DCK Human

Deoxycytidine Kinase Human Recombinant

DCK Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 296 amino acids (1-260 a.a.) and having a molecular mass of 34.6kDa. The DCK is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9720
Source
Escherichia Coli.
Appearance
DCK is supplied as a sterile filtered clear solution.

DTYMK Human

Deoxythymidylate Kinase Human Recombinant

DTYMK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212 a.a) and having a molecular mass of 26kDa.
DTYMK is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9798
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

DYRK1A Human

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

DYRK1A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (159-479a.a) and having a molecular mass of 39.4kDa.
DYRK1A is fused to a 22 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9854
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

ETNK2 Human

EthanolamineKinase 2 Human Recombinant

ETNK2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (1-386 a.a) and having a molecular mass of 47.2kDa.
ETNK2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9959
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

Flavokinase Human

Riboflavin Kinase Human Recombinant

Flavokinase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids (1-162 a.a.) and having a molecular mass of 20.5kDa. Flavokinase is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10036
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

GALK1 Human

Galactokinase 1 Human Recombinant

GALK1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 412 amino acids (1-392 a.a.) and having a molecular mass of 44.4 kDa. The GALK1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT10105
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

GLK E.coli

Glucokinase E.coli Recombinant

GLK E.coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-321 a.a) and having a molecular mass of 37.1kDa.
GLK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10176
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

GLK E.Coli, Active

Glucokinase E.coli Recombinant, BioActive

GLK E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-321) and having a molecular mass of 37.1kDa.
GLK is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT10243
Source

Escherichia Coli.

Appearance
Sterile Filtered colorless solution.

GlpK E. coli

Glycerol kinase E. Coli Recombinant

GlpK E. Coli Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 525 amino acids (1-502 a.a) and having a molecular mass of 58.6 kDa.
GlpK is fused to a 23 amino acid His-tag at N-terminus& purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10314
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

HYKK Human

Hydroxylysine Kinase Human Recombinant

HYKK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 396 amino acids (1-373a.a) and having a molecular mass of 44.3kDa.
HYKK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10381
Source
E.coli.
Appearance
Sterile Filtered colorless 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 .

© Copyright 2024 Thebiotek. All Rights Reserved.