Shopping Cart
Remove All
Your shopping cart is currently empty
Anti-RUVBL1 Antibody (3V175) is a Rabbit antibody targeting RUVBL1. Anti-RUVBL1 Antibody (3V175) can be used in WB,FCM.
| Pack Size | Price | USA Warehouse | Global Warehouse | Quantity |
|---|---|---|---|---|
| 25 μL | $151 | 7-10 days | 7-10 days | |
| 50 μL | $263 | 7-10 days | 7-10 days | |
| 100 μL | $472 | 7-10 days | 7-10 days |
| Description | Anti-RUVBL1 Antibody (3V175) is a Rabbit antibody targeting RUVBL1. Anti-RUVBL1 Antibody (3V175) can be used in WB,FCM. |
| Ig Type | IgG |
| Clone | 3V175 |
| Reactivity | Human,Mouse,Rat |
| Application | |
| Recommended Dose | WB: 1:1000-2000; FCM: 1:50-100 |
| Antibody Type | Monoclonal |
| Host Species | Rabbit |
| Subcellular Localization | Nucleus matrix. Nucleus > nucleoplasm. Cytoplasm. Membrane. Cytoplasm > cytoskeleton > centrosome. Mainly localized in the nucleus, associated with nuclear matrix or in the nuclear cytosol, although it is also present in the cytoplasm and associated with the cell membranes. In prophase and prometaphase it is located at the centrosome and the branching microtubule spindles. After mitotic nuclear membrane disintigration it accumulates at the centrosome and sites of tubulin polymerization. As cells pass through metaphase and into telophase it is located close to the centrosome at the early phase of tubulin polymerization. In anaphase it accumulates at the zone of tubule interdigitation. In telophase it is found at polar tubule overlap, and it reappears at the site of chromosomal decondensation in the daughter cells. |
| Tissue Specificity | Ubiquitously expressed with high expression in heart, skeletal muscle and testis. |
| Construction | Recombinant Antibody |
| Purification | Protein A purified |
| Appearance | Liquid |
| Formulation | 10mM phosphate buffered saline (pH 7.4) with 150mM sodium chloride, 0.05% BSA, 0.02% Proclin300 and 50% glycerol. |
| Research Background | Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (3' to 5') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity.Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. |
| Immunogen | A synthesized peptide: human RUVBL1 |
| Antigen Species | Human |
| Gene Name | RUVBL1 |
| Gene ID | |
| Protein Name | RuvB-like 1 |
| Uniprot ID | |
| Function | Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (3' to 5') activity. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. RUVBL1 plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex.
May be able to bind plasminogen at cell surface and enhance plasminogen activation. Essential for cell proliferation. |
| Molecular Weight | Theoretical: 50 kDa. Actual: 50 kDa. |
| Stability & Storage | Store at 2°C-8°C for 1 month. Store at -20°C or -80°C for 12 months. Avoid repeated freeze-thaw cycles. |
| Transport | Shipping with blue ice. |
| Size | Quantity | Unit Price | Amount | Operation |
|---|

Copyright © 2015-2026 TargetMol Chemicals Inc. All Rights Reserved.