MEK1 Human

Mitogen Activated Kinase Kinase 1 Human Recombinant

MAP2K1 active Human Recombinant produced in Sf9 cells is a glycosylated, polypeptide chain containing amino acids 2-393 having a molecular mass of 47 kDa. MAP2K1 is fused to a polyhistidine tag and is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11318
Source
Sf9 Insect Cells.
Appearance
Sterile Filtered clear solution.

MERTK Mouse

MER Proto-Oncogene Tyrosine Kinase Mouse Recombinant

MERTK Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 718 amino acids (19-497 aa) and having a molecular mass of 79.2kDa.
MERTK is fused to a 239 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT11395
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

MOB1B Human

MOB Kinase Activator 1B Human Recombinant

MOB1B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 239 amino acids (1-216 a.a) and having a molecular mass of 27kDa.
MOB1B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11443
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

MOB3B Human

MOB Kinase Activator 3B Human Recombinant

MOB3B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 239 amino acids (1-216) and having a molecular mass of 27.9 kDa. MOB3B is fused to a 23 amino acid His-tag at N-terminus.
Shipped with Ice Packs
Cat. No.
BT11527
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

MVK Human

Mevalonate Kinase Human Recombinant

MVK Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 419 amino acids (1-396) and having a molecular mass of 44.8kDa.
The MVK is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques. 
Shipped with Ice Packs
Cat. No.
BT11588
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

NAGK Human

N-Acetylglucosamine Kinase Human Recombinant

NAGK Human Recombinant produced in E. coli is a single polypeptide chain containing 367 amino acids (1-344) and having a molecular mass of 39.8kDa.
NAGK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11641
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

NDK E.Coli

Nucleoside Diphosphate Kinase E.Coli Recombinant

NDK E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (1-143 a.a.) and having a molecular mass of 18kDa.
NDK is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11688
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

NEK7 Human

NIMA-related kinase 7 Human Recombinant

NEK7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 326 amino acids (1-302 a.a) and having a molecular mass of 37kDa.NEK7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11746
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

NME2 Rat

Non-Metastatic Cells 2 Rat Recombinant

NME2 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids (1-152 a.a) and having a molecular mass of 19.7kDa.
NME2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11804
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

NNMT Mouse

Nicotinamide N-Methyltransferase Mouse Recombinant

NNMT Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids (1-264a.a) and having a molecular mass of 32.1kDa.
NNMT is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT11870
Source
Escherichia 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 .

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