TK2 Human

Thymidine Kinase 2 Human Recombinant

Recombinant human TK2, produced in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of 30.2 kDa. This single-chain protein consists of 257 amino acids (34-265 a.a) and includes a 25 amino acid His-tag at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15106
Source
E.coli.
Appearance
Clear, colorless solution, sterile-filtered.

TPK1 Human

Thiamin Pyrophosphokinase 1 Human Recombinant

This product contains a recombinant human TPK1 protein produced in E. coli. The protein is a single, non-glycosylated polypeptide chain with 267 amino acids, including a 24 amino acid His-tag at the N-terminus. With a molecular weight of 29.8 kDa, the protein is purified using proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT15211
Source
Escherichia Coli.
Appearance
Clear and colorless solution, sterilized by filtration.

TPMT Human

Thiopurine S-methyltransferase Human Recombinant

Recombinant human TPMT, expressed in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of 28 kDa. It encompasses amino acids 1-245, representing the full protein sequence. The purification process involves proprietary chromatographic methods to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT15283
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

UCK2 Human

Uridine-Cytidine Kinase 2 Human Recombinant

UCK2, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 30.3 kDa. It consists of 269 amino acids, including an 8 amino acid His-tag at the C-terminus (1-261a.a.). The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15656
Source
Escherichia Coli.
Appearance
Clear, sterile solution.

GlpK E. coli

Glycerol kinase E. Coli Recombinant

Recombinant GlpK E. Coli is produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 525 amino acids (1-502 a.a) and has a molecular mass of 58.6 kDa. GlpK is fused to a 23 amino acid His-tag at the N-terminus and 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

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

IDNK E.Coli

Thermosensitive Gluconokinase E.Coli Recombinant

Recombinant IDNK, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 210 amino acids (including a 23-amino acid His-tag at the N-terminus, spanning residues 1-187). It has a molecular mass of 23.4 kDa. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10449
Source
E.coli.
Appearance
A clear, colorless solution, sterile-filtered.

IDNK E.Coli, Active

Thermosensitive Gluconokinase E.Coli Recombinant, BioActive

Recombinant IDNK, expressed in E.Coli, is a single, non-glycosylated polypeptide chain. It consists of 210 amino acids, including a 23 amino acid His-Tag at the N-terminus, and has a molecular weight of 23.4 kDa. The protein is purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT10537
Source

Escherichia Coli.

Appearance
A clear, sterile-filtered solution.

ILK1 Human

Integrin Linked Kinase Human Recombinant

Recombinant human ILK1, produced in E. coli, is a non-glycosylated polypeptide chain comprising 452 amino acids (fragment 1-452). It has a molecular weight of 55.92 kDa and includes a 4.5 kDa amino-terminal hexahistidine tag. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10587
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

NEK7 Human

NIMA-related kinase 7 Human Recombinant

Recombinant human NEK7 protein has been produced in E. coli. It is a single, non-glycosylated polypeptide chain comprising 326 amino acids (amino acids 1-302) with a molecular weight of 37 kDa. A 24-amino acid His-tag is fused to the N-terminus of NEK7. The protein has been purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11746
Source
Escherichia Coli.
Appearance
A clear 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 .

© Copyright 2024 Thebiotek. All Rights Reserved.