalized with RhoA at the midbody (PubMed:10579713). Its subcellular localization to tight junction is increased by calcium (PubMed:15254234). |
Tissue Location | Expressed in lung epithelial cells (at protein level). Expressed in squamous cell carcinoma, primary non-small cell lung cancer tumors and lung adenocarcinoma |
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Background
The protein encoded by this gene is a transforming protein that is related to Rho-specific exchange factors and yeast cell cycle regulators. The expression of this gene is elevated with the onset of DNA synthesis and remains elevated during G2 and M phases. In situ hybridization analysis showed that expression is at a high level in cells undergoing mitosis in regenerating liver. Thus, this protein is expressed in a cell cycle-dependent manner during liver regeneration, and is thought to have an important role in the regulation of cytokinesis.
References
Justilien, V., et al. Oncogene 28(41):3597-3607(2009)
Burkard, M.E., et al. PLoS Biol. 7 (5), E1000111 (2009) :
Wolfe, B.A., et al. PLoS Biol. 7 (5), E1000110 (2009) :
Hirata, D., et al. Clin. Cancer Res. 15(1):256-266(2009)
Seguin, L., et al. Mol. Cell. Biol. 29(2):570-581(2009)
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