MAPKAPK3 Human

Mitogen-Activated Protein Kinase-Activated Protein Kinase 3 Human Recombinant

Recombinant Human MAPKAPK3, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 405 amino acids (amino acids 1-382). It has a molecular weight of 45.4 kDa. The MAPKAPK3 protein is fused to a 23 amino acid His-tag at its N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11232
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

MEK1 Human

Mitogen Activated Kinase Kinase 1 Human Recombinant

Active human recombinant MAP2K1, produced in Sf9 cells, is a glycosylated polypeptide chain comprising amino acids 2-393. With a molecular mass of 47 kDa, it is fused to a polyhistidine tag and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11318
Source
Sf9 Insect Cells.
Appearance
Clear, sterile-filtered solution.

PDXK Human

Pyridoxal Kinase Human Recombinant

Recombinant human PDXK, expressed in E. coli, is a 37.6 kDa non-glycosylated polypeptide chain containing 336 amino acids (including a 24 amino acid His tag at the N-terminus). The protein sequence comprises amino acids 1-312 of the PDXK protein. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12618
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

PFKM Human

Phosphofructokinase, Muscle Human Recombinant

Recombinant PFKM protein, of human origin, was produced in E. coli. This protein is a single, non-glycosylated polypeptide chain consisting of 800 amino acids (residues 1-780) and has a molecular weight of 87.3 kDa. The PFKM protein is fused to a 20 amino acid His-Tag at the N-terminus. Purification was achieved using standard chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12708
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

PGK1 Human

Phosphoglycerate Kinase 1 Human Recombinant

Recombinant human PGK1, expressed in E. coli, is a non-glycosylated polypeptide chain containing 417 amino acids (corresponding to residues 1-417 of the native protein) with a 20 amino acid His-tag fused at the N-terminus. The protein has a molecular weight of 46.8 kDa and is purified to high purity using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12776
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

PKM2 Mouse

Tumour Type M2 Pyruvate Kinase Mouse Recombinant

Recombinant PKM2 Mouse protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 554 amino acids (1-531 a.a) with a molecular weight of 60.2kDa. A 23 amino acid His-tag is fused to the N-terminus of PKM2, and the protein undergoes purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT13819
Source
Escherichia Coli.
Appearance
Clear solution subjected to sterile filtration.

ACKA E.Coli

Acetate Kinase E.Coli Recombinant

This product consists of recombinant ACKA, produced in E. coli. The protein is a single, non-glycosylated polypeptide chain with a molecular weight of 45.7 kDa. It encompasses amino acids 1-400 of the native ACKA sequence and includes a 23 amino acid His-Tag fused at the N-terminus to facilitate purification. The protein has been purified using proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT8909
Source
Escherichia Coli.
Appearance
A clear solution that has undergone sterile filtration.

AKAP7 Human

A Kinase Anchor Protein 7 Human Recombinant

Recombinant human AKAP7, expressed in E. coli, is a single polypeptide chain with a molecular weight of 11.5 kDa. It encompasses amino acids 1-81 and includes a 24-amino acid His-tag at the N-terminus. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9050
Source
E.coli.
Appearance
Clear, colorless solution, sterile filtered.

TIE1 Human

TIE1 Human Recombinant

Recombinant Human TIE1 protein, produced in HEK293 cells, is a single, glycosylated polypeptide chain. It consists of 977 amino acids (22-759 a.a), resulting in a molecular mass of 106.8 kDa. The protein includes a C-terminal fusion of a 239 amino acid hIgG-His-Tag. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14934
Source

HEK293 Cells.

Appearance
Sterile Filtered colorless solution.

TK1 Human

Thymidine Kinase 1 Human Recombinant

This product consists of the recombinant human TK1 enzyme, produced in E. coli. It is a single-chain polypeptide with 258 amino acids (residues 1-234) and a molecular weight of 28.0 kDa. The enzyme has a His-tag attached to its N-terminus to facilitate purification, which is performed using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15032
Source
E.coli.
Appearance
Clear and colorless solution, sterilized by filtration.
Definition and Classification

Protein kinases are enzymes that catalyze the transfer of phosphate groups from high-energy, phosphate-donating molecules to specific substrates, a process known as phosphorylation . This modification typically results in a functional change of the target protein by altering its enzyme activity, cellular location, or interaction with other proteins . Protein kinases are classified into several groups based on the amino acid residue they phosphorylate: serine/threonine kinases, tyrosine kinases, and dual-specificity kinases .

Biological Properties

Protein kinases are key regulators of cell function and are involved in almost all cellular processes . They are expressed in various patterns and distributed across different tissues. For instance, serine/threonine kinases are widely distributed and play roles in processes such as cell division and metabolism . Tyrosine kinases are often involved in signaling pathways that regulate cell growth and differentiation . The human genome contains about 500 protein kinase genes, constituting approximately 2% of all human genes .

Biological Functions

Protein kinases play crucial roles in regulating cellular processes such as cell division, metabolism, transcription, differentiation, and apoptosis . They are also involved in immune responses and pathogen recognition. For example, certain kinases are activated in response to pathogens and help coordinate the immune response by modulating the activity of immune cells .

Modes of Action

Protein kinases function by transferring a phosphate group from ATP to specific amino acids in their substrate proteins . This phosphorylation can activate or deactivate the substrate protein, alter its interaction with other molecules, or change its cellular location . Kinases often work in signaling cascades, where one kinase activates another, leading to a chain reaction that amplifies the signal and results in a specific cellular response .

Regulatory Mechanisms

The activity of protein kinases is tightly regulated by various mechanisms, including transcriptional regulation, post-translational modifications, and interactions with other proteins . For instance, kinases can be activated or inhibited by phosphorylation, binding to regulatory proteins, or changes in their cellular localization . These regulatory mechanisms ensure that kinases are activated only in response to specific signals and that their activity is precisely controlled .

Applications

Protein kinases are important targets in biomedical research and have applications in diagnostic tools and therapeutic strategies . Kinase inhibitors are used to treat various diseases, including cancer, cardiovascular diseases, and inflammatory disorders . For example, tyrosine kinase inhibitors are used to treat certain types of leukemia and other cancers . Additionally, kinases are used as biomarkers for disease diagnosis and prognosis .

Role in the Life Cycle

Protein kinases play essential roles throughout the life cycle, from development to aging and disease . During development, kinases regulate processes such as cell proliferation, differentiation, and tissue formation . In adulthood, they continue to regulate cellular functions and maintain homeostasis . Dysregulation of kinase activity can lead to various diseases, including cancer, neurodegenerative disorders, and metabolic diseases .

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