Target Name: HMGA2-AS1
NCBI ID: G100129940
Review Report on HMGA2-AS1 Target / Biomarker Content of Review Report on HMGA2-AS1 Target / Biomarker
HMGA2-AS1
Other Name(s): Uncharacterized protein LOC100129940 | LOC100129940 variant 1 | Uncharacterized protein LOC100129940 (isoform 1) | HMGA2 antisense RNA 1 | Uncharacterized LOC100129940, transcript variant 1 | Protein LOC100129940

HMGA2-AS1: A Potential Drug Target and Biomarker

Hemoglobin (HB) is a protein found in red blood cells that is responsible for carrying oxygen from the lungs to the rest of the body. Hemoglobin is composed of four subunits, alpha, beta, gamma, and delta, which are held together by a single oxygen-carrying molecule called hemoglobin subunit (HSA). One of the subunits of hemoglobin, gamma subunit (HG), has been identified as a potential drug target and biomarker due to its unique structure and function.

The gamma subunit (HG) of hemoglobin is a 24-kDa protein that contains a single transmembrane domain and a cytoplasmic tail. It plays a critical role in the stability and function of hemoglobin, as well as the regulation of cell signaling pathways. HG has been shown to interact with various intracellular signaling molecules, including TGF-beta, NF-kappa-B, and SMAD.

One of the key functions of HG is its role in cell signaling pathways, particularly in the regulation of angiogenesis, which is the process by which new blood vessels are formed. HG has been shown to play a critical role in the regulation of angiogenesis by promoting the migration and proliferation of blood vessels, as well as the formation of new endothelial cells.

In addition to its role in cell signaling pathways, HG has also been shown to play a critical role in the regulation of cellular stress responses. HG has been shown to interact with various stress-responsive molecules, including p62, a protein that is involved in the regulation of cell stress responses, and heat shock protein (HSP)70, which is involved in the regulation of cellular stress responses.

HG has also been shown to play a critical role in the regulation of cellular apoptosis, which is the process by which cells die as a result of various stressors, including those that are caused by diseases such as cancer. HG has been shown to interact with various apoptosis-related molecules, including Bax, a protein that is involved in the regulation of cellular apoptosis, and caspase-3, which is involved in the execution of apoptotic cell death.

Due to its unique structure and function, the gamma subunit (HG) of hemoglobin has been identified as a potential drug target and biomarker. Studies have shown that inhibiting the activity of HG has been effective in a variety of therapeutic applications, including the treatment of cancer, heart disease, and neurological disorders.

In addition to its potential therapeutic applications, HG has also been shown to be a valuable biomarker for a variety of diseases. For example, HG has been shown to be elevated in the blood of patients with various cancers, including breast, lung, and colorectal cancers. Additionally, HG has also been shown to be elevated in the blood of patients with cardiovascular disease, including heart failure and hypertension.

In conclusion, the gamma subunit (HG) of hemoglobin has been identified as a potential drug target and biomarker due to its unique structure and function. HG plays a critical role in the regulation of cell signaling pathways, as well as the regulation of cellular stress responses and apoptosis. Its potential therapeutic applications and use as a biomarker make it an attractive target for future research and development.

Protein Name: HMGA2 Antisense RNA 1

The "HMGA2-AS1 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about HMGA2-AS1 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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HMGB1 | HMGB1P1 | HMGB1P10 | HMGB1P19 | HMGB1P37 | HMGB1P38 | HMGB1P46 | HMGB1P5 | HMGB1P6 | HMGB2 | HMGB2P1 | HMGB3 | HMGB3P1 | HMGB3P14 | HMGB3P15 | HMGB3P19 | HMGB3P2 | HMGB3P22 | HMGB3P24 | HMGB3P27 | HMGB3P30 | HMGB3P6 | HMGB4 | HMGCL | HMGCLL1 | HMGCR | HMGCS1 | HMGCS2 | HMGN1 | HMGN1P16 | HMGN1P30 | HMGN1P37 | HMGN1P8 | HMGN2 | HMGN2P13 | HMGN2P15 | HMGN2P18 | HMGN2P19 | HMGN2P24 | HMGN2P25 | HMGN2P30 | HMGN2P38 | HMGN2P46 | HMGN2P5 | HMGN2P6 | HMGN2P7 | HMGN3 | HMGN3-AS1 | HMGN4 | HMGN5 | HMGXB3 | HMGXB4 | HMHB1 | HMMR | HMOX1 | HMOX2 | HMSD | HMX1 | HMX2 | HNF1A | HNF1A-AS1 | HNF1B | HNF4A | HNF4G | HNF4GP1 | HNMT | HNRNPA0 | HNRNPA1 | HNRNPA1L2 | HNRNPA1L3 | HNRNPA1P10 | HNRNPA1P12 | HNRNPA1P16 | HNRNPA1P2 | HNRNPA1P21 | HNRNPA1P27 | HNRNPA1P33 | HNRNPA1P35 | HNRNPA1P36 | HNRNPA1P39 | HNRNPA1P41 | HNRNPA1P5 | HNRNPA1P51 | HNRNPA1P6 | HNRNPA1P60 | HNRNPA1P7 | HNRNPA1P70 | HNRNPA2B1 | HNRNPA3 | HNRNPA3P1 | HNRNPA3P6 | HNRNPAB | HNRNPC | HNRNPCL1 | HNRNPCL2 | HNRNPCL3 | HNRNPCP1 | HNRNPD | HNRNPDL | HNRNPF