VRK1 Antibodies

Serine/threonine-protein kinase VRK1 (VRK1)

Serine/threonine kinase involved in Golgi disassembly during the cell cycle: after phosphorylation by PLK3 during mitosis, required to induce Golgi fragmentation. Acts by mediating phosphorylation of downstream target protein.

Phosphorylates'Thr- 18' of p53/TP53 and may thereby prevent the interaction between p53/TP53 and MDM2. Phosphorylates casein and histone H3.

Gene Information

Human
Gene Name:	VRK1
Uniprot:	Q99986
Entrez:	7443

Family

Belongs to:
protein kinase superfamily

Alternative Names

EC 2.7.11.1; MGC117401; MGC138280; MGC142070; PCH1; serine/threonine-protein kinase VRK1; vaccinia related kinase 1; vaccinia virus B1R-related kinase 1; Vaccinia-related kinase 1; VRK1

Molecular Weight

Mass (kDA):
45.476 kDA

Genomic Context

Human
Location:	14q32.2
Sequence:	14; NC_000014.9 (96797382..96881614)

Tissue Specificity

Widely expressed. Highly expressed in fetal liver, testis and thymus.

Subcellular Localizations

Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle. Dispersed throughout the cell but not located on mitotic spindle or chromatids during mitosis.

Diseases

• Neoplasms
• Vaccinia
• Malignant Neoplasms
• Atrophy
• Muscular Atrophy
• Female Infertility
• Leukemia
• Malignant Neoplasm Of Breast
• Infertility
• Carcinoma
• Chromosome Breakage
• Mammary Neoplasms
• Spinal Muscular Atrophy

• Precursor T-cell Lymphoblastic Leukemia-lymphoma
• Sterility
• Muscle Weakness
• Weakness
• Adult T-cell Lymphoma/leukemia
• Lung Neoplasms
• Male Infertility

Interacting Proteins

• ATF2
• AURKB
• COIL
• H2AFX
• JUN

• NBN
• PLK3
• RAN
• RNF8
• SOX2

• TP53
• TP53BP1

Pathways

• Cell Cycle
• Cell Proliferation
• Localization
• Cell Division
• Mitosis
• Dna Replication
• Chromosome Segregation
• Cell Cycle Arrest
• Histone Phosphorylation
• Meiosis
• Transport
• Protein Phosphorylation
• Hyperphosphorylation

• Cell Cycle Phase
• Nuclear Envelope Disassembly
• Translation
• Female Meiosis
• Telomere Maintenance
• Chromatin Organization
• Interphase

PTMs

• Phosphorylation
• Acetylation

• Dephosphorylation
• Ubiquitination

• Reduction

Research Areas

• Core ESC-Like Genes
• Protein Kinase
• Stem Cell Markers

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/VRK1

Best Uses Of The VRK1 Marker From Boster Bio

This article will be about the AntiVRK1 Marker by Boster Bio. In this article we will discuss anti-human antibodies and anti-mouse antibody that react with the VRK1 protein. We will also explain how in-situ RNA hybridization works, and what applications it has for the spastic population.

Anti-VRK1 Signer

There are many biological assays that use the anti-VRK1 marker. It can either be a monoclonal or polyclonal antibody. Boster Bio creates antibodies against rabbit- and mouse strains. This serine/threonine/threonine-protein kinase phosphorylates downstream targets proteins such as p53/TP53 [Thr-18'] and histone He3.

This antibody can recognize cells expressing VRK1 protein. It is a potent inhibitor of p53 mediated downregulation. It also binds with the protein at the site known as p53 promoter. However, it doesn't protect cells from the effects caused by p53. It is therefore crucial to distinguish between PCAF (p300) and PCAF. Boster Bio makes an anti-VRK1 antibody that can detect the presence in the body of a cancerous tumor.

The C/H3 Domain of p300 is responsible for binding transcription factors. This domain is also responsible SV40 large T antigen binding. Mutations in this domain inhibit the effect on the protein, but it retains the gene repressor function. By interfacing with VRK1, p300 inhibits p53 and downregulates VRK1.

This antibody recognizes human, mouse, and rat VRK1. It is a highly effective antiVRK1 marker that can be used in experiments. It can be used in vitro experiments. The boster Bio Anti–VRK1 antibody is compatible with rat, mouse, human and other mammals. It is suitable for the detection of various protein types, including cancer cells, in vitro, and in vivo studies.

In vitro research has shown that VRK2 enhances polyQ protein turnover. The results of this study show that VRK2 expression in HD patients leads to an increase in the levels of soluble Q aggregates. In a filter-trap assay, the nonpathogenic HttQ25-GFP remained diffuse even after VRK2 overexpression. The protein is highly foldable despite the disruption of the TRiC.

Researchers have found that transfected EC109 cells and EC1 cells produce high levels of both VRK1 protein and BANF1 protein in a study where they have determined their protein expression levels. Transfected cells were harvested within 24 hours of transfection and were washed three time in ice-cold PBS. Wuhan Boster Biological Technology, Ltd. extracted the proteins using a RIPA lysis buffer containing PMSF.

Chloroquine inhibits the N-terminus (or degradation) of VRK1 in cells. Chloroquine acts as an inhibitor of the VRK2 genes, which has an impact on the endosome/lysosome path. It also prevents the export of phosphorylated proteins. When it enters cells and is absorbed, chloroquine inactivates VRK2 as well as P53.

VRK1 can be found in many cancer cells, including those in and around the esophageal. The expression of this protein was elevated in ESCC cell lines, which was correlated with clinical characteristics. In addition, cell lines containing the myc epitope were used to investigate the interaction between VRK1 and BANF1. They were treated with small interfering RNA (siRNA) to inhibit VRK1 expression and assessed for changes in their migration and proliferation. This study suggests VRK1 and BANF1 might be potential targets for ESCC target therapy.

Applications for spastic patient

Spastic patients can benefit from cryotherapy, a method in which the body is chilled using a soaking solution. This method reduces spastic resistance to rapid stretching and thereby reduces the spastic reflex. While cryotherapy has many potential benefits, it is important to note that most studies have focused on the dipping or rubbing methods, not continuous cold air therapy. This is an important aspect of spasticity treatment.

A sensitivity analysis was used in order to study the treatment. Three studies were done by the authors. One used botulinumtoxin and one used physiotherapy. All three studies found no significant improvement of spasticity. These studies are not conclusive. Further research is needed to compare botulinum poison with NMES for spastic people.

Spasticity can cause mild stiffness or painful spasms that may affect daily activities. These symptoms can become severe and incapacitating if they are not treated promptly. Untreated spasticity can lead to frozen joints and painful pressure sores on the skin. Untreated spasticity may also cause a person to become unable to perform daily tasks.

Spasticity is a common condition in stroke survivors. It can decrease quality of care, increase caregiver burden, affect patient comfort, and impact patient function. Effective treatment includes non-pharmacological, pharmacological, and pharmacological interventions to increase independence and functional ability of patients with spasticity. There is no single treatment for spasticity. However, effective treatment depends on understanding the causes of spasticity and identifying the best way to relieve them.

Electrical stimulation is an effective method for reducing spasticity in spastic patients. It activates nerves and causes a contraction in a particular muscle group. Patients may find it easier to relax and regain normal neuron activity. Transcutaneous Electrical Neuron Stimulation (TENS), is the name for this technique.

Spasticity in patients with hemiplegic stroke is difficult to quantify. However, electromyographic and biomechanical analyses can be used to measure spasticity in stroke victims. These studies are encouraging, but more research is needed to confirm and refine these methods. The SIS method may be an effective therapy for patients with spasticity.

Vibrational stimulation of DAVS, one of many treatment options for spasticity, is the most promising. Researchers used a clinical protocol to determine which stimulation method was most effective for each patient in the current study. The intervention resulted in decreased spasticity in the upper limbs of hemiplegics. They recruited 36 post-stroke patients at the Kirishima Rehabilitation Centre of Kagoshima University, Japan. All patients were supine for 30 min. Modified Ashworth Scale scores and F-wave parameters were recorded before and after the interventions.

In situ RNA hybridization

The BosterBio VRK1 marker is used for in-situ DNA hybridization. It allows researchers to visualize gene transcription by using a labeled Probe. The probe is designed to hybridize with a specific sequence and detect mRNA. This kit comes with protocols, scientific support and a range of useful tools to make the experiment as simple as possible. The MK1030 marker for in-situ hybridization is highly sensitive and is suitable for oligonucleotide probes that have been intensively conjugated by one or two digoxins.

The Boster Bio VRK1 marker for in-situ hybridization is non-enzymatic and enables resolution of single RNA molecules within a tissue section. To achieve high sensitivity and low probabilities of non-specific hybridization, the method requires at least 20 double-Z probe pairs. The in-situ hybridization protocol takes only 36 hours.

Fluorescence in-situ hybridization is an effective technique for visualizing target DNA sequences. ISH is based on principles of nucleic-acid thermodynamics. Researchers can visualize the target DNA sequence by using complementary nucleic acid. It is also highly sensitive and reproducible.

In-situ hybridization probes can be made from DNA, cDNA, and RNA. They are single or double-stranded and should match the target sequence's base-pair. The target sequence and probe's sequence determine the optimal temperature. Additionally, the target sequence's concentration of guanine and cytosine is important. Non-specific interactions can be removed by adjusting the solution's parameters.

ISH can be used to detect low levels (vRNA, viral DNA) in cells and tissues. As a result, it can guide research into HIV/SIV tissue reservoirs and eradication. ISH has low detection limits and can visualize vRNA in situ. It has also been able to show that BCFs are vital sanctuary sites for this virus thanks to its low-level of sensitivity.