SGK1 Human

Serum/Glucocorticoid Regulated Kinase 1 Human Recombinant

SGK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (60-431 a.a.) and having a molecular mass of 44.5kDa.
SGK1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14625
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

SKP1 Alpha Human

S-phase Kinase-Associated Protein 1 Isoform A Human Recombinant

Recombinant Human SKP1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 160 amino acids (1-160 a.a.) and having a molecular mass of 18kDa.
SKP1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14676
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

Staphylokinase

Staphylokinase Recombinant

Staphylokinase Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 136 amino acids and having a molecular weight of 16kDa.
The Staphylokinase is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14747
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

STAT1 Human

Signal Transducer and Activator of Transcription 1 Human Recombinant

STAT1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 732 amino acids (1-712 a.a.) and having a molecular mass of 85.2 kDa. The STAT1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14807
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

STAT3 Human

Signal Transducer and Activator of Transcription 3 Human Recombinant

STAT3 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (1-770 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 776 amino acids and having a molecular mass of 88.8kDa.STAT3 shows multiple bands between 70-100kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques. 

Shipped with Ice Packs
Cat. No.
BT14834
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

Streptokinase

Streptokinase Recombinant

Streptokinase Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 414 amino acids and having a molecular weight of 47.3kDa.
The Streptokinase is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14880
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

TIE1 Human

TIE1 Human Recombinant

TIE1 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 977 amino acids (22-759 a.a) and having a molecular mass of 106.8kDa.
TIE1 is fused to a 239 amino acid hIgG-His-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT14934
Source

HEK293 Cells.

Appearance

Sterile Filtered colorless solution.

TK1 Human

Thymidine Kinase 1 Human Recombinant

TK1 Human Recombinant produced in E. coli is a single polypeptide chain containing 258 amino acids (1-234) and having a molecular mass of 28.0 kDa.
TK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15032
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

TK2 Human

Thymidine Kinase 2 Human Recombinant

TK2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 257 amino acids (34-265 a.a) and having a molecular mass of 30.2kDa.
TK2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15106
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

TPK1 Human

Thiamin Pyrophosphokinase 1 Human Recombinant

TPK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (1-243 a.a.) and having a molecular mass of 29.8kDa.
TPK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15211
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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