SKP2 Antibodies

S-phase kinase-associated protein 2 (SKP2)

Substrate recognition element of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction and transcription. Degradation of CDKN1B/p27kip also needs CKS1.

Recognizes target proteins ORC1, CDT1, RBL2, KMT2A/MLL1, CDK9, RAG2, FOXO1, UBP43, and likely MYC, TOB1 and TAL1. Degradation of TAL1 also needs STUB1.

Gene Information

Human
Gene Name:	SKP2
Uniprot:	Q13309
Entrez:	6502

Family

Belongs to:
No superfamily

Alternative Names

CDK2/cyclin A-associated protein p45; cyclin A/CDK2-associated protein p45; Cyclin-A/CDK2-associated protein p45; FBL1; F-box protein Skp2; F-box/LRR-repeat protein 1; FBXL1; FBXL1MGC1366; FLB1; p45skp2; Skp2; S-phase kinase-associated protein 2 (p45); S-phase kinase-associated protein 2

Molecular Weight

Mass (kDA):
47.761 kDA

Genomic Context

Human
Location:	5p13.2
Sequence:	5; NC_000005.10 (36152043..36184319)

Subcellular Localizations

Cytoplasm. Nucleus.

Diseases

• Malignant Neoplasms
• Neoplasms
• Carcinoma
• Cell Transformation, Neoplastic
• Neoplasm Metastasis
• Malignant Neoplasm Of Breast
• Retinoblastoma
• Mammary Neoplasms
• Malignant Squamous Cell Neoplasm
• Hyperplasia
• Malignant Neoplasm Of Prostate
• Prostatic Neoplasms
• Malignant Paraganglionic Neoplasm

• Lymphoma
• Adenocarcinoma
• Carcinogenesis
• Malignant Neoplasm Of Lung
• Leukemia
• Growth Arrest
• Liver Neoplasms

Interacting Proteins

• Cdh1
• CDKN1A
• CDKN1B
• CKS1B
• CUL1

• DUSP1
• EP300
• FZR1
• KMT2A
• MYC

• ORC1
• PHB
• RBX1
• SIRT3
• SKP1

Pathways

• Cell Cycle
• Cell Proliferation
• Proteolysis
• S Phase
• Cell Growth
• Cell Cycle Arrest
• Pathogenesis
• G1 Phase
• Rna Interference
• Localization
• Mitosis
• Dna Replication
• Senescence

• Cell Death
• Oncogenesis
• Nuclear Export
• Cell Division
• Cell Migration
• Anaphase
• Gene Silencing

PTMs

• Phosphorylation
• Ubiquitination
• Dephosphorylation
• Cleavage
• Acetylation
• Methylation

• Deacetylation
• Demethylation
• Reduction
• Hydroxylation
• Palmitoylation
• Myristoylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/SKP2

Boster Bio - Best Uses Of The SKP2 Marker

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SKP2 can be oncogenic

Many cancers exhibit an overexpression of SKP2 which is an oncogenic protein. The activation of the AKT pathway triggers SKP2 nucleotranslocation, thereby triggering subsequent consequences of the AKT cascade. This includes ERK-mediated phosphorylation, hexakinase II, stearoyl-coA-desaturase 1, and proteins involved in protein translation and glycolysis.

The overexpression in the liver of SKP2 causes cell cycle progress. It also regulates the turnover of negative regulators of cell cycle. Skp2 aids in cell progression by increasing the ubiquitination p27. Furthermore, p27 is stable in G0/G1 and then becomes unstable after the cell leaves G1. In addition, the protein regulates the abundance of cyclin E and E2F-1 transcription.

Using puromycin-resistant SKP2/H-RasG12V-transfected cells, we tested whether or not SKP2 was oncogenic. The levels of SKP2 were higher in transformed cells however, they did not increase Cdk2 levels. Moreover, SKP2/H-RasG12V-transformed cells had an unusual cell morphology and failed to attach to culture dishes. However, cells expressing E1A/H–RasG12V displayed spindles that were typical.

HCC cells that have nuclear-SKP2 accumulating tend to have elevated p–AKT and p–ERK. In 11.6% of HCC specimens there was p-ERK detected in b-catenin , as well as nuclear SKP2 accumulation. These findings are not in correlation with other features of the clinicopathology. Therefore, SKP2 may be an important marker for HCC.

In mice it has been found that SKP2 is associated with hepatocarcinogenesis. The N-RasV12, which is an oncogenic version of the protein is used to deliver the protein to the liver. It is interesting to note that overexpression of SKP2 in mice did not result in the formation of tumors or cause any other abnormalities. It doesn't mean SKP2 could cause cancer. Let's consider some of the possible causes of hepatocellular carcinoma.

The study revealed that lymphomas expressing high levels Skp2 were associated with lymphomas that had increased p27Kip1 levels. Skp2 expression could be a significant mechanism to regulate the p27Kip1 gene, which may be a factor in malignant transformations of NHL cells. In a subset, however, increased Skp2 levels of protein did not result in an increase in growth. This suggests that Skp2 is a factor in the malignant phenotype, but does not influence cell proliferative capacity.

The significance of SKP2 in lymphomagenesis was proven by studies of mice overexpressing SKP2. Studies of mice that have SKP2 overexpression demonstrated that SKP2 is responsible for the destruction of tumor suppressor protein like Rassf1A, Dusp1, Rassp1A, and p57. Although this has not been proven in humans but a recent study showed that SKP2 stimulates the synthesis of tumor-inducing p27 by the Wingless/Wnt pathway.

The SKP2 protein not only regulates the expression of p27, but also plays a part in the process of transformation. Skp2 stimulates the ubiquitin-mediated degradation of p27, which may lead to the malignant progression and growth of tumors. Studies on human cancers have demonstrated Skp2 to be an protooncogene. Skp2 has been implicated in malignant transformations of primary rodent fibroblasts.

The SKP2 regulates the signaling pathways of p300-p53.

The SKP2 protein blocks the acetylation activity of a crucial cytochrome B subunit called the p53. In doing so, it suppresses p53 activity and its killing of cells. However this mechanism may not work in every cell type. In certain cases, a mutant form of Skp2 may counteract its effects.

Skp2 blocks apoptosis-dependent p53 by weakening the p300/p53 interactions. The role of Skp2 in the signaling pathways of p53 remains unclear. There are however other mechanisms that could be responsible for this paradox. Certain of these mechanisms have been previously discussed. Here, we will discuss some examples. We will look at Skp2's role as a regulator of p53-dependent Apoptosis.

Skp2 binds to the Ch2 and CH3 domains of the protein p300. It has been demonstrated that overexpression of Skp2 blocks the activity of Gal4-p53-fusion proteins and the effect of ectopic expression p53. Additionally, Skp2 deletion is equally effective as an attenuator for p53.

Cancer cells are known for their overexpression of Skp2, an oncogenic protein whose overexpression is linked to the malignancy of certain cancers. Additionally, it regulates the G(1)-S transition and the stability of G(1) regulators, p27, and p53. Skp2 is also implicated in the development of lymphomas. An antibody against SKP2 is a possibility for cancer research.

IKKa and CHK1 regulate p53 via their interactions. Acetylation of K1535/1499. is a crucial p53-related residue, is essential for activation. Complex formation between p300/CBP/p53 is also prevented by reducing IKKa expression. However both proteins could have targets that are similar. If you're looking to know more about how Skp2 regulates the p300-p53 signaling pathways Read on!

This study used siRNAs that were specific for Skp2 (p300) in its analysis. Silencers of Skp2 are available for transfection using Lipofectamine Plus or Lipofectamine 2000. The study employed siRNAs with 25 nM each. To inhibit Skp2 as well as p53, siRNA has to be utilized at a higher level. And this was not enough, since SKP2 knockdown inhibits both p300 as well as p53.

We utilized mouse cell lines to incubate Skp2 mutant cells for 20 hours in 10 mM PonaA, then Nutlin-3 (0.5mg/ml) with mouse cell lines. The cells were then removed at the specified times and the p300 levels were determined by immunoblot analysis. Finally, total lysates were prepared. Quantitative PCR was applied to detect Skp2 expression in a cell-culture sample.

The nucks1 -SKP2-p21/p27Axis integrate mitogenic and DNA damage signalling pathways. It is essential for embryonic development and tissue homoeostasis but unscheduled entry into S phase is associated with oncogenesis. The SKP2-p21/p27 axis functions as a checkpoint for the G1/S transition. Mitogenic stimulation activates SKP2, while DNA damage causes p21/p27 be destroyed. This causes deregulation NUCKS1/p21/p27. The results of cell cycle arrest

The SKP2 signaling pathway is controlled by p53.

Researchers have discovered that the gene SKP2 regulates p53 signalling pathways such as the apoptotic pathway as well as cellular growth. More research is required to determine the precise role of Skp2 in these pathways. Furthermore, Skp2 is required for cellular survival and apoptosis, consequently, more research will be required to determine the protein's function in drug resistance. For now, this gene has been linked with a variety of different cancers.

FoxP3 levels are not inversely related to SKP2 expression in human primary breast cancer cells. FoxP3 regulates Skp2 expression and its increased regulation in breast cancer cells hinders growth. Skp2 may also be linked to other pathways involved in breast cancer. In a study, Zhang et al. Zhang and Zhang. Skp2 levels were increased by FoxP3 downregulation.

The protein SKP2 plays a crucial regulator of DNA damage as a result of oxidative stress. Additionally, it helps limit the apoptosis-inducing effects of the stress of oxidative. Additionally, MAPK upregulates the Skp2-MTh2 protein, which makes cells more resistant to oxidative stress. The Skp2 protein regulates the MTh2 pathway, making them an important regulator mechanism in melanomas.

In addition to being a transcriptional regulatory, Skp2 has an oncogenic role in various cancers. Skp2 inhibition may be beneficial in the treatment of cancer and prevention. The gene also interacts with other signaling pathways, and inactivation of Skp2 will result in increased p53 activity. Skp2 plays a critical role in the development and treatment of human cancer.

A variety of studies have also shown that overexpression of SKP2 hinders the function of PDCD4 and p53. Overexpression of SKP2 in breast cancer may also be a contributing factor to this reduction in. Further studies are needed to determine whether this protein is essential to produce the anti-tumor effects of PPARg. If the gene is important in the prevention of cancer and prevention, then preventing ERK activity would aid in reaching this goal.

Nontransformed cells have lower SKP2 regulation. Recent studies have shown that cells that express FRNK do not block ERK signaling. However, it was demonstrated that activated Akt and Raf do not reverse the FRNK-induced proliferation block. Inactivated FAK signaling could be an alternative mechanism for controlling. These results suggest that Skp2 is responsible for controlling p53 signaling pathways within the body, as well as other cancers.

Skp2 is a key player in the development of cancer however, the mechanisms for post-transcriptional regulation are not clear. In the ovarian cancer cell, the gene has a negative impact on epithelial-mesenchymal transition. The expression of miR-339 in Skp2 is linked to the spread of cancer in ovarian tissue and could assist in stopping cell invasion and migration. In addition to preventing EMT miR-339 also has an impact on the metastasis of cancer in ovarian tissue.