Methanethiol oxidase Antibodies

Methanethiol oxidase (SELENBP1)

Catalyzes the oxidation of methanethiol, an organosulfur compound known to be produced in substantial amounts by gut bacteria (PubMed:29255262). Selenium-binding protein which might be involved in the feeling of reactive xenobiotics from the cytoplasm.

Might be involved in intra-Golgi protein transport (By similarity). .

Gene Information

Human
Gene Name:	SELENBP1
Uniprot:	Q13228
Entrez:	8991

Family

Belongs to:
selenium-binding protein family

Alternative Names

56 kDa selenium-binding protein; hSBP; hSP56; LPSB; SBP; SBP56; selenium binding protein 1; selenium-binding protein 1; SP56FLJ13813

Molecular Weight

Mass (kDA):
52.391 kDA

Genomic Context

Human
Location:	1q21.3
Sequence:	1; NC_000001.11 (151364304..151372725, complement)

Tissue Specificity

Widely expressed. Highly expressed in liver, lung, colon, prostate, kidney and pancreas. In brain, present both in neurons and glia (at protein level). Down-regulated in lung adenocarcinoma, colorectal carcinoma and ovarian cancer. Two-fold up-regulated in brain and blood from schizophrenia patients.

Subcellular Localizations

Nucleus. Cytoplasm, cytosol. Membrane; Peripheral membrane protein. May associate with Golgi membrane (By similarity). May associate with the membrane of autophagosomes (By similarity).

Diseases

• Malignant Neoplasms
• Neoplasms
• Carcinoma
• Adenocarcinoma
• Colorectal Cancer
• Schizophrenia
• Carcinogenesis
• Malignant Tumor Of Colon
• Hypoxia
• Malignant Paraganglionic Neoplasm
• Colorectal Neoplasms
• Colonic Neoplasms
• Malignant Neoplasm Of Prostate

• Stomach Neoplasms
• Neoplasm Metastasis
• Ulcer
• Ovarian Neoplasm
• Fatty Liver
• Psychotic Disorders
• Mental Disorders

Interacting Proteins

• TRIP13

Pathways

• Cell Growth
• Cell Proliferation
• Localization
• Pathogenesis
• Secretion
• Cell Migration
• Cellular Senescence
• Response To Hypoxia
• Proteolysis
• Skin Development
• Demethylation
• Cell Maturation
• Senescence

• Methylation
• Reverse Transcription
• Cell Cycle
• Locomotion
• Protein Folding
• Cell Differentiation
• Wound Healing

PTMs

• Methylation
• Demethylation

• Phosphorylation
• Reduction

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/SELENBP1

Best Uses Of The SELENBP1 Marker

This article provides an overview of SELENBP1, a cell differentiation/maturation marker. It also explains the biological process that SELENBP1 is involved in. We will talk about the most important functions that the SELENBP1 genome performs. It is an essential marker of cell differentiation/maturation in various biological systems. Continue reading to learn more. The body has many functions to the SELENBP1 genetic.

SELENBP1 is a marker of cell differentiation/maturation

Recent studies have shown that serum levels of SELENBP1 are associated with neurologic impairment in patients suffering from traumatic spinal cord injuries. A strong correlation was found between CCL2 and SELENBP1 levels. This suggests a possible link in Se metabolism and immune cell activation. These findings have important implications for the diagnosis, treatment, and regeneration of neurological damage.

The study found that SELENBP1 levels were lower in CRC-derived samples than in a controlled group. RTPCR and immunoblotting revealed that proteins and mRNA were decreased in CRC-cells. However, SELENBP1 gene expression was higher in benign polyps that in tumor cells. NaB treatment increased CEA expression in SW480, SW620 and HT29 cells.

SELENBP1 has been implicated not only in tumorigenesis but also as a potential marker for cancer. It is thought that it is involved in the process of cell differentiation/maturation. Similarly, it has been found to be associated with cancer-related death. It is also known to regulate a number of other genes, including Akt. These findings are still being confirmed by further studies.

SELENBP1 expression is high in normal mucosa. However, it is lower in uterine leiomyoma. SELENBP1 plays a normal biologic function in myometrium. It is absent in gastric carcinoma, which suggests that suppression may occur at a late molecular phase. This could offer insight into gastric carcinogenesis.

Comparing the expression of SELENBP1 among CRC samples with different degrees of differentiation was done. In total, 10 samples of CRC were well differentiated, 14 samples were moderately differentiated, and four were poorly differentiated. Western blot and real-time RT-PCR analysis showed that SELENBP1 expression was significantly different between these three groups of tumors.

The severity of the injury was responsible for the rise in SELENBP1 levels in TSCI patients. Patients with AIS class A, B, and C had the highest levels of SELENBP1 in their serum. This was also true for patients with neurological impairment. However, this correlation was not significant in patients with mild injury or remission.

Although the role of SELENBP1 in cell differentiation/maturation remains unclear, the findings support its role as a potential biomarker for schizophrenia. The protein is involved with Se metabolism, transport, as well as accumulation in various parts of the body. It can also oxidize methanethiol. SELENBP1 is also a potential biomarker of schizophrenia.

Both CC10 & SELENBP1 serve as tumor clonal indicators. These proteins are found in all tumor cells and indicate clonal origin. They are found in normal cells of the lungs, in YFP/CFP tumors in TKO/Motley mice, and clonal lung cancer.

In addition to SELENBP1, the gene also encodes several other proteins that are important for determining the state of cell differentiation/maturation. In some cases, the protein may not be expressed in hematopoiesis but persists in terminally differentiated cells despite being deleted from the genome. For further studies, the role of SELENBP1 in cell differentiation/maturation remains unknown.

In the present study, SELENBP1 was found to be a marker of cell differentiation/maturity in human erythrocytes and megakaryocytes. Both have common bipotent progenitor and differentiation pathways. They also share transcription factor dependency. The overlap between SELENBP1 and FOG16 suggests that these genes are linked.

It is a marker of cell differentiation/maturation

The expression of SELENBP1 was increased in cells at various stages and stages of cell division and maturation, including SW480 (HT29), SW620 (SW620), which are all representative CRC subtypes. The mRNA level for SELENBP1 was also different in these three cell types. Western blot analysis and real-time RTPCR analyses revealed that SELENBP1 levels are significantly higher in SW480, HT29 and SW620 cell types.

SELENBP1 expression was increased in wild-type 3T3-L1 cells during the differentiation/maturation process and significantly lower in the sh86 and sh85 cells. Knockdown efficiency was also observed with the sh86, sh85 cell lines. Adiponectin expression was also suppressed in sh86 and D7 shCtr cells. SELENBP1 could be an endogenous regulator for adipogenesis.

SELENBP1 was also found in serum of patients after cardiac surgery and myocardial infarction. These serum levels were associated with tissue damage and hypoxic stresses. Therefore, SELENBP1 may represent an important marker for cell differentiation/maturation. These results show the potential value of this protein for the diagnosis of various disease states. It is not yet clear if SELENBP1 could have a negative effect on the Se status of your blood.

The study also revealed that circulating levels of SELENBP1 did not correlate with the concentrations of other Se state biomarkers. Their correlation coefficients proved to be low, with patients in both the G0- and G1 group showing opposite results. SELENBP1 and Se are also negatively correlated. Moreover SELENBP1 inversely correlated with Se in both G1 and G0 patients, suggesting that they may have important implications regarding neurodegeneration or regeneration.

Inhibiting lipid accumulation during adipogenesis by knocking down SELENBP1 from 3T3-L1 cell lines, These cells showed lower levels of lipid in comparison to sh86-cell line controls. Similar proliferation rates were observed in sh85 and sh86 cells. SELENBP1 is therefore likely to influence cell proliferation in both mature and undifferentiated adipocytes.

Tumorigenesis and progression is also associated with the upregulation SELENBP1 by cancer cells. SELENBP1 might be a new target in cancer therapies. It is also associated with DNA methylation as well as histone modifications. It is important to remember that DNA methylation patterns at CpG islands have been associated with CRC. Similarly, Pohl et al. Pohl et.al. demonstrated that colon cancer cell lines had hypermethylated SELENBP1 promotors, which inhibited protein synthesis. SELENBP1 expression was also overexpressed in mice, which inhibited tumor growth.

A new study revealed that SELENBP1 is linked to mitochondrial activity. SELENBP1 knockdown cell showed lower activity in mitochondrial respiration, glycolysis, and was able to produce less ATP. These results suggest that SELENBP1 might be a useful biomarker to diagnose schizophrenia. The protein also plays a role in cell division.

SELENBP1 plays a role in differentiation of cancer cells. This protein was found to be differentially expressed within colorectal cancer tissues. It was also found to be associated in CRC tissues with decreased expression of CEA, a differentiation marker. It is possible that SELENBP1 is a marker of cancer differentiation and maturation, but the results have yet to be confirmed.

SELENBP1 is an excellent candidate marker of cell differentiation/maturation. It can be used to identify leukocyte-specific cell types, which are a hallmark in the differentiation process. This protein may also serve as a marker in hematopoiesis. Additionally, it may be found in terminally differentiation cells and may not be subject to sustained transcription. This discovery is a significant advance in our understanding of the function of this protein.

R7E mice with dedifferentiated rods show decreased expression of h2c. However, cells from the other two subtypes show increased levels of MECP2. It is striking to see the differences between these three groups. The dedifferentiated rods show decreased expression of h2c and increased expression of MECP2, which are markers of cell differentiation/maturation.