Recombinant Human ADCY5 Protein, N-His

Reference: YHB70002
Product nameRecombinant Human ADCY5 Protein, N-His
Origin speciesHuman
Expression systemEukaryotic expression
Molecular weight24.10 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°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)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeSer1066-Ser1261
Aliases /SynonymsAC5, ATP pyrophosphate-lyase 5, Adenylate cyclase type 5, Adenylate cyclase type V, Adenylyl cyclase 5, ADCY5
ReferenceYHB70002
NoteFor research use only.

Description of Recombinant Human ADCY5 Protein, N-His

Structure of Recombinant Human ADCY5 Protein

Recombinant Human ADCY5 Protein is a type of protein that is produced through genetic engineering techniques. It is a modified version of the natural human ADCY5 protein, which plays a crucial role in cellular signaling pathways. The recombinant protein is made up of 1214 amino acids and has a molecular weight of approximately 136 kDa.

The structure of Recombinant Human ADCY5 Protein is similar to that of the natural protein, with a complex three-dimensional shape. It is composed of several functional domains, including a catalytic domain, regulatory domains, and transmembrane domains. These domains work together to regulate the activity of the protein and its interactions with other molecules.

Activity of Recombinant Human ADCY5 Protein

Recombinant Human ADCY5 Protein is a crucial component of the cellular signaling pathway known as the cAMP signaling pathway. This pathway is responsible for regulating a wide range of cellular processes, including metabolism, cell growth, and gene expression. The activity of ADCY5 protein is essential for maintaining the proper functioning of this pathway.

The main function of Recombinant Human ADCY5 Protein is to catalyze the conversion of ATP (adenosine triphosphate) to cAMP (cyclic adenosine monophosphate). This conversion is a crucial step in the cAMP signaling pathway, as cAMP acts as a second messenger and activates downstream signaling molecules. In addition to its catalytic activity, ADCY5 protein also has regulatory functions that help to fine-tune the activity of the pathway.

Application of Recombinant Human ADCY5 Protein

Recombinant Human ADCY5 Protein has a wide range of applications in both research and clinical settings. One of its main uses is in studying the cAMP signaling pathway and its role in various cellular processes. Researchers use the recombinant protein to investigate the function of ADCY5 and its interactions with other molecules in the pathway.

In addition to its research applications, Recombinant Human ADCY5 Protein has potential therapeutic uses. Mutations in the ADCY5 gene have been linked to several diseases, including diabetes, obesity, and certain types of cancer. By studying the structure and activity of the recombinant protein, researchers can gain insights into these diseases and develop potential treatments targeting ADCY5.

Furthermore, Recombinant Human ADCY5 Protein can also be used in drug discovery and development. As the cAMP signaling pathway is involved in many disease processes, targeting ADCY5 with specific inhibitors or activators can potentially lead to the development of new drugs for various conditions.

Conclusion

In summary, Recombinant Human ADCY5 Protein is a modified version of the natural human ADCY5 protein, with a complex three-dimensional structure and crucial functions in the cAMP signaling pathway. Its applications in research and therapeutic development make it a valuable tool in understanding and treating various diseases. Further studies on this protein can lead to a better understanding of its role in cellular processes and potential new treatments for diseases associated with its dysfunction.

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