PRKRA Antibodies

Interferon-inducible double-stranded RNA-dependent protein kinase activator A (PRKRA)

Activates EIF2AK2/PKR in the absence of double-stranded RNA (dsRNA), resulting in phosphorylation of EIF2S1/EFI2-alpha and inhibition of translation and induction of apoptosis. Required for siRNA production by DICER1 and for following siRNA-mediated post- transcriptional gene silencing.

Doesn't seem to be required for processing of pre-miRNA to miRNA by DICER1. Promotes UBC9-p53/TP53 association and sumoylation and phosphorylation of p53/TP53 at'Lys-386' in'Ser-392' respectively and enhances its activity at a EIF2AK2/PKR-dependent manner (By similarity).

Gene Information

Human
Gene Name:	PRKRA
Uniprot:	O75569
Entrez:	8575

Family

Belongs to:
PRKRA family

Alternative Names

DYT16; DYT16interferon-inducible double stranded RNA-dependent activator; HSD14; PACT; PACTPKR-associating protein X; PKR-associated protein X; PKR-Associating Protein X; PRKRA; protein kinase, interferon-inducible double stranded RNA dependent activator; RAX; RAXHSD14

Molecular Weight

Mass (kDA):
34.404 kDA

Genomic Context

Human
Location:	2q31.2
Sequence:	2; NC_000002.12 (178431414..178451175, complement)

Subcellular Localizations

Cytoplasm, perinuclear region. Cytoplasm.

Diseases

• Dystonia Disorders
• Virus Diseases
• Neoplasms
• Secondary Parkinson Disease
• Dystonia, Primary
• Generalized Dystonia
• Malignant Neoplasms
• Congenital Small Ears
• Physiological Stress
• Familial Dystonia
• Movement Disorders
• Immunologic Deficiency Syndromes

• Pituitary Diseases
• Influenza
• Infective Disorder
• Carcinoma
• Lupus Erythematosus, Systemic
• Hereditary Diseases
• Neurodegenerative Disorders

Interacting Proteins

• AGO2
• DDX58
• DICER1
• EIF2AK2
• LYAR

• NKRF
• TARBP2
• ZMAT3

Pathways

• Translation
• Rna Interference
• Cell Cycle
• Cell Proliferation
• Mitosis
• Gene Silencing
• Interphase
• Localization
• Cell Death
• Pathogenesis
• Transport
• Cell Differentiation
• Mrna Processing

• Response To Stress
• Regulation Of Cell Proliferation
• Programmed Cell Death
• Immune Response
• Platelet Activation
• Type I Interferon Production
• Cell Cycle Arrest

PTMs

• Phosphorylation
• Cleavage

• Sumoylation
• Biotinylation

• Ubiquitination

Research Areas

• Epigenetics

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

Boster Bio - Best Uses Of The PRKRA Marker

High-affinity primary antibodies are the foundation for research, and Boster Bio offers several of them. These antibodies are cited throughout the scientific community and have been validated in Western Blotting, Immunohistochemistry, and ELISA. In addition, Boster provides highly specific, multitargeted antisera that specifically target the PRKRA Marker. Find out more about Boster’s PRKRA Primary Antibodies.

Boster's high affinity primary antibodies

Boster is the right choice if you are searching for an antibody with high affinity against PRKRA. These antibodies have been validated in Western Blotting, Immunohistochemistry, and ELISA, making them an excellent choice for research. They have excellent specificity and are highly cited in scientific literature. They are also guaranteed to not cross-react with any other antibodies because they use the PRKRA marker for their internal control.

Boster high affinity primary antibodies are highly specific epitopes of human PRKRA and are used to detect them. Secondary antibodies may also bind to these epitopes, resulting in cross-reactivity and a nonspecific signal. Dual antibodies require additional incubation because of these limitations. They are sensitive and require more sensitivity optimization.

Although high affinity primary antibodies are desirable, they're not always the most practical. Their high affinity can make it difficult for elution, which can lead to costly and potentially dangerous methods. High-affinity primary antibodies from Boster use the PRKRA marker, and PRKRA–G, which is a highly specific agent. It is easy to see how boster has a competitive advantage.

Traditional mIHC depends on antibodies raised from different species and isotypes. The reactivity for primary antibodies in tissue-based experiments is therefore limited to three markers. Furthermore, to use fluorescent mIHC, primary antibodies should be raised in different species and isotypes, and they may require a chromatophore. But for the most accurate results, fluorescent mIHC uses three markers.

His research

His research on PRKRA Marker has revealed that it is likely act as an element within the nuageRNAsilence system. This includes ectoplasmic specificization and tubulobulbar Complexes of Sertoli Cells, which attach the head late spermatids. PRKRA may also play an important role in regulation of spermatogenesis, in addition to its role as an ectoplasmic specialist.

The PRKRA protein, which is involved the cell's response in stress response, makes the PACT Protein. It activates another protein, PKR. This, in turn, inhibits the eIF2alpha (eIF2a), protein and reduces the cell's ability to produce proteins. PACT's function is critical for cell survival. A defect could cause the cell’s self-destruct.

He found that the 36kDa protein was found in all cell fractions with comparable amounts and that the microsomal fraction contained the highest amount of the 30kDa protein. Additionally, his research on the PRKRA Marker revealed that the rat and mouse testis exhibited similar PRKRA staining patterns. This was especially surprising considering that the mice testis had been made by a manufacturer.

In step seven, the PRKRA Marker in the cytoplasm was found in spermatocytes. Interestingly, the gene's function was limited to round spermatids, and DDX4 could only be detected in the early stages. The ISPG of pachytene-spermatocytes at stage II showed a variety of staining patterns. Some were positive for both DDX4 but others were negative. These results suggest that the nuage structures dynamically reproduce fission and/or fusion.

Furthermore, elevated inflammation may be caused by the increased interaction of PRKRA with EIF2AK2. This, in turn, may contribute to a poor prognosis for HBV-related HCC. This research is currently the only one of its kind to identify the PRKRA Marker. There are no clinical studies that have examined the relationship between PRKRA, EIF2AK2 and HBV-positive patients.