TSSK2 Human

Testis Specific Serine Kinase 2 Human Recombinant

Recombinant human TSSK2, expressed in E. coli, is a non-glycosylated polypeptide chain with 381 amino acids (1-358 a.a) and a molecular weight of 43 kDa. It includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15460
Source
E.coli.
Appearance
Clear, colorless solution, sterile-filtered.

CMPK1 Human

Cytidine Monophosphate Kinase 1 Human Recombinant

Recombinant human CMPK1, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 248 amino acids (1-228) with a molecular weight of 28kDa. A 20 a.a His-Tag is fused to the N-terminus of CMPK1, and it undergoes purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT9497
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

COAA E.Coli

Pantothenate Kinase E.Coli Recombinant

Recombinant COAA from E. coli is produced as a single, non-glycosylated polypeptide chain. It encompasses 340 amino acids (residues 1-316) and exhibits a molecular weight of 38.9 kDa. The protein is engineered with a 24 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9544
Source
E.coli.
Appearance
Sterile, colorless solution.

CSK Human

C-Src Tyrosine Kinase Human Recombinant

Recombinant human CSK, expressed in E. coli, is a single polypeptide chain devoid of glycosylation. It comprises 473 amino acids (specifically residues 1-450) and exhibits a molecular weight of 53.1 kDa. This CSK variant features a 23 amino acid His-Tag fused at its N-terminus, facilitating purification through specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT9645
Source
Escherichia Coli.
Appearance
A clear solution that has undergone sterile filtration.

AKT3 Human

AKT Serine/Threonine Kinase 3 Human Recombinant

Recombinant human AKT3, expressed in HEK293 cells, is a single, glycosylated polypeptide chain comprising 485 amino acids (1-479a.a) with a molecular weight of 56.5 kDa.
A 6-amino acid His-tag is fused to the C-terminus of AKT3. The protein is purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT9151
Source

HEK293 Cells.

Appearance

Sterile, colorless solution.

BLK Human

B lymphoid tyrosine kinase Human Recombinant

Recombinant BLK protein, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 525 amino acids (1-505 a.a.) with a molecular weight of 59.8 kDa. It includes a 20 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT9275
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

BRAF Human

B-Raf Proto-Oncogene Human Recombinant

Recombinant Human BRAF, produced in E. coli, is a non-glycosylated polypeptide chain consisting of 360 amino acids (432-766a.a). It has a molecular weight of 40.6 kDa. The protein includes a 25 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9351
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

CKB Human

Creatine Kinase Brain Human Recombinant

Recombinant human CKB, produced in E. coli, is a single polypeptide chain that lacks glycosylation. It consists of 381 amino acids (1-381a.a) and has a molecular weight of 42.6kDa. The purification of CKB is achieved using specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT9408
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

CKS2 Human

CDC28 Protein Kinase 2 Human Recombinant

Recombinant human CKS2, fused to a T7-Tag, is produced in E. coli. It is a single, non-glycosylated polypeptide chain with 94 amino acids and a molecular weight of 11 kDa.
Shipped with Ice Packs
Cat. No.
BT9477
Source
Escherichia Coli.
Appearance
A sterile, colorless solution.

GLK E.Coli, Active

Glucokinase E.coli Recombinant, BioActive

Recombinant GLK from E. coli, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 344 amino acids (residues 1-321) and has a molecular weight of 37.1 kDa. The protein includes a 23-amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10243
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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