Sulfotransferase 2B1 Antibodies

Sulfotransferase 2B1 (SULT2B1)

Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs and xenobiotic compounds. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also lead to bioactivation to form active metabolites.

Sulfates hydroxysteroids like DHEA. Isoform 1 preferentially sulfonates cholesterol, and isoform 2 avidly sulfonates pregnenolone but not cholesterol.

Gene Information

Human
Gene Name:	SULT2B1
Uniprot:	O00204
Entrez:	6820

Family

Belongs to:
sulfotransferase 1 family

Alternative Names

Alcohol sulfotransferase; Cytosolic Sulfotransferase 2B1; EC 2.8.2; EC 2.8.2.2; HSST2; HSST2sulfotransferase family cytosolic 2B member 1; Hydroxysteroid sulfotransferase 2; ST2B1; Sulfotransferase 2B1; sulfotransferase family, cytosolic, 2B, member 1; SULT2B1

Molecular Weight

Mass (kDA):
41.308 kDA

Genomic Context

Human
Location:	19q13.33
Sequence:	19; NC_000019.10 (48552172..48599427)

Tissue Specificity

Expressed in the stratum granulosum-stratum corneum junction in the skin (at protein level). Expressed highly in placenta, prostate and trachea and lower expression in the small intestine and lung.

Subcellular Localizations

Cytoplasm, cytosol. Microsome. Nucleus. Phosphorylation of Ser-348 is required for translocation to the nucleus.

Diseases

• Malignant Neoplasms
• Malignant Neoplasm Of Breast
• Mammary Neoplasms
• Neoplasms, Hormone-dependent
• Steroid Sulfatase Deficiency Disease
• Choriocarcinoma
• Hyperplasia
• Endometrial Polyp
• Carcinoma
• Neoplasms
• Malignant Neoplasm Of Prostate
• Adenocarcinoma
• Secondary Malignant Neoplasm

• Neurodegenerative Disorders
• Colonic Neoplasms
• Breast Adenocarcinoma
• Endometrial Neoplasms
• Malignant Tumor Of Colon
• Placental Choriocarcinoma
• Breast Diseases

Interacting Proteins

• ACYP2
• ALS2CR12
• PRICKLE3
• SULT1A1
• SULT1B1

Pathways

• Sulfation
• Localization
• Conjugation
• Reverse Transcription
• Transport
• Cell Proliferation
• Fermentation
• Secretion
• Cell Activation
• Regulation Of Cholesterol Homeostasis
• T Cell Activation
• Aging
• Immune Response

• Skin Development
• Sterol Homeostasis
• Platelet Aggregation
• Cellular Localization
• Fibrinolysis
• Lipid Homeostasis
• Cell Growth

PTMs

• Sulphation

• Phosphorylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/SULT2B1

Boster Bio: Best Uses Of The SULT2B1 Marker

The SULT2B1 marker can be used for many applications, from species to special samples. Boster scientists can submit results to receive product credits, and these credits are available to scientists worldwide. This article will provide an overview of the SULT2B1 marker and its relation to prostate cancer. To get started, please download the Boster Bio: Best Uses Of The SULT2B1 Marker guide.

SULT2B1b

SULT2B1b is a fusion protein of human and mouse. The cDNA for the human SULT2B1b gene was generously provided by Dr Richard Weinshilboum and Dr Renee Yew from the Mayo Clinic. The fusion protein was affinity purified on amylose. Transfections were performed in 24-well flasks with 5% CSS cells, and calcitriol was added to the media 6 hours after transfection.

The fusion protein T0901317 inhibits LXR signaling in the liver. T0901317 blocks LXRa signaling and induces hepatocyte regeneration. Thus, upregulation of SULT2B1b might be useful in improving the liver regeneration in hepatic steatosis. Hence, SULT2B1b may play a crucial role in liver regeneration in diseases involving hepatic steatosis.

SULT2B1b is expressed at high levels in the prostate, placenta, and skin. This molecule is closely related to SULT2A1, a founding member of the hydroxysteroid SULT subfamily. It is present in the liver, placenta, and adrenocortical tissue, but is absent in prostate tissues. In addition to prostate cancer, SULT2B1b is expressed in several tissues, including skin, kidney, and placenta.

The synthesis of SUL2B1 involves amplification of a cDNA with the SUL2B1 promoter fused to a luciferase gene and a vitamin D responsive region. The resulting cDNA was sequenced using a primer extension assay. The reverse transcribed cDNA was then used in a sequencing ladder on a 6% gel.

The SULT2B1a1 and SULT2B1b proteins are required for the glucuronidation of prototype substrates. In human hepatocytes, the enzymes are transcriptionally controlled by the PPAR receptor. Similarly, SULT2B1b mediates the glucuronidation of bilirubin. A similar pathway is used to activate SULT2A1 in human hepatocytes.

SULT2B1b correlates with prostate cancer

The expression of the prostate gene SULT2B1b was found to be associated with various stages of prostate cancer, including benign prostate hyperplasia, metastatic disease, and prostate tumorigenesis. Several different methods were used to measure SULT2B1b expression, including immunohistochemistry, immunofluorescence staining, immunoblotting, and real-time polymerase chain reaction.

Expression of SULT2B1b was found to negatively correlate with several TNF-related genes in lymph node-derived CRPC samples. It is associated with death receptor 4 and apoptotic-receptor signaling. Furthermore, SULT2B1b expression is negatively correlated with multiple TNF-related genes, including NFKB1 and TNFSF11.

SULT2B1b promotes CRC cell proliferation, motility, and invasion, a major characteristic of prostate cancer. To study how SULT2B1b correlates with prostate cancer, researchers first used lentiviral vectors containing siRNAs. A siRNA corresponding to SULT2B1b was used as the target gene. In the experiment, cells were transfected with a lentiviral vector containing either siRNA or a negative control (LV-siSCR). The cells were then incubated with the indicated virus at a MOI of 10 and polybrene (8 mg/ml). They were then selected and cultured for three days in medium containing 3g/l of antibiotic.

Interestingly, SULT2B1b expression was found to be low in recurrent prostate cancer samples compared to nonrecurrent samples. The intensity of SULT2B1b staining in the cancerous cells was 0.15 to 1.30, while it was higher in nonrecurrent prostate tumor tissues. Additionally, SULT2B1b expression was also associated with other markers of malignant prostate cancer.

Among ten Chinese men with prostate cancer, SULT2B1b expression was significantly associated with TNM stage and lymph node metastasis. Increased intratumoral SULT2B1b expression was associated with shorter disease-free and disease-specific survival in stage II patients. In addition, knockdown of SULT2B1b inhibits invasion and is associated with a higher risk of recurrence.

Furthermore, SULT2B1b expression was significantly higher in tumor tissue than in adjacent nontumor tissues. Western blot analysis also revealed that SULT2B1b protein levels were increased in CRC tissues. Despite the findings, however, it remains unclear whether SULT2B1b expression is associated with CRC risk. But it is still possible that a genetic test could reveal a link between SULT2B1b expression and prostate cancer risk.

Besides predicting prostate cancer risk, SULT2B1b is associated with apoptosis in prostate cancer. Similarly, a heightened level of TNF in CRPC patients may suppress SULT2B1b expression. If so, SULT2B1b may be a valuable target for treatment of prostate cancer. In addition, low-dose TNF may be able to sensitize prostate cancer cells to TNF.

Moreover, SULT2B1b regulates VEGF-A expression in human tumors. This transcription factor has several consensus TRF-binding sites. Moreover, it is required for tumor angiogenesis. The overexpression of AP2 or SP1 in SULT2B1b-depleted GC cells partially restored HUVEC migration. These results show that SULT2B1b has an important role in prostate cancer progression.

Moreover, the expression of SULT2B1b is correlated with prostate cancer in patients with a high-grade enlargement of the testicles. Although SULT2B1b expression is low in prostate cancer, its loss is significant and affects over 2,000 DE genes. It is important to understand the molecular mechanism of SULT2B1b because it influences multiple pathways.

The data analyzed by cBioPortal shows the frequency of cancerous mutations in TCGA and their types. Enrichr analyzes the network dynamics of dysregulated genes. This analysis can help to identify hub genes that may serve as biomarkers and potential druggable targets in prostate cancer. In addition, mutational landscape and survival analyses can improve our understanding of prostate cancer at a molecular level.

Six1 protein expression was significantly associated with high Gleason scores (8-10) and lower Gleason scores (pN) in prostate cancer. This association was not significant with age, stage, or distant metastasis, and was not found in low-grade or high-grade prostate cancers. The data showed that prostate cancer patients with high Six1 expression had a poor prognostic index and were more likely to die from their disease.