Rabbit Polyclonal USP37 antibody. Suitable for WB and reacts with Xenopus laevis, Human, Mouse, Rat samples. Cited in 4 publications. Immunogen corresponding to Recombinant Fragment Protein within Human USP37 aa 1-300.
Preservative: 0.05% Sodium azide
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Human | Tested |
Mouse | Tested |
Rat | Tested |
Xenopus laevis | Tested |
Species | Dilution info | Notes |
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Species Xenopus laevis | Dilution info 1/2000 | Notes - |
Species Human | Dilution info 1/2000 | Notes - |
Species Mouse | Dilution info 1/2000 | Notes - |
Species Rat | Dilution info 1/2000 | Notes - |
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Deubiquitinase that plays a role in different processes including cell cycle regulation, DNA replication or DNA damage response (PubMed:26299517, PubMed:27296872, PubMed:31911859, PubMed:34509474). Antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), thereby promoting S phase entry. Specifically mediates deubiquitination of 'Lys-11'-linked polyubiquitin chains, a specific ubiquitin-linkage type mediated by the APC/C complex. Phosphorylation at Ser-628 during G1/S phase maximizes the deubiquitinase activity, leading to prevent degradation of cyclin-A (CCNA1 and CCNA2) (PubMed:21596315). Plays an important role in the regulation of DNA replication by stabilizing the licensing factor CDT1 (PubMed:27296872). Plays also an essential role beyond S-phase entry to promote the efficiency and fidelity of replication by deubiquitinating checkpoint kinase 1/CHK1, promoting its stability (PubMed:34509474). Sustains the DNA damage response (DDR) by deubiquitinating and stabilizing the ATP-dependent DNA helicase BLM (PubMed:34606619). Mechanistically, DNA double-strand breaks (DSB) promotes ATM-mediated phosphorylation of USP37 and enhances the binding between USP37 and BLM (PubMed:34606619). Promotes cell migration by deubiquitinating and stabilizing the epithelial-mesenchymal transition (EMT)-inducing transcription factor SNAI (PubMed:31911859). Plays a role in the regulation of mitotic spindle assembly and mitotic progression by associating with chromatin-associated WAPL and stabilizing it through deubiquitination (PubMed:26299517).
KIAA1594, USP37, Ubiquitin carboxyl-terminal hydrolase 37, Deubiquitinating enzyme 37, Ubiquitin thioesterase 37, Ubiquitin-specific-processing protease 37
Rabbit Polyclonal USP37 antibody. Suitable for WB and reacts with Xenopus laevis, Human, Mouse, Rat samples. Cited in 4 publications. Immunogen corresponding to Recombinant Fragment Protein within Human USP37 aa 1-300.
Preservative: 0.05% Sodium azide
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USP37 also known as Ubiquitin-Specific Protease 37 is an enzyme that functions as a deubiquitinase. Mechanically it removes ubiquitin from specific protein substrates therefore regulating their degradation by the proteasome. The protein has a mass of approximately 110 kDa. It expresses widely across various tissues with higher levels noticeable in testis brain and placenta which suggests a context-dependent role in different cell types.
USP37 plays an important role in cell cycle regulation by stabilizing proteins that are key during this process. For example it stabilizes the cyclin A protein which is necessary for the transition between G1/S phases of the cell cycle. USP37 does not function alone; it interacts with other proteins and sometimes becomes part of complexes orchestrating both cellular growth and division by ensuring precise timing and progression within the cell cycle.
USP37 is particularly integral to the cell cycle control and DNA damage response pathways. In the cell cycle pathway it closely interacts with Cyclin-dependent kinase 2 (CDK2) regulating transition checkpoints. In the DNA damage response pathway its interaction with proteins like ATR (ataxia telangiectasia and Rad3-related protein) helps maintain genomic integrity by modulating repair processes. These interactions illustrate how USP37 links mechanistic actions to larger functional pathways.
USP37 has implications in oncogenesis and neurodegenerative diseases. Its deregulation may contribute to the development of cancers by affecting the stability of proteins involved in cell proliferation evident in some breast and prostate cancers. In neurodegenerative diseases like Alzheimer’s USP37’s interaction with the protein Tau may influence neurofibrillary tangle formation a hallmark of the disorder. Understanding these connections aids in researching potential therapeutic targets and interventions.
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All lanes: Western blot - Anti-USP37 antibody (ab190184) at 1/2000 dilution
Lane 1: Human U2OS cell lysate si Control at 40 µg
Lane 2: Human U2OS cells transfected with USP37 siRNA at 40 µg
Lane 3: Mouse Embryo Fibroblaste cell Lysate at 40 µg
Lane 4: Rat INS1 cell lysate at 40 µg
Predicted band size: 110 kDa
All lanes: Western blot - Anti-USP37 antibody (ab190184) at 1/2000 dilution
Lane 1: Xenopus laevis crude egg extracts at 50 µg
Lane 2: U2OS whole cell lysate at 50 µg
Predicted band size: 110 kDa
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