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Brand: ProteoGenix

Recombinant Human AASDHPPT, N-His

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

$392.00

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Met1–Ser309
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Recombinant Human AASDHPPT, N-His

Recombinant Human AASDHPPT, N-His

Product name Recombinant Human AASDHPPT, N-His
Origin species Human
Expression system Prokaryotic expression
Molecular weight 38.09 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 Met1-Ser309
Aliases /Synonyms L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase, Alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase, LYS5 ortholog, AASD-PPT, AASDHPPT, 4'-phosphopantetheinyl transferase
Reference ARO-P12931
Note For research use only.
Molecular Constructor
Met1–Ser309

Introduction

Recombinant Human AASDHPPT (alanyl-tRNA synthetase domain-containing protein 2) is a protein that plays a crucial role in the process of protein synthesis. This protein is encoded by the AASDHPPT gene and is found in both prokaryotic and eukaryotic cells. In this article, we will delve into the structure, activity, and applications of this important protein.

Structure of Recombinant Human AASDHPPT

Recombinant Human AASDHPPT is a 57 kDa protein that consists of 520 amino acids. It contains a highly conserved alanyl-tRNA synthetase domain, which is responsible for the catalytic activity of the protein. The protein also has a C-terminal domain that is unique to AASDHPPT and is essential for its function.

The crystal structure of Recombinant Human AASDHPPT has been determined, revealing a homodimeric structure. Each monomer consists of an N-terminal domain and a C-terminal domain, connected by a long linker region. The C-terminal domain forms the active site of the protein, while the N-terminal domain is involved in protein-protein interactions.

Activity of Recombinant Human AASDHPPT

Recombinant Human AASDHPPT is an essential component of the protein synthesis machinery. It plays a crucial role in the attachment of alanine to its cognate transfer RNA (tRNA), which is a necessary step in the process of protein synthesis. This activity is carried out by the alanyl-tRNA synthetase domain of the protein.

Apart from its role in protein synthesis, Recombinant Human AASDHPPT has also been found to have non-canonical functions. It has been shown to interact with other proteins involved in cellular processes such as DNA repair and cell cycle regulation. This suggests that the protein may have additional roles in the cell beyond its canonical function in protein synthesis.

Applications of Recombinant Human AASDHPPT

Recombinant Human AASDHPPT has a wide range of applications in both research and industrial settings. One of the most significant applications of this protein is in the production of recombinant proteins. The alanyl-tRNA synthetase domain of AASDHPPT is often used as a fusion tag in recombinant protein production, allowing for easy purification and detection of the target protein.

In addition to its use in protein production, Recombinant Human AASDHPPT has also been studied for its potential therapeutic applications. It has been found to be overexpressed in certain types of cancer, making it a potential target for cancer treatment. Furthermore, the protein has been shown to have a role in neurodegenerative diseases, making it a potential therapeutic target for these conditions as well.

Conclusion

In conclusion, Recombinant Human AASDHPPT is a crucial protein involved in protein synthesis and has additional non-canonical functions. Its structure, activity, and applications make it a valuable tool in both research and industrial settings. Further studies on this protein may provide insights into its potential therapeutic applications, making it an exciting area of research in the field of molecular biology.

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