Recombinant Bacteriophage Lambda Serine/threonine-protein phosphatase Protein, C-His-Myc

Reference: YVV15503
Product nameRecombinant Bacteriophage Lambda Serine/threonine-protein phosphatase Protein, C-His-Myc
Origin speciesEscherichia phage lambda (Bacteriophage lambda)
Expression systemEukaryotic expression
Molecular weight27.37 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 TypeMet1-Ala221
Aliases /SynonymsSerine/threonine-protein phosphatase, 3.1.3.16
ReferenceYVV15503
NoteFor research use only.

Description of Recombinant Bacteriophage Lambda Serine/threonine-protein phosphatase Protein, C-His-Myc

Introduction

The Recombinant Bacteriophage Lambda Serine/threonine-protein phosphatase Protein, also known as Lambda Ser/Thr-PPase, is a protein that plays a crucial role in regulating cellular signaling pathways. It is a recombinant protein that is derived from the bacteriophage Lambda, a virus that infects bacteria. This protein has been extensively studied and its structure, activity, and applications have been well characterized. In this article, we will provide a comprehensive description of this protein, highlighting its importance and potential uses in various fields.

Structure of Recombinant Bacteriophage Lambda Serine/threonine-protein phosphatase Protein

The Lambda Ser/Thr-PPase protein is a member of the protein phosphatase family, which is responsible for removing phosphate groups from other proteins. It is a homodimeric protein, meaning it is composed of two identical subunits. Each subunit contains a catalytic domain and a regulatory domain. The catalytic domain is responsible for the enzymatic activity of the protein, while the regulatory domain helps in its proper functioning and regulation.

The overall structure of the Lambda Ser/Thr-PPase protein is similar to other protein phosphatases, with a central core formed by the catalytic domain and a more flexible regulatory domain. The catalytic domain contains a conserved active site, which is responsible for the dephosphorylation of its target proteins. The regulatory domain, on the other hand, contains binding sites for various regulatory molecules, which can modulate the activity of the protein.

Activity of Recombinant Bacteriophage Lambda Serine/threonine-protein phosphatase Protein

The main function of the Lambda Ser/Thr-PPase protein is to regulate the activity of other proteins by removing phosphate groups from them. This dephosphorylation process is crucial in many cellular signaling pathways, as it can either activate or inhibit the function of target proteins. The Lambda Ser/Thr-PPase protein has been shown to dephosphorylate a wide range of target proteins, including transcription factors, kinases, and other signaling molecules.

Moreover, the activity of the Lambda Ser/Thr-PPase protein can also be regulated by other molecules. For example, binding of regulatory proteins to the regulatory domain can either enhance or inhibit the enzymatic activity of the protein. This allows for fine-tuning of its activity and precise regulation of cellular signaling pathways.

Applications of Recombinant Bacteriophage Lambda Serine/threonine-protein phosphatase Protein

The Lambda Ser/Thr-PPase protein has a wide range of potential applications in various fields, including biotechnology, medicine, and research. One of its main applications is in the production of recombinant proteins. The Lambda Ser/Thr-PPase protein can be used to remove phosphate groups from recombinant proteins, which can improve their stability and activity. This is particularly useful in the production of therapeutic proteins, where stability and activity are crucial for their effectiveness.

In addition, the Lambda Ser/Thr-PPase protein has been studied for its potential role in cancer treatment. It has been shown to dephosphorylate proteins involved in cancer cell growth and survival, making it a potential target for anti-cancer therapies. Furthermore, the protein has also been studied for its role in neurodegenerative diseases, as it has been shown to regulate the activity of proteins involved in these conditions.

Lastly, the Lambda Ser/Thr-PPase protein has been used as a research tool to study various cellular signaling pathways and their regulation. Its ability to dephosphorylate a wide range of target proteins makes it a valuable tool for understanding the complex mechanisms of cellular signaling.

Conclusion

In conclusion, the Recombinant Bacteriophage Lambda Serine/threonine-protein phosphatase Protein is a crucial protein involved in regulating cellular signaling pathways

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