ErbB3 Human, sf9

Tyrosine Kinase ErbB-3 Human Recombinant, sf9

Recombinant Human ErbB3, produced in Sf9 Baculovirus cells, is a single glycosylated polypeptide chain consisting of 863 amino acids (specifically, amino acids 20 to 643). It has a molecular weight of 95.6 kDa. On SDS-PAGE analysis under reducing conditions, it migrates between 100-150 kDa. The protein is expressed with a 239 amino acid hIgG-His tag at its C-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT16222
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless solution that has been sterilized by filtration.

ErbB3 Mouse

Tyrosine Kinase ErbB-3 Mouse Recombinant

Recombinant ErbB3 protein was expressed in Sf9 insect cells using a baculovirus expression system. The protein encompasses amino acids 20 to 641 of the ErbB3 sequence, with an 8-amino acid Histidine tag added at the C-terminus to facilitate purification. The molecular weight of the protein is approximately 69.5 kDa, but it may appear as a band between 70-100 kDa on SDS-PAGE due to glycosylation. The protein was purified using proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT16300
Source
Sf9, Baculovirus cells.
Appearance
A clear and colorless solution.

ErbB4 Human

Tyrosine Kinase ErbB-4 Human Recombinant

Recombinant Human ErbB4, expressed in HEK293 cells, is a single, glycosylated polypeptide chain. It consists of 863 amino acids, spanning from position 26 to 649, with a molecular weight of 96.6 kDa. The protein is engineered with a C-terminal fusion of a 239 amino acid hIgG-His-Tag and purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT16372
Source

HEK293 Cells.

Appearance

Sterile filtered, colorless solution.

TDP1 Human, Sf9

Tyrosyl-DNA Phosphodiesterase 1 Human Recombinant, Sf9

Recombinant human TDP1, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain. It consists of 617 amino acids (1-608) with a molecular mass of 69.5kDa. This protein is fused to a 6 amino acid His-Tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16457
Source
Sf9, Baculovirus cells.
Appearance
Clear, sterile-filtered solution.

ErbB2 Human

ErbB-2 Human Recombinant

Recombinant Human ErbB-2 is a 43.4 kDa protein comprising 397 amino acid residues of human Herstatin, with an additional Methionine residue at the N-terminus (indicated by underlining). It is produced in E. coli.
Shipped with Ice Packs
Cat. No.
BT16001
Source
Escherichia Coli.
Appearance
A clear, colorless solution after filtration.

ErbB2 Human, Sf9

Tyrosine Kinase ErbB-2 Human Recombinant, Sf9

Recombinant Human ErbB2, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain. It contains 638 amino acids (23-652) and has a molecular weight of 70.4kDa (it will appear at approximately 70-100kDa on SDS-PAGE). ErbB2 has an 8 amino acid IgG His-Tag fused to its C-terminus and is purified using special chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT16077
Source
Sf9, Baculovirus cells.
Appearance
A clear, sterile-filtered solution.

ErbB3 Human

Tyrosine Kinase ErbB-3 Human Recombinant

Recombinant Human Tyrosine Kinase ErbB3 (HER3) is produced in E. coli. This non-glycosylated polypeptide is a single chain comprising several epitopes from the extracellular domain of human Erb-b3. Its total molecular weight is approximately 12.0 kDa. The purification of ErbB3 is achieved using specialized chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16160
Source
Escherichia Coli.
Appearance
White, semi-transparent suspension with a concentration of 1 mg/ml.

TYRO3 Mouse

TYRO3 Protein Tyrosine Kinase Mouse Recombinant

TYRO3 Mouse, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain consisting of 628 amino acids (31-419 aa). It has a molecular weight of 68.9 kDa. The protein is fused to a 239 amino acid hIgG-His-Tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16535
Source
Sf9, Baculovirus cells.
Appearance
A sterile, filtered solution that is colorless.
Definition and Classification

Tyrosine kinases are enzymes that transfer a phosphate group from ATP to the tyrosine residues of specific proteins inside a cell. This process, known as phosphorylation, acts as an “on” or “off” switch in many cellular functions . Tyrosine kinases are classified into two main types:

  • Receptor Tyrosine Kinases (RTKs): These are transmembrane proteins located on the cell surface that bind to specific signaling molecules, such as growth factors or hormones .
  • Non-receptor Tyrosine Kinases (NRTKs): These are located in the cytoplasm or nucleus and are activated by various signaling pathways .
Biological Properties

Tyrosine kinases play crucial roles in cellular communication, growth, and differentiation. They are expressed in various tissues and have distinct expression patterns . For example, RTKs are often found on the cell surface, while NRTKs are located within the cell . Their tissue distribution is widespread, affecting numerous cellular processes.

Biological Functions

The primary biological functions of tyrosine kinases include regulating cell growth, proliferation, differentiation, and survival . They play a significant role in immune responses and pathogen recognition by activating various signaling pathways that control these processes .

Modes of Action

Tyrosine kinases interact with other molecules and cells through binding partners and downstream signaling cascades . For instance, RTKs bind to extracellular signaling molecules, causing dimerization and activation of their kinase domains . This leads to autophosphorylation and the activation of downstream signaling proteins .

Regulatory Mechanisms

The expression and activity of tyrosine kinases are tightly regulated through various mechanisms, including transcriptional regulation and post-translational modifications . For example, ligand binding to RTKs triggers dimerization and autophosphorylation, which activates the kinase domains . Additionally, protein tyrosine phosphatases remove phosphate groups, turning off the signaling pathways .

Applications

Tyrosine kinases have numerous applications in biomedical research, diagnostic tools, and therapeutic strategies . They are targets for cancer treatment, with tyrosine kinase inhibitors (TKIs) being used to block the activity of specific kinases involved in tumor growth . Additionally, they serve as biomarkers for various diseases and are used in diagnostic assays .

Role in the Life Cycle

Throughout the life cycle, tyrosine kinases play essential roles in development, aging, and disease . They are involved in cell division, metabolism, migration, cell survival, and apoptosis . Dysregulation of tyrosine kinase activity can lead to various diseases, including cancer .

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