产品详情
简单介绍：
Anti-UBR5 Antibody
详情介绍：
Overview
| Name: | Anti-UBR5 Antibody See all UBR5 primary antibodies
|
| Description: | Goat polyclonal antibody to UBR5. |
| Applications: | ELISA, IHC |
| Reactivity: | Human |
| Immunogen: | Synthetic peptide corresponding to Human UBR5 (C terminal). |
| Sequence: | C-LAIKTKNFGFV |
| Host: | Goat |
| Clonality: | Polyclonal |
| Isotype: | IgG |
| Conjugate: | Unconjugated |
| Purification: | Purified from goat serum by ammonium sulphate precipitation followed by antigen affinity chromatography using the immunizing peptide. |
| Concentration: | 100 μg at 0.5 mg/ml. |
| Product Form: | Liquid |
| Formulation: | Supplied in Tris Buffered Saline, pH 7.30, with 0.02% Sodium Azide and 0.5% BSA. |
| Storage: | Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles. |
Target
| Function: | E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (By similarity). Involved in maturation and/or transcriptional regulation of mRNA by activating CDK9 by polyubiquitination. May play a role in control of cell cycle progression. May have tumor suppressor function. Regulates DNA topoisomerase II binding protein (TopBP1) in the DNA damage response. Plays an essential role in extraembryonic development. Ubiquitinates acetylated PCK1. Also acts as a regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes. |
| Tissue Specificity: | Widely expressed. Most abundant in testis and expressed at high levels in brain, pituitary and kidney. |
| Cellular Location: | Nucleus. |
| Database Links: |
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| Synonyms: | |
| Information: | Target information shown above is from the UniProt Consortium. |
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