NTRK1 Rat

Neurotrophic Receptor Tyrosine Kinase 1 Rat Recombinant

NTRK1 Rat Recombinant produced in HEK is a single, non-glycosylated polypeptide chain containing 623 amino acids (35-418 a.a) and having a molecular mass of 69 kDa. NTRK1 is fused to a 239 amino acid human IgG-His-tag at C-terminus & purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT11930
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

p38a/SAPK2 Human

p38a/SAPK2 Human Recombinant

p38/SAPK2 is a non-glycosilated polypeptide produced by phosphorylation of the purified p38 alpha with MKK6 having a molecular mass of 42.7 kDa.
Shipped with Ice Packs
Cat. No.
BT12002
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

PAK4 Human

p21 Activated Kinase 4 Human Recombinant

PAK4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 628 amino acids (1-591 a.a.) and having a molecular mass of 68.3 kDa.
PAK4 is fused to 37 amino acid His-Tag at N-terminus and is purified by standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT12088
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

PBK Human

PDZ Binding Kinase Human Recombinant

PBK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 346 amino acids (1-322 a.a) and having a molecular mass of 38.6kDa (Molecular weight on SDS-PAGE will appear higher).
PBK is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12165
Source
Escherichia Coli.
Appearance
DCK is supplied as a sterile filtered clear solution.

PCK1 Human

Phosphoenolpyruvate Carboxykinase 1 Human Recombinant

PCK1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 646 amino acids (1-622) and having a molecular mass of 71.7kDa.
PCK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12263
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

PDK1 Human

Pyruvate Dehydrogenase Kinase Isozyme 1 Human Recombinant

PDK1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 429 amino acids (29-436) and having a molecular mass of 48.6 kDa. PDK1 is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12324
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

PDXK Human

Pyridoxal Kinase Human Recombinant

PDXK Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 336 amino acids (1-312 a.a.) and having a molecular mass of 37.6kDa. The PDXK is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12618
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

PFKM Human

Phosphofructokinase, Muscle Human Recombinant

PFKM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 800 amino acids (1-780 a.a.) and having a molecular mass of 87.3 kDa. PFKM protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Shipped with Ice Packs
Cat. No.
BT12708
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

PGK1 Human

Phosphoglycerate Kinase 1 Human Recombinant

PGK1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 437 amino acids (1-417 a.a.) and having a molecular mass of 46.8kDa. PGK1 is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12776
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

PGK1 Human, Active

Phosphoglycerate Kinase 1 Human Recombinant, BioActive

PGK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 437 amino acids (1-417a.a.) and having a molecular mass of 46.8kDa.
PGK1 is fused to a 20 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT12906
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 .

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