DCK Human

Deoxycytidine Kinase Human Recombinant

Recombinant human DCK, expressed in E. coli, is a monomeric protein with a His-tag at its N-terminus. This non-glycosylated polypeptide consists of 296 amino acids, with a molecular weight of 34.6 kDa. The protein encompasses amino acids 1-260 of the DCK sequence and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT9720
Source
Escherichia Coli.
Appearance
The DCK protein is provided as a clear, sterile-filtered solution.

DTYMK Human

Deoxythymidylate Kinase Human Recombinant

Recombinant human DTYMK, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 232 amino acids (with a sequence spanning from amino acid position 1 to 212) and has a molecular weight of 26kDa. The recombinant protein is designed with a 20 amino acid His-tag fused at the N-terminus to facilitate purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9798
Source
E.coli.
Appearance
A clear and colorless solution that has been sterilized by filtration.

DYRK1A Human

Dual-Specificity Tyrosine-(Y)-Phosphorylation Regulated 1A Human Recombinant

Recombinant human DYRK1A, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein consists of 343 amino acids (159-479a.a), resulting in a molecular weight of 39.4 kDa. It is fused to a 22 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9854
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

Ketohexokinase Human

Ketohexokinase Human Recombinant

Recombinant Human Ketohexokinase, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 32.7 kDa. It comprises 298 amino acids.
Shipped with Ice Packs
Cat. No.
BT10990
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile solution.

KIT Human

KIT Proto-Oncogene Receptor Tyrosine Human Recombinant

Produced in Sf9 Insect cells, KIT is a single, glycosylated polypeptide chain consisting of 507 amino acids (26-524 a.a.). It has a molecular mass of 57.1kDa, though it appears as approximately 50-70kDa on SDS-PAGE. The protein is expressed with an 8 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11062
Source

Sf9, Baculovirus.

Appearance
Colorless, sterile-filtered solution.

MAPK13 Human

Mitogen-Activated Protein Kinase 13 Human Recombinant

Recombinant human MAPK13, produced in E.coli, is a single, non-glycosylated polypeptide chain consisting of 385 amino acids (residues 1-365) with a molecular weight of 44.2 kDa. It includes a 20 amino acid His-tag fused at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11153
Source
E.coli.
Appearance
Clear, colorless solution, sterile-filtered.

IP6K2 Human

Inositol Hexakisphosphate Kinase 2 Human Recombinant

Recombinant human IP6K2, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 446 amino acids (1-426a.a) with a molecular weight of 51.3 kDa. This protein is fused to a 20 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10675
Source
E.coli.
Appearance
Colorless, sterile-filtered solution.

ITPK1 Human

Inositol-Tetrakisphosphate 1-Kinase Human Recombinant

This product is a purified version of the human ITPK1 protein. It has been produced in a laboratory setting using E. coli bacteria. The protein is not glycosylated and has a molecular weight of 48.1 kDa. It is provided in a solution with specific buffer conditions.
Shipped with Ice Packs
Cat. No.
BT10770
Source
E.coli.
Appearance
A clear and colorless liquid that has been sterilized by filtration.

JAK2 Human

Janus Kinase 2 Human Recombinant

Recombinant human JAK2, expressed in E. coli, is a non-glycosylated polypeptide chain comprising 157 amino acids (residues 1014-1132). It has a molecular weight of 18.1 kDa. The protein includes a 37 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10920
Source
E.coli.
Appearance
A sterile, colorless solution.

PAK4 Human

p21 Activated Kinase 4 Human Recombinant

PAK4 Human Recombinant, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 628 amino acids (1-591 a.a.) with a molecular weight of 68.3 kDa. This protein is fused to a 37 amino acid His-Tag at the N-terminus and purified using standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT12088
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been 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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