ALDH6A1 Antibodies

Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial (ALDH6A1)

Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA.

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Gene Information

Human
Gene Name:	ALDH6A1
Uniprot:	Q02252
Entrez:	4329

Family

Belongs to:
aldehyde dehydrogenase family

Alternative Names

aldehyde dehydrogenase 6 family, member A1; Aldehyde dehydrogenase family 6 member A1; EC 1.2.1.18; EC 1.2.1.27; Malonate-semialdehyde dehydrogenase [acylating]; malonate-semialdehyde dehydrogenase; methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial; MGC40271; MMSADHA; MMSDHmitochondrial acylating methylmalonate-semialdehyde dehydrogenase

Molecular Weight

Mass (kDA):
57.84 kDA

Genomic Context

Human
Location:	14q24.3
Sequence:	14; NC_000014.9 (74056847..74084453, complement)

Subcellular Localizations

Mitochondrion.

Diseases

• Developmental Delay (disorder)
• Carcinoma
• Malignant Neoplasms
• Abnormal Behavior
• Succinate-semialdehyde Dehydrogenase Deficiency
• Malignant Neoplasm Of Kidney
• Liver Carcinoma
• Proline Dehydrogenase Deficiency
• Kidney Neoplasm
• Disorder Characterized By Fever
• Metabolic Diseases

• Neoplasms
• Renal Cell Carcinoma
• Genetic Diseases, Inborn
• Liver Neoplasms
• Sjogren-larsson Syndrome

Pathways

• Cell Proliferation
• Aging
• Rna Interference

PTMs

• Acetylation

• Phosphoprotein

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/ALDH6A1

Best Uses Of The ALDH6A1 Marker

If you're looking for a new gene marker for your research project, read this Boster bio to learn more about Steven Boster's background and career. Boster has high affinity primary antibodies that are known for their outstanding quality, high-citation rates, and exceptional quality. They're endorsed by the research community and have been validated for use in Western Blotting, Immunohistochemistry, and ELISA.

Historiography

ALDHs, a group of enzymes, oxidize a variety od organic compounds to make carboxylic acid. These enzymes perform a variety functions in the body, and they contribute to a wide variety of biological processes including detoxification and biosynthesis. They play a variety of roles in metabolism, including membrane anchorage, antioxidant function and structural and regulatory mechanism. While the majority of ALDHs are monomeric, some contain multifunctional domains.

ALDH6A1 displays transhierarchical structural similarities to ALDH2, with the nicotinamide portion mimicking the structure of the bovine enzyme. The ALDH6A1 protein contains a pyrophosphate moiety that makes close contact with the first b-a-b-a-b loop. It shares the same amino acid composition as aldh2 and includes the Rossmann fold.

The sequence of the C-terminal extensions and N-terminal residues will determine the structure of ALDHs. The tetramerization-stabilizing structure of ALDH6A1 is dependent on the presence of two dimers of ALDH6A1. ALDH2 is ALDH6A1's opposing dimer.

Glu268, an amino acids that is very conserved, is involved in the catalysis. Glu268 is involved in the formation NAD. It provides the thioester-carbon with a water molecule. Lys192 is less important because Glu399, which is conserved, is involved in binding NAD. It is bound the nicotinamide Ring and appears to move in catalysis.

ALDH enzymes, which are essential for cell death, play an important role in maintaining health and viability. ALDH-related diseases are caused by mutations, catalytic knockout and structural disruption. Understanding the molecular foundation of these diseases and their therapeutic potential is crucial for pathophysiology. ALDH disease is currently being studied primarily in terms of its phenotype and not its molecular basis.

Historial career

Boster's Historial career stretched over almost three centuries, and began in the twelfth. His most notable work is on the American Revolution. Historiography is a study of the past. It is an important part to the humanities. However, historians are also required to write history. Boster's Historial work included both research and teaching. The career of a historian can lead to many different jobs.

Biological applications

The ALDH6A1 mitochondrial enzyme is responsible for the irreversible oxidative descarboxylation malonate semialdehydes. Previous studies have shown that ALDh2 is significantly associated with lymphatic infiltration and bone metastasis in PCa. Overexpression of ALDH6A1 has been linked to epithelial tumor cells prognosis.

ALDH6A1 includes five distinct steps for its catalysis. The first step involves activating NAD and then deprotonation. The second step is the hydrolysis of a Thioester. Regeneration of the enzyme is the last step. This requires NAD(P) to be bound.

ALDH6A1's cofactor-binding domain is made up of two subunits, the monomer and dimer. The dimeric ALDh2 variant is the most popular, followed closely by the tetrameric. It is a dimer made up of two monomers. The nicotinamide part is located at the 5A shift. The pyrophosphate moiety is present in the tetrameric tetrameric variant.

The ALDH6A1 genes are part of the ALDH enzyme family that detoxifies a variety, including aldehydes. It is also required to synthesize retinoic acids and other molecular regulators that regulate cellular function. ALDH is now considered a marker for stem cell status due to growing evidence that it regulates cell functions including self-renewal. expansion. differentiation and resistance to drugs.

This enzyme is involved in metabolic programming in ccRCC. ALDH6A1 gene expression has been suggested as a therapeutic target for IR of T2DM. The gene also plays a role in immune inflammation and metabolic pathways. This suggests that the ALDH6A1 gene could be a promising candidate to develop new therapies. However, this hypothesis has not been supported by clinical trials.

High-affinity primary antibodies

High-affinity primary antibodies using the ALH6A1 marker have been successfully developed to identify human hematopoietic stem cells (SCs) in cancer. These cells show a marked expansion after treatment with ALDh2 inhibitors, suggesting that overexpression of ALDh2A1 is a critical regulator of SC function. Furthermore, it may be the most important determinant of ALDH activity in SCs from normal tissues. ALDh2A1 has also been implicated with breast cancer. It may play a critical role in the proliferation and differentiation of cancer cells.

One limitation of high-affinity primary antibodies using the ALDh2A1 marker is that they do not detect all cell types. Some studies have shown that ALDh2A1 overexpression is not associated with prognosis for cancer. Thus, in order to assess whether this marker can serve as an accurate biomarker for esophageal cancer, more research is needed.

ALDh2ATI is a gene that encodes an enzyme which activates the ALDH6A1 protein. This enzyme is involved in many different processes, including ATP manufacturing. When the enzyme is activated, it may be toxic to the cells, which may lead to an immune response. CSCs and cells expressing the ALDh2ATI gene are high in ovarian cancer cells. An increase in ALDh2ATI gene levels may indicate malignant cells.

ALDH genes can be found in many cells and are widely distributed in nature. They can be found in bacteria and yeast, as well as animals and plants. ALDH proteins are part of the ALDH superfamily, an enzyme family with distinct chromosomal sites and gene organisation. Furthermore, they are important in the oxidative metabolism of dopamine and norepinephrine.