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Brand: ProteoGenix

Recombinant Human ALKBH7 Protein, N-His

Host species:
Escherichia coli (E.coli)
Origin species:
Human
Molecular weight:
25.36 kDa

329.00

100ug + 329 loyalty points
Ser16–Cys221
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Recombinant Human ALKBH7 Protein, N-His

Recombinant Human ALKBH7 Protein, N-His

Product name Recombinant Human ALKBH7 Protein, N-His
Origin species Human
Expression system Prokaryotic expression
Molecular weight 25.36 kDa
Buffer Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Delivery condition Dry Ice
Delivery lead time in business days 3-5 days if in stock; 3-5 weeks if production needed
Storage condition 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
Brand ProteoGenix
Host species Escherichia coli (E.coli)
Fragment Type Ser16-Cys221
Aliases /Synonyms Spermatogenesis-associated protein 11, ABH7, Alkylated DNA repair protein alkB homolog 7, ALKBH7, Spermatogenesis cell proliferation-related protein, SPATA11, Alpha-ketoglutarate-dependent dioxygenase alkB homolog 7, mitochondrial
Reference ARO-P11144
Note For research use only.
Molecular Constructor
Ser16–Cys221

Introduction to Recombinant Human ALKBH7 Protein

Recombinant Human ALKBH7 Protein, also known as AlkB homolog 7, is a protein that is encoded by the ALKBH7 gene in humans. It belongs to the AlkB family of proteins, which are involved in DNA repair and maintenance of genomic stability. The ALKBH7 gene is located on chromosome 11 and is highly expressed in various tissues such as the brain, heart, and liver.

Structure of Recombinant Human ALKBH7 Protein

The Recombinant Human ALKBH7 Protein is a 43 kDa protein that consists of 386 amino acids. It contains an N-terminal domain, a central catalytic domain, and a C-terminal domain. The N-terminal domain is responsible for protein-protein interactions, while the central catalytic domain contains the active site for enzymatic activity. The C-terminal domain is involved in substrate recognition and binding.

The crystal structure of Recombinant Human ALKBH7 Protein has been determined, revealing a unique fold that is distinct from other AlkB family proteins. The protein adopts a compact globular structure with a central cavity that accommodates the active site. The active site contains a conserved Fe(II) ion, which is essential for the enzymatic activity of ALKBH7.

Enzymatic Activity of Recombinant Human ALKBH7 Protein

Recombinant Human ALKBH7 Protein is a dioxygenase enzyme that catalyzes the demethylation of N6-methyladenine (6mA) in single-stranded DNA and RNA. 6mA is a common modification in both DNA and RNA, and its presence can affect gene expression and RNA stability. ALKBH7 specifically targets 6mA in single-stranded DNA and RNA, and it is the only known enzyme that can demethylate 6mA in RNA.

The enzymatic activity of Recombinant Human ALKBH7 Protein is dependent on the presence of Fe(II) and α-ketoglutarate (α-KG). Fe(II) acts as a cofactor and is essential for the catalytic activity of ALKBH7, while α-KG serves as a co-substrate and is required for the binding of the substrate to the active site. The reaction mechanism involves the hydroxylation of 6mA by ALKBH7, followed by the release of formaldehyde and the formation of unmodified adenine.

Applications of Recombinant Human ALKBH7 Protein

The ability of Recombinant Human ALKBH7 Protein to specifically demethylate 6mA in single-stranded DNA and RNA makes it a valuable tool in various research applications. One of its main applications is in epigenetics, as 6mA is considered an epigenetic mark that can regulate gene expression and cellular processes. By studying the role of ALKBH7 in the demethylation of 6mA, researchers can gain a better understanding of the epigenetic mechanisms involved in gene regulation.

Another potential application of Recombinant Human ALKBH7 Protein is in cancer research. Dysregulation of ALKBH7 has been linked to various types of cancer, and its role in DNA repair and maintenance of genomic stability suggests that it may play a crucial role in tumorigenesis. By studying the enzymatic activity and function of ALKBH7, researchers can gain insights into its potential as a therapeutic target for cancer treatment.

Furthermore, Recombinant Human ALKBH7 Protein can be used in drug discovery and development. Its unique structure and enzymatic activity make it a potential target for small molecule inhibitors that can modulate its function. These inhibitors can be used to study the role of ALKBH7 in various cellular processes and potentially lead to the development of novel therapeutics.

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