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AB236094

Anti-SENP1 antibody

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(12 Publications)

Rabbit Polyclonal SENP1 antibody. Suitable for WB, IHC-P, ICC/IF and reacts with Human, Mouse samples. Cited in 12 publications. Immunogen corresponding to Recombinant Fragment Protein within Human SENP1 aa 50-250.

View Alternative Names

Sentrin-specific protease 1, Sentrin/SUMO-specific protease SENP1, SENP1

2 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-SENP1 antibody (AB236094)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-SENP1 antibody (AB236094)

Paraffin-embedded human colon cancer tissue stained for SENP1 with ab236094 at 1/100 dilution in immunohistochemical analysis.

Immunocytochemistry/ Immunofluorescence - Anti-SENP1 antibody (AB236094)
  • ICC/IF

Supplier Data

Immunocytochemistry/ Immunofluorescence - Anti-SENP1 antibody (AB236094)

HeLa (Human epithelial cell line from cervix adenocarcinoma) cells stained for SENP1 (Green) using ab236094 at 1/100 dilution in ICC/IF, followed by Alexa Fluor 488® conjugated Goat Anti-Rabbit IgG (H+L).

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Mouse, Human

Applications

WB, ICC/IF, IHC-P

applications

Immunogen

Recombinant Fragment Protein within Human SENP1 aa 50-250. The exact immunogen used to generate this antibody is proprietary information.

Q9P0U3

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Purification notes
Purity >95%.
Storage buffer
pH: 7.4 Preservative: 0.03% Proclin 300 Constituents: PBS, 50% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

SENP1 also known as SUMO-specific protease 1 is an enzyme involved in the process of sumoylation a post-translational modification mechanism affecting various proteins. This enzyme has an approximate molecular mass of 73 kDa. SENP1 specifically cleaves SUMO (Small Ubiquitin-like Modifier) from target proteins regulating their function and localization. It shows strong expression in tissues with high cellular turnover like the thymus spleen and testis indicating its significant role in cell growth and development processes.
Biological function summary

SENP1 contributes to cellular homeostasis by modifying and controlling protein interactions and functions. This enzyme facilitates the recycling of SUMO proteins and affects transcription factors such as HIF1α which are vital for cellular response to hypoxia. SENP1 interacts closely with SUMO E3 ligases in complexes coordinating the addition or removal of SUMO groups from target proteins. Its activity is essential for maintaining the balance between protein sumoylation and desumoylation which impacts numerous cellular processes including cell cycle progression and stress response.

Pathways

SENP1 modulates key regulatory pathways related to its sumoylation mechanism. Major pathways where SENP1 plays a role include the HIF-1 signaling pathway where it affects the stability and activity of HIF1α under low oxygen conditions and the p53 signaling pathway influencing cell cycle and apoptosis. SENP1's interactivity with proteins like Ubc9 a SUMO-conjugating enzyme and PIAS3 a SUMO E3 ligase indicates its broad involvement and regulation within these pathways emphasizing its impact on maintaining cellular function and adaptation.

SENP1 associates with certain cancers and neurodegenerative disorders due to its regulatory influence on protein stability and gene expression. Overexpression of SENP1 is often observed in prostate cancer where it desumoylates HIF1α enhancing its transcriptional activity and promoting tumorigenesis. Additionally alterations in SENP1 function might connect to neurodegenerative diseases like Alzheimer's where protein turnover and cellular stress responses are disrupted. Through these disorders SENP1 connects with proteins such as AR (androgen receptor) in cancer contexts and Tau in Alzheimer's underlying its role in disease pathology.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Protease that catalyzes two essential functions in the SUMO pathway (PubMed : 10652325, PubMed : 15199155, PubMed : 15487983, PubMed : 16253240, PubMed : 16553580, PubMed : 21829689, PubMed : 21965678, PubMed : 23160374, PubMed : 24943844, PubMed : 25406032, PubMed : 29506078, PubMed : 34048572, PubMed : 37257451). The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins (PubMed : 15487983). The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein (PubMed : 15199155, PubMed : 16253240, PubMed : 21829689, PubMed : 21965678, PubMed : 23160374, PubMed : 24943844, PubMed : 25406032, PubMed : 29506078, PubMed : 34048572, PubMed : 37257451). Deconjugates SUMO1 from HIPK2 (PubMed : 16253240). Deconjugates SUMO1 from HDAC1 and BHLHE40/DEC1, which decreases its transcriptional repression activity (PubMed : 15199155, PubMed : 21829689). Deconjugates SUMO1 from CLOCK, which decreases its transcriptional activation activity (PubMed : 23160374). Deconjugates SUMO2 from MTA1 (PubMed : 21965678). Inhibits N(6)-methyladenosine (m6A) RNA methylation by mediating SUMO1 deconjugation from METTL3 and ALKBH5 : METTL3 inhibits the m6A RNA methyltransferase activity, while ALKBH5 desumoylation promotes m6A demethylation (PubMed : 29506078, PubMed : 34048572, PubMed : 37257451). Desumoylates CCAR2 which decreases its interaction with SIRT1 (PubMed : 25406032). Deconjugates SUMO1 from GPS2 (PubMed : 24943844).
See full target information SENP1

Publications (12)

Recent publications for all applications. Explore the full list and refine your search

Nature communications 16:7248 PubMed40769964

2025

IRX3 controls a SUMOylation-dependent differentiation switch in adipocyte precursor cells.

Applications

Unspecified application

Species

Unspecified reactive species

Jan-Inge Bjune,Samantha Laber,Laurence Lawrence-Archer,Patrizia M C Nothnagel,Shuntaro Yamada,Xu Zhao,Pouda Panahandeh Strømland,Niyaz Al-Sharabi,Kamal Mustafa,Pål R Njølstad,Melina Claussnitzer,Roger D Cox,Pierre Chymkowitch,Gunnar Mellgren,Simon N Dankel

International journal of molecular medicine 56: PubMed40682835

2025

SENP1 promotes p27kip1 nuclear export though enhanced SUMOylation in cholangiocarcinoma leading to increased cell proliferation and chemoresistance.

Applications

Unspecified application

Species

Unspecified reactive species

Kainian Jiang,Wei Yang,Jie Huang,Xiaolong Tan,Yan Liu,Saiya Tu,Jian Luo

Scientific reports 15:21497 PubMed40593246

2025

Dynamic changes in sumoylation related proteins SUMO1, SENP1, and UBC9 during the peri implantation period in mice.

Applications

Unspecified application

Species

Unspecified reactive species

Ezgi Golal,Cemre Nur Balci,Nuray Acar

CNS neuroscience & therapeutics 31:e70463 PubMed40485217

2025

DeSUMOylation of IGF2BP2 Promotes Neuronal Differentiation of OM-MSCs by Stabilizing SOX11 to Ameliorate Brain Injury After Intracerebral Hemorrhage.

Applications

Unspecified application

Species

Unspecified reactive species

Jun He,Yuhan Luo,Chuang Wang,Chonghua Jiang,Jian Wang,Ying Xia

Journal of orthopaedic surgery and research 20:542 PubMed40442713

2025

A-485 alleviates postmenopausal osteoporosis by activating GLUD1 deacetylation through the SENP1-Sirt3 signal pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Yinghong Ma,Xiaohua Zou,Qianhong Jian,Jiaxin Dong,Xianbing Huang,Yue Zhai,Li Qian

Technology in cancer research & treatment 23:15330338241257490 PubMed38803001

2024

SENP1-Mediated deSUMOylation Regulates the Tumor Remodeling of Glioma Stem Cells Under Hypoxic Stress.

Applications

Unspecified application

Species

Unspecified reactive species

Ping Wen,Haoran Li,Liang Liu,Xinglei Liu,Zhipeng Xu,Jun Dong

Advanced science (Weinheim, Baden-Wurttemberg, Germany) 11:e2305677 PubMed38225750

2024

SUMOylation of TEAD1 Modulates the Mechanism of Pathological Cardiac Hypertrophy.

Applications

Unspecified application

Species

Unspecified reactive species

Xin Shi,Xuening Dang,Zhenyu Huang,Yanqiao Lu,Huan Tong,Feng Liang,Fei Zhuang,Yi Li,Zhaohua Cai,Huanhuan Huo,Zhaolei Jiang,Changqing Pan,Xia Wang,Chang Gu,Ben He

Journal of the American Heart Association 11:e027004 PubMed36370010

2022

SENP1 Protects Against Pressure Overload-Induced Cardiac Remodeling and Dysfunction Via Inhibiting STAT3 Signaling.

Applications

Unspecified application

Species

Unspecified reactive species

Dan Yang,Di Fan,Zhen Guo,Fang-Yuan Liu,Ming-Yu Wang,Peng An,Zheng Yang,Qi-Zhu Tang

Cell communication and signaling : CCS 20:104 PubMed35836260

2022

SENP1 regulates the transformation of lung resident mesenchymal stem cells and is associated with idiopathic pulmonary fibrosis progression.

Applications

Unspecified application

Species

Unspecified reactive species

Wei Sun,Xiaoshu Liu,Xiaoyu Yang,Xiaoyan Jing,Chunyan Duan,Ganghao Yang,Chi Wu,Hui Huang,Qun Luo,Shu Xia,Qian Zhang,Yang Yang,Zuojun Xu

International journal of molecular sciences 23: PubMed35163636

2022

COVID-19 and Lung Mast Cells: The Kallikrein-Kinin Activation Pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Seigo Nagashima,Anderson Azevedo Dutra,Mayara Pezzini Arantes,Rafaela Chiuco Zeni,Carolline Konzen Klein,Flávia Centenaro de Oliveira,Giulia Werner Piper,Isadora Drews Brenny,Marcos Roberto Curcio Pereira,Rebecca Benicio Stocco,Ana Paula Camargo Martins,Eduardo Morais de Castro,Caroline Busatta Vaz de Paula,Andréa Novaes Moreno Amaral,Cleber Machado-Souza,Cristina Pellegrino Baena,Lucia Noronha
View all publications

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