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AB58418

Anti-SENP2 antibody

5

(2 Reviews)

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(9 Publications )

Rabbit Polyclonal SENP2 antibody. Suitable for WB, ICC/IF and reacts with Human samples. Cited in 9 publications. Immunogen corresponding to Synthetic Peptide within Human SENP2 aa 450 to C-terminus.
2 Images
Immunocytochemistry/ Immunofluorescence - Anti-SENP2 antibody (AB58418)
  • ICC/IF

Unknown

Immunocytochemistry/ Immunofluorescence - Anti-SENP2 antibody (AB58418)

ICC/IF image of ab58418 stained HepG2 cells. The cells were 4% formaldehyde fixed (10 min) and then incubated in 1%BSA / 10% normal goat serum / 0.3M glycine in 0.1% PBS-Tween for 1h to permeabilise the cells and block non-specific protein-protein interactions. The cells were then incubated with the antibody (ab58418, 5µg/ml) overnight at +4°C. The secondary antibody (green) was Alexa Fluor® 488 goat anti-mouse IgG (H+L) used at a 1/1000 dilution for 1h. Alexa Fluor® 594 WGA was used to label plasma membranes (red) at a 1/200 dilution for 1h. DAPI was used to stain the cell nuclei (blue) at a concentration of 1.43µM.

Western blot - Anti-SENP2 antibody (AB58418)
  • WB

Unknown

Western blot - Anti-SENP2 antibody (AB58418)

All lanes:

Western blot - Anti-SENP2 antibody (ab58418) at 1/500 dilution

Lane 1:

MDA-MB-435 cell extract

Lane 2:

MDA-MB-435 cell extract with immunizing peptide

Predicted band size: 68 kDa

Observed band size: 70 kDa

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Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

ICC/IF, WB

applications

Immunogen

Synthetic Peptide within Human SENP2 aa 450 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

Q9HC62

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.4 Preservative: 0.02% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.87% Sodium chloride
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Storage information
Stable for 12 months at -20°C

Supplementary information

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

SENP2 also known as Sentrin/SUMO-specific protease 2 functions as a protease that removes SUMO (Small Ubiquitin-like Modifier) moieties from target proteins. This activity regulates the sumoylation state of proteins affecting their stability activity and localization. SENP2 has a molecular mass of around 63 kDa. It is widely expressed in various tissues including the heart liver and placenta with particularly high levels in these areas suggesting its importance across different biological processes.
Biological function summary

SUMO E3 ligase complexes often include SENP2 as an integral part. It modulates various signaling pathways by targeting transcription factors and other proteins involved in cellular stress response cell division and apoptosis. Through de-sumoylation SENP2 influences the activity of proteins by altering their transcriptional potency nuclear transport or protein degradation rates. SENP2's activity ensures appropriate cellular responses to environmental cues and maintains proper cellular homeostasis by balancing protein modifications.

Pathways

SUMO-related mechanisms like nucleocytoplasmic transport and DNA repair involve SENP2. In these pathways SENP2 interacts with proteins like RanBP2 and PML contributing to cell cycle regulation and maintaining genomic stability. In the hypoxia response pathway SENP2's influence is important for modulating hypoxia-inducible factors (HIFs). These interactions illustrate SENP2’s regulatory roles in adapting cellular function in response to stress and changes in the cellular environment.

SENP2 displays relevance in cancer and cardiovascular disorders. Altered sumoylation activity linked with SENP2 is often observed in certain cancers where it may misregulate transcription factors like p53 and c-Myc. In cardiovascular diseases SENP2 interacts with proteins such as NFATc1 impacting cardiac development and function. These associations highlight SENP2's potential as a therapeutic target where modulation of its activity might offer novel treatment avenues for related diseases.

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 : 11896061, PubMed : 12192048, PubMed : 15296745, PubMed : 20194620, PubMed : 21965678). 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 : 15296745). 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 : 15296745, PubMed : 20194620, PubMed : 21965678). May down-regulate CTNNB1 levels and thereby modulate the Wnt pathway (By similarity). Deconjugates SUMO2 from MTA1 (PubMed : 21965678). Plays a dynamic role in adipogenesis by desumoylating and promoting the stabilization of CEBPB (PubMed : 20194620). Acts as a regulator of the cGAS-STING pathway by catalyzing desumoylation of CGAS and STING1 during the late phase of viral infection (By similarity).
See full target information SENP2

Alternative Names

KIAA1331, SENP2, Sentrin-specific protease 2, Axam2, SMT3-specific isopeptidase 2, Sentrin/SUMO-specific protease SENP2, Smt3ip2

Publications (9)

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

Cell death & disease 15:596 PubMed39152119

2024

Sumo-regulatory SENP2 controls the homeostatic squamous mitosis-differentiation checkpoint.

Applications

Unspecified application

Species

Unspecified reactive species

Jesús Galán-Vidal,Lorena García-Gaipo,Rut Molinuevo,Samantha Dias,Alex Tsoi,Javier Gómez-Román,James T Elder,Helfrid Hochegger,Alberto Gandarillas

Nature communications 12:1812 PubMed33753739

2021

SUMOylation controls the binding of hexokinase 2 to mitochondria and protects against prostate cancer tumorigenesis.

Applications

Unspecified application

Species

Unspecified reactive species

Xun Shangguan,Jianli He,Zehua Ma,Weiwei Zhang,Yiyi Ji,Kai Shen,Zhiying Yue,Wenyu Li,Zhixiang Xin,Quan Zheng,Ying Cao,Jiahua Pan,Baijun Dong,Jinke Cheng,Qi Wang,Wei Xue

PloS one 15:e0242606 PubMed33211757

2020

Zinc deficiency induces abnormal development of the myocardium by promoting SENP5 overexpression.

Applications

Unspecified application

Species

Unspecified reactive species

Xiaoyu Zhang,Cuancuan Wang,Dan Zhao,Xuhong Chen,Chunyan Zhang,Jun Zheng,Xiaozhi Liu

Molecular brain 13:59 PubMed32290845

2020

Forebrain excitatory neuron-specific SENP2 knockout mouse displays hyperactivity, impaired learning and memory, and anxiolytic-like behavior.

Applications

Unspecified application

Species

Unspecified reactive species

Dehua Huang,Huiqing Liu,Aoxue Zhu,Yi Zhou,Yong Li

Experimental and therapeutic medicine 19:1855-1863 PubMed32104241

2020

Expression of SUMO associated proteins in the mouse endometrium is regulated by ovarian hormones throughout the estrous cycle.

Applications

IHC

Species

Mouse

Yi Liu,Xiaofang Ma,Xuhong Chen,Jinsheng Chen,Li Yuan,Lili Li,Yaowu Bai,Xiaozhi Liu

Frontiers in pharmacology 10:1039 PubMed31616295

2019

Saikosaponin-d Inhibits the Hepatoma Cells and Enhances Chemosensitivity Through SENP5-Dependent Inhibition of Gli1 SUMOylation Under Hypoxia.

Applications

Unspecified application

Species

Unspecified reactive species

Chun-Yan Zhang,Zhong-Min Jiang,Xiao-Fang Ma,Yue Li,Xiao-Zhi Liu,Li-Li Li,Wen-Han Wu,Tao Wang

Biochimica et biophysica acta. Biomembranes 1861:1293-1301 PubMed31054272

2019

The SUMO-Specific Protease Senp2 Regulates SUMOylation, Expression and Function of Human Organic Anion Transporter 3.

Applications

Unspecified application

Species

Unspecified reactive species

Haoxun Wang,Guofeng You

Oncotarget 8:70142-70155 PubMed29050267

2017

Reversible regulation of ORC2 SUMOylation by PIAS4 and SENP2.

Applications

Unspecified application

Species

Unspecified reactive species

Ronghua Wang,Fangming Liu,Yongxu Zhao,Dan Wu,Lihan Chen,Edward T H Yeh,Chao Huang

The Journal of biological chemistry 285:28064-75 PubMed20587419

2010

Sumoylation regulates interaction of FOG1 with C-terminal-binding protein (CTBP).

Applications

WB

Species

Human

Jonathan W Snow,Jonghwan Kim,Caroline R Currie,Jian Xu,Stuart H Orkin
View all publications

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