STK3 Human

Serine/Threonine Kinase 3 Human Recombinant

STK3 Human Recombinant produced in Sf9 Insect cell is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-322aa.a) and having a molecular mass of 37.6kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).
STK3 is fused to a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22582
Source
Sf9 Insect cells.
Appearance
Sterile Filtered colorless solution.

STK11 Human

Serine/Threonine Kinase 11 Human Recombinant

STK11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 456 amino acids (1-433) and having a molecular mass of 51kDa.
STK11 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT22335
Source

Escherichia Coli.

Appearance
Sterile Filtered colorless solution.

STK16 Human

Serine/Threonine Kinase 16 Human Recombinant

STK16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 329 amino acids (1-305 a.a) and having a molecular mass of 37.2kDa.
STK16 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22393
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

STK17A Human

Serine/Threonine Kinase 17A Human Recombinant

STK17A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (64-321 a.a) and having a molecular mass of 31.9kDa.STK17A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22451
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

STK17B Human

Serine/Threonine Kinase 17B Human Recombinant

STK17B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 395 amino acids (1-372 a.a) and having a molecular mass of 44.7kDa.
STK17B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22505
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.
Definition and Classification

Serine/threonine kinases (STKs) are a class of enzymes that phosphorylate the hydroxyl group of serine or threonine residues in proteins. This phosphorylation process is crucial for regulating various cellular processes. STKs are part of the larger family of protein kinases, which also includes tyrosine kinases. They are further classified into classical STKs, found in all eukaryotic cells, and atypical STKs, found in specific cell types .

Biological Properties

Key Biological Properties: STKs are highly conserved and multifunctional enzymes that play a role in cell activity, survival, proliferation, and apoptosis . They are constitutively active and regulate several signaling pathways.

Expression Patterns and Tissue Distribution: STKs are expressed in various tissues, including the brain, heart, liver, and muscles. Their expression patterns can vary depending on the specific kinase and the physiological or pathological conditions .

Biological Functions

Primary Biological Functions: STKs are involved in regulating cell proliferation, programmed cell death (apoptosis), cell differentiation, and embryonic development . They also play a role in immune responses and pathogen recognition by phosphorylating key proteins involved in these processes .

Role in Immune Responses and Pathogen Recognition: STKs are crucial for the activation of immune cells and the production of cytokines. They help in recognizing and responding to pathogens by phosphorylating proteins that initiate immune signaling cascades .

Modes of Action

Mechanisms with Other Molecules and Cells: STKs transfer phosphate groups from ATP to serine or threonine residues on target proteins. This phosphorylation can alter the activity, stability, or localization of the target proteins .

Binding Partners and Downstream Signaling Cascades: STKs interact with various binding partners, including other kinases, phosphatases, and scaffold proteins. These interactions help propagate downstream signaling cascades that regulate cellular functions .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: The activity of STKs is regulated by multiple mechanisms, including transcriptional regulation, post-translational modifications, and subcellular localization .

Transcriptional Regulation: The expression of STKs can be regulated by transcription factors that respond to various signals, such as cyclic AMP (cAMP) and calcium ions .

Post-Translational Modifications: STKs can undergo various post-translational modifications, such as phosphorylation, ubiquitination, and acetylation, which can modulate their activity and stability .

Applications

Biomedical Research: STKs are widely studied in biomedical research due to their role in various cellular processes and diseases. They are used as models to understand signaling pathways and cellular regulation .

Diagnostic Tools: STKs can serve as biomarkers for certain diseases, such as cancer and neurodegenerative disorders. Their activity levels can be measured to diagnose and monitor disease progression .

Therapeutic Strategies: STKs are potential targets for therapeutic interventions. Inhibitors of specific STKs are being developed as treatments for cancer, inflammatory diseases, and other conditions .

Role in the Life Cycle

Role Throughout the Life Cycle: STKs play a critical role throughout the life cycle, from development to aging and disease. During development, they regulate cell differentiation and tissue formation . In adulthood, they maintain tissue homeostasis and regulate responses to stress and injury . In aging and disease, dysregulation of STK activity can contribute to various pathologies, including cancer, neurodegenerative diseases, and metabolic disorders .

© Copyright 2024 Thebiotek. All Rights Reserved.