SENP1 Antibodies

Sentrin-specific protease 1 (SENP1)

Protease which catalyzes two essential functions in the SUMO pathway (PubMed:10652325, PubMed:15199155, PubMed:16253240, PubMed:16553580, PubMed:21829689, PubMed:21965678, PubMed:23160374, PubMed:24943844, PubMed:25406032, PubMed:29506078). The first is the hydrolysis of an alpha-linked peptide bond in the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins.

The second is that 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. Deconjugates SUMO1 from HIPK2 (PubMed:16253240).

Gene Information

Human
Gene Name:	SENP1
Uniprot:	Q9P0U3
Entrez:	29843

Family

Belongs to:
peptidase C48 family

Alternative Names

EC 3.4.22; EC 3.4.22.-; SENP1; Sentrin/SUMO-specific protease SENP1; sentrin-specific protease 1; SUMO1/sentrin specific peptidase 1; SUMO1/sentrin specific protease 1; SuPr-2

Molecular Weight

Mass (kDA):
73.481 kDA

Genomic Context

Human
Location:	12q13.11
Sequence:	12; NC_000012.12 (48042893..48106308, complement)

Tissue Specificity

Highly expressed in testis. Expressed at lower levels in thymus, pancreas, spleen, liver, ovary and small intestine.

Subcellular Localizations

Nucleus. Cytoplasm. Shuttles between cytoplasm and nucleus.

Diseases

• Malignant Neoplasms
• Neoplasms
• Hypoxia
• Malignant Neoplasm Of Prostate
• Leukemia
• Acute Promyelocytic Leukemia
• Prostatic Neoplasms
• Tumor Angiogenesis
• Carcinoma
• Cell Transformation, Neoplastic
• Physiological Stress
• Rheumatoid Arthritis
• Prostatic Intraepithelial Neoplasias

• Arthritis
• Intraepithelial Neoplasia
• Malignant Tumor Of Colon
• Genotoxic Stress
• Ataxia
• Pathologic Neovascularization
• Ataxia Telangiectasia

Interacting Proteins

• SUMO1
• SUMO2

Pathways

• Conjugation
• Localization
• Cell Cycle
• Protein Sumoylation
• Pathogenesis
• Cell Death
• Cell Growth
• Angiogenesis
• Oncogenesis
• Cell Proliferation
• Response To Stress
• Transport
• Proteolysis

• Nuclear Import
• Insulin Secretion
• Response To Hypoxia
• Nucleocytoplasmic Transport
• Rna Interference
• Cellular Response To Hypoxia
• Secretion

PTMs

• Sumoylation
• Phosphorylation
• Ubiquitination
• Cleavage
• Acetylation

• Deacetylation
• Dephosphorylation
• Oxidation
• Methylation
• Ribosylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/SENP1

Best Uses Of The SENP1 Marker

A number of biological assays use antibodies to detect the SENP1 protein. These antibodies may be monoclonal or polyclonal. Boster Bio uses mouse and rabbit as models for development of its SENP1 antibodies. Sentrin-specific protease catalyzes two essential functions in the SUMO pathway. It hydrolyzes the alpha-linked peptide bond at the C-terminus of SUMO propeptides.

SUMOylation is a critical step in cell cycle progression

SUMOylation is a process whereby cellular proteins are covalently conjugated to a SUMO protein. In budding yeast, as many as 300 proteins are considered SUMO targets. The process controls multiple events, including transcription, DNA repair, recombination, and mitotic chromosome segregation. Here, we focus on three classes of SUMO targets and their roles in mitosis.

Although the exact molecular mechanisms of SUMOylation are still unknown, there are several mechanisms that may govern its function. SUMOylation may direct the localization of target proteins, change protein-protein interactions, or select targets for ubiquitin-mediated degradation. In addition, the process may coordinate mitotic processes. Thus, SUMOylation plays a critical role in cell cycle progression.

SUMOylation is essential for the survival and proliferation of cells. It is a crucial step in cell cycle progression and is controlled by the protein Myc. In B cells, Myc coordinates the expression of the SUMOylation genes. It is thought that Myc controls cell growth and metabolism. By inhibiting the activity of Myc, SUMOylation is upregulated.

SUMOylation targets that are involved in mitotic cell cycle progression include the Cohesin complex and the Condensin complex. The Condensin complex is composed of structural maintenance proteins. The SMC family consists of SMC proteins that form rod-shaped structures through antiparallel coiled-coil interactions. The SMC2p and SMC4p form heterodimers in specific combinations and are critical for maintaining the condensed structure of mitotic chromosomes.

Myc is responsible for enhancing SUMOylation in B-cell lymphomas. In addition to increasing the expression of SUMO pathway genes, Myc also acts as a transcription activator, triggering apoptosis and cell-cycle arrest. Targeting Myc-driven lymphomas through SUMO inhibition might be an attractive strategy for eradicating these tumors.

SUMOylation regulates several biological processes, including transcription, hypoxia response, and DNA damage response. Therefore, SUMOylation is crucial for cell cycle progression. Besides regulating cell cycle, SUMOylation is important in a wide variety of other biological functions. Further, SUMOylation is required for gene expression and DNA repair. It is essential for the cell cycle and the development of the chromosomes.

SENP3 is a key node for integrating M phase entry with spindle assembly in mouse oocytes

Our results show that SENP3 is essential for integrating M phase entry with spindles assembly in mouse oocytes. In the present study, we found that SENP3 knockdown impairs the GVBD process. We also found that more than 50% of oocytes remain at the GV-stage after 14 hours of culture.

We analyzed the interactions between SUMO-2/3 and SENP3 during meiotic maturation in oocytes. As SENP3 is a SUMO-specific protease, it preferentially binds SUMO-2/3 and SUMO-132. The knockdown of SENP3 resulted in a reduction in SUMO-2/3 conjugates worldwide. Although SENP3 knockdown did not impair the localization of SUMO-2/3, it impeded SUMO-2/3 maturation in mouse oocytes.

We also found that knockdown of SENP3 impaired the initiation of meiosis. In addition, the knockdown of SENP3 influenced Aurora A expression, which is crucial for MTOC localization and spindle dynamics. Furthermore, SENP3 RNAi decreased SUMO-2/3 conjugates but not SUMO-1. Therefore, SENP3 may have other physiological functions, which we have not yet identified.

Furthermore, it is thought that SENP3 is essential for the morphogenesis of the mouse oocyte. We previously reported that Aurora A, another MTOC-binding protein, co-localized with spindles in control mice, while SENP3 knockdown disrupted Bora's localization at the spindle poles. This suggests that SENP3 is important for the assembly of spindles dictated by g-tubulin.

In addition to this role, the spindle apparatus also plays a critical role in chromosome segregation. Molecular mechanisms that coordinate spindle morphogenesis are orchestrated by proteins called Microtubule Organizing Centers or (MOCs) and Nucleators. The segregation of homologous chromosomes is required for an euploid egg.

To confirm the findings, we used rabbit anti-SENP3 antibody, sheep polyclonal anti-SUMO-1, goat anti-G-tubulin, and goat anti-rabbit IgG. In addition, we used non-immunized mouse or rabbit IgG to serve as negative controls. After blocking the membranes, we used rabbit or mouse anti-SUMO-1 and rabbit anti-SUMO-2/3 antibodies as primary antibodies.

SENP3 antibodies are used in biological assays

SENP3 is an important mediator of mild oxidative stress-induced cell proliferation and regulates the SUMOylation status of PML. Several primary human cancers exhibit over-expression of SENP3, including colon adenocarcinoma. Conversely, cells from normal epithelial tissue exhibit hypo-SUMOylation of PML. This finding points to a possible link between the two proteins.

The SENP3 constructs were prepared as previously described (8). The RGS-His (RH) tagged PMLs encode PML isoform IV. The HA-tagged PML mutant construct lacked all three SUMOylation sites. Site-directed mutagenesis was used to make these constructs. Using these constructs, siRNA-insensitive PMLs were generated using cloned HA-PML WT.

SENP3 is a redox sensor that participates in an adaptive response to oxidative stress. Using SENP3 antibodies, we were able to detect SUMO2/3-containing proteins in PML under mild oxidative stress. Moreover, SENP3 can deconjugate SUMO2/3 from proteins and p300. The protein is involved in many physiological processes including aging, oxidative stress and inflammation.

The protein levels of SENP3 increased with exposure to H2O2. When cells were exposed to low doses of H2O2, identical levels of H2O2 promoted cell proliferation over one day. The inclusion of cyclinD1 and BrdUrdUrd confirmed this process. Knockdown of SENP3 inhibited basal cell proliferation and blocked H2O2-mediated cell proliferation.

Boster Bio SENP3 antibodies are used for various purposes. Its catalog number is A04474Y24. The anti-SENP3 antibodies have been validated in IHC, ICC, and ELISA. These antibodies are ideal for biomedical applications in research and development. They are available for purchase through tebu-bio and are suitable for research and development.

The SENP3 protein is involved in a complex process known as de-SUMOylation. In the presence of SENP3, PML bodies are deconjugated resulting in increased cell proliferation. For further analysis, the SENP3 mutant was incubated with 10 mm H2O2 for 6 h. Cells were then stained with propidium iodide to detect cell cycle.

SENP3 is a modulator of cell cycle progression

You have probably heard about SENP3 (serinephrine nitrate polypeptide), but what exactly is it? This protein is responsible for regulating cell cycle progression. It is also involved in cell signaling. This protein is essential to a variety of processes, from metabolism to reproduction. Boster Bio's SENP3 is a modulator of cell cycle progression antibody is a unique solution for the problem.