TPMT Human

Thiopurine S-methyltransferase Human Recombinant

TPMT Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 245 amino acids (1-245) and having a molecular mass of 28 kDa.
Thiopurine S-methyltransferase is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15283
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

TRIB3 Human

Tribbles Pseudokinase 3 Human Recombinant

TRIB3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-358 a.a) and having a molecular mass of 42.0kDa.
TRIB3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15360
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

TSSK2 Human

Testis Specific Serine Kinase 2 Human Recombinant

TSSK2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-358 a.a) and having a molecular mass of 43kDa.
TSSK2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15460
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

TSSK6 Human

Testis Specific Serine Kinase 6 Human Recombinant

TSSK6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-273) and having a molecular mass of 32.7kDa.
TSSK6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15525
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

UCK1 Human

Uridine-Cytidine Kinase 1 Human Recombinant

UCK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids (143-273a.a) and having a molecular mass of 17.5kDa.
UCK1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15592
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

UCK2 Human

Uridine-Cytidine Kinase 2 Human Recombinant

UCK2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 269 amino acids (1-261a.a.) and having a molecular mass of 30.3kDa.
UCK2 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15656
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.
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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