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- Table of Contents
Facts about NGFI-A-binding protein 1.
.
Human | |
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Gene Name: | NAB1 |
Uniprot: | Q13506 |
Entrez: | 4664 |
Belongs to: |
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NAB family |
EGR1 binding protein 1; EGR-1-binding protein 1; NGFI-A binding protein 1 (EGR1 binding protein 1); NGFI-A-binding protein 1; Transcriptional regulatory protein p54
Mass (kDA):
54.401 kDA
Human | |
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Location: | 2q32.2 |
Sequence: | 2; NC_000002.12 (190648860..190692766) |
Isoform Short is found in myeloid leukemia cell line KG-1.
Nucleus.
Steven Boster, who invented his first product in 1993, earned the nickname "he Who Converts Science in the Lavatory". Over the next several decades, he created dozens of IHC and hundreds of primary antibody products. In the late 90s, he was the head of China's largest antibody catalog company. During the same time, he created a proprietary ELISA platform, PicoKine(tm). PicoKine (tm) ELISA platform utilized trade secrets to deliver high sensitivity ELISA Kits.
Steve Boster's many talents were not the only reason the NAB1 was so versatile. It was used for everything, from writing down his time in the game to putting his name in it. Boster was the child of James Meier and Evelyn Meier. He had a distinguished retail sales career. He was also a U.S. Army Veteran and a Concordia Hall Member in Staunton. Boster is survived and cared for by his two daughters, Crystal Boster (Natosha) and four brothers, Jack Boster (Sandra Blanton) and Lisa Milton (Military Veteran). There are many nieces as well as nephews.
In the genomes of Xenopus oocytes, a consensus pattern that recognizes NAB1 has been identified. NAB1 is an RNA binding translation regulator. FRGY2 recognizes the exact same motif in Xenopus. The black outlines indicate identical positions. The sequence identity levels can be found to the right. The NAB1 protein has two RNA-binding domains, and a CSD at its N terminus.
Many mRNAs conserve the CSDCS like binding domain of NAB1. This indicates that NAB1 does not only exist in LHCBM mRNAs. There are however other mRNAs that have CSDCS-like domains which might functionally overlap with NAB1.
This bone is not functionally useful, but it might be interesting to know its origins. Humans' spinal columns were an unwise modification on the horizontal spine of four-legged relatives. Evolution should add evolutionary inertia to the bone structure for optimal function. As such, humans evolved to enhance this characteristic in order to improve their quality and life. But there is a problem.
In vitro competition with NAB1 has shown that NAB1's role in the expression of light-harvesting RNAs was essential. A HA tagged LHCBM gene construct was created to test the NAB1 proteins ability to bind RNA. It was later identified as HA -LHCBM6 et HA -LHCBM4 through site-directed mutagenesis.
NAB1 has a unique DNA-binding function. The NAB1 gene's location in cytosol is also unique. This demonstrates the importance of NAB1 in the evolution of the genome and cellular structure. It is also important to understand NAB1's evolutionary function in human evolution. However, there is still some disagreement about the function. It is important for us to understand how this gene affects our body's functions.
Using the NAB1 gene model as a template, we first cloned the wild type cDNA into a pQE80L vector. This was transformed into Escherichiacoli strain M15, and 6x His-tagged NAB1 expression. Afterward, we purified the peptide by nickel-nitril-triacetic acid agarose column chromatography. Finally, we used thrombin to examine the NAB1 protein.
Adeno-associated viruses (AAVs) are remarkable templates for gene therapy vector development. These viruses are especially well-suited to rational capsid engineering because they are highly susceptible for retargeting specific cell types. This type of rational design uses short stretches to insert amino acids into exposed regions of the viral capid in the hope that the protein will be displayed on its surface and mediate the retargeting process of the particle to a certain cell type. The AAV2 prototype capsid has been used successfully to display peptides in order to select candidates with the desired tropism in cell cultures and in vivo.
Designer capsids are the result of rational approaches to AAV surfaces engineering. The creation of large, asymmetrical capids was a significant milestone in rational engineering. These advances made it possible to clone AAV genes and manipulate them to express desired transgenes. It was also possible to modify the cap gene. This allowed rational engineering of AAV capsids that have altered functions such as nuclear transport or cellular uptake.
AAV capsids are rationally engineered so that proteins can be targeted with specific functions. These modifications are challenging because large biomolecules or proteins cannot be inserted into capsid proteins without causing significant functional and titer loss. This is a step towards targeting gene therapy by modifying the capsid's surface. The goal is to improve AAV's ability to transduce genes successfully without resistance.
These strategies are possible due to the fact that vectors can be created to control the packaged transgene. These strategies can be further enhanced by combining strategies that enhance control of packaged transgenes, with engineered capsid varieties. Additionally, rational capsid engineering can improve gene delivery strategies. To improve gene delivery efficiency, engineered capsids can be used with synthetic gene switches and other capid design techniques. There are many options.
PMID: 8668170 by Svaren J., et al. NAB2, a corepressor of NGFI-A (Egr-1) and Krox20, is induced by proliferative and differentiative stimuli.
PMID: 21836637 by Garcia-Gutierrez P., et al. The transcription factor Krox20 is an E3 ligase that sumoylates its Nab coregulators.