UL16-binding protein 2 Antibodies

UL16-binding protein 2 (ULBP2)

Binds and activates the KLRK1/NKG2D receptor, mediating natural killer cell cytotoxicity. .

Gene Information

Human
Gene Name:	ULBP2
Uniprot:	Q9BZM5
Entrez:	80328

Family

Belongs to:
MHC class I family

Alternative Names

ALCAN-alpha; N2DL2; N2DL-2; NKG2D ligand 2; NKG2DL2; RAET1H; RAET1HNKG2DL2; retinoic acid early transcript 1 H; Retinoic acid early transcript 1H; UL16 binding protein 2; UL16-binding protein 2; ULBP2; ULBP-2

Molecular Weight

Mass (kDA):
27.368 kDA

Genomic Context

Human
Location:	6q25.1
Sequence:	6; NC_000006.12 (149941947..149949235)

Tissue Specificity

Expressed in various types of cancer cell lines and in the fetus, but not in normal tissues.

Subcellular Localizations

Cell membrane; Lipid-anchor, GPI-anchor. Endoplasmic reticulum. Secreted. In CMV-infected fibroblasts, detected in the endoplasmic reticulum/cis-Golgi.

Diseases

• Neoplasms
• Malignant Neoplasms
• Carcinoma
• Leukemia
• Cytomegalovirus Infections
• Malignant Paraganglionic Neoplasm
• Melanoma
• Tumor Escape
• Neoplasm Metastasis
• Myeloid Leukemia
• Ovarian Neoplasm
• Leukemia, Myelocytic, Acute

• Infective Disorder
• Lymphoma
• Lung Neoplasms
• Hiv Infections
• Immunologic Deficiency Syndromes
• Liver Carcinoma
• Liver Diseases

Interacting Proteins

• KLRK1

Pathways

• Immune Response
• Cytolysis
• Cell Activation
• Cell Recognition
• Secretion
• Cell Proliferation
• Transport
• Cell Cycle
• Innate Immune Response
• Exocytosis
• Cell Killing
• Senescence
• Methylation

• Cell Death
• Cell Growth
• Rna Interference
• Lymphocyte Activation
• Cell Adhesion
• Gene Silencing
• Chemokine Production

PTMs

• Cleavage
• Phosphorylation
• Methylation

• Demethylation
• Glycosylation
• Gpi Anchoring

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/ULBP2

Best Uses Of The ULBP2 Marker

Antitumor Immunity is a powerful tool to fight cancer. The ULBP2Marker is a powerful monoclonal anti-cancer antibody. It can be used in many different ways, including to identify tumor cells and to boost immune responses in human bodies. The ULBP2 protein is a molecule expressed on cancer cells. The immune system can target this protein to stop tumor cells growing by targeting it.

Steven Boster

Steve Boster passed away on Sunday, June 26, 2022. His passing was not unexpected. Boster had been fighting COVID-19 for years. He was a long-time sales manager and was a member Concordia Hall, Staunton, VA. He is survived by Nina Mae, his two daughters Natosha and Crystal Peck, 6 grandchildren, and 4 brothers - Jack Boster (and Sandra Blanton). He has a sister, Lisa Milton and many nieces and nephews.

High-affinity primary antibodies

To identify ULBP2, high affinity primary antibody were developed by labelling a protein on the cell surface with sulfo–NHS–biotin. This label is incapable of crossing the plasma membrane and binds to ULBP2 at the surface. Western blotting was used to analyze the immunoprecipitated prot. Control immunoprecipitations (actin) showed that biotin marking was cell-surface-specific because an anti-actin antibodies detected a biotin containing protein. EndoglycosidaseH, which is an enzyme that cleaves and digests proteins, was used to digest the biotin-containing protein.

A high-affinity primary antibody is defined by the affinity and specificity of binding to an antigen. This is usually measured with the equilibrium disociation constant (KD), a measure of bimolecular affinity. As affinity binding is reversible, the rate of reaction is proportional to the concentrations of the reactants. The rate at which reactants separate is equal their rate of dissociation from their component molecules. KD values are measured at the rate at which the reactants react to the antigen. The higher this value, the greater the affinity.

Another characteristic of ULBP2 includes the fact that it attaches to the plasma membrane via a transmembrane. This protein is found in wt cells in the upper spectrum, which corresponds the mature protein. The SDS/PAGE will show that the immature ULBP2 is more mobile than the mature protein. This makes it important to create high-affinity primary antibodies by using this marker.

Molecular analysis with s-ULBP2 was conducted using heat-induced eptope retrieval as well as the ULBP2 indicator. The ULBP-2/5/6 antibodies were detected in paraffin-embedded tissue samples. This was done to assess their specificity and sensitivity. Abcam produced antihuman monoclonal antibodies that had a KD at 10. The corresponding sulBP2 or sulBP markers were compared using DMi8.

ULBP2 Marker

The ULBP2 marker can be used to diagnose and prognostize lung cancer. It is found in the serum of patients suffering from lung cancer. Recent studies revealed that the soluble ULBP2 protein was found in patients with lung disease. Its proteolytic site will need to be further investigated. The ULBP2 marker can be used as a diagnostic and prognostic tool.

Their case-control group has a higher serum sULBP2 level than cancer patients. These patients have a worse prognosis because of their sULBP2-related status. This observation suggests that patients with higher sULBP2 levels have a poorer prognosis. Further research is needed to determine the role of this marker when diagnosing lung cancer. Its sensitivity should be measured before it is used in clinical trials.

An immunosensor is another important biomarker that can be used to detect PC. As a PC biomarker, the ULBP2 marker makes a great candidate. It is a simple, reliable and affordable biosensor. The researchers developed a zinc oxide nanoparticle-based immunosensor and evaluated the sensitivity, linearity, and optimal measuring frequency using this method. The immunosensors can be used for a wide range applications if they are successful.

Another method of detecting the protein is by studying the release of exosomes from cancer cells. The ULBP2 marker can be released by tumor cells in exosomes. Cells that express the protein produce the soluble ULBP2 marker. The primary source of ULBP3 is the soluble protein forms. The electron microscopy allows for the analysis of the soluble form.

Antitumor immune response in vivo

This study demonstrates that murine splenic NK cytoplasm can activate antitumor immune mechanisms to kill ULBP tumor cells. Freshly isolated NK Cells are capable of killing ULBP-expressing tumour cells in vitro. They are not like NK cell cultures in IL-15. However, it is not clear how these NK-cells induce antitumor immune response in vivo.

To test this hypothesis, the researchers created RMA and EL4 tumor cell lines that express ULBP. These clones were created by retroviral gene transfer. The mock-transduced knockout clones could be identified using reverse transcriptionPCR. To confirm RAE-1b expression, the clones were stained using an anti-ULBP antibody as well as an anti-mouse IgGPE antibody. These clones were further analyzed with flow cytometry.

The ULBP2 mark has been shown to increase tumor-specific T cells, which can indicate that cancer is progressing. When paired with anti-CD45 antibodies, the tumor immune response can be monitored and assessed. The graph below shows the results. To calculate the amount IL-15 in tumor tissue, it is necessary that the supernatants for the two groups contain the same concentrations.

ULBP2-aCEA inhibits cancer growth in mice. EL4 cell lines expressing ULBP1 & ULBP2 have been partially rejected. IL-15 also boosted EL4 cells expressing ULBP3 & ULBP2. These results are preliminary. The ULBP2-aCEA therapy must be tested in a clinical setting.

Other proteins that can be quantified using ELISA

ELISA is a quantitative method that measures various proteins. The test involves binding an Antigen to a Solid Surface using an Enzyme and then detecting that reaction. The resulting color or fluorescence is then recorded. The absorbance of each well is then measured with a microplate scanner. The concentration of each enzyme or protein in each well determines its absorbance. However, the exact process is not well understood.

ELISA assays on 96-well plates have a higher throughput rate than Western blots. They can detect native protein and detect interactions that require intact three dimensional structures. While the assay is highly quantitative, it can also give false positives due to cross-reactivity. Its high throughput makes the assay useful for studies on binding competition between protein. In the case of coeliac disease, ELISA is one of the few methods that can be used in clinical practice to detect gluten intolerance.

A new HistoELISA technique was also developed to measure target protein concentrations within tissues and cells. This involves identifying target regions and applying peroxide substrata to them. Then, the dye's optical densities are measured. The results from the paired comparisons showed that IPRM measurements were slightly higher in correlation to ELISA measurements (r = 0.93).

There are several benefits to other proteins quantified with ELISA. They are simple to use. In most cases, they can be used to identify specific proteins. ELISA tests have a higher sensitivity than other methods. It is fast and accurate as well, and it is often quicker than other methods. It is highly recommended that you use the ELISA method for clinical trials.