ANGPTL3 Human, HEK

Angiopoietin Like Protein 3 Human Recombinant, HEK

Recombinant Human ANGPTL3, produced in HEK cells, is a single, glycosylated polypeptide chain encompassing amino acids 17-460. With a total of 450 amino acids, it has a calculated molecular mass of 52.6 kDa. The 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.
BT9946
Source
HEK 293.
Appearance
White, lyophilized powder after filtration.

ANGPTL4 Human

Angiopoietin-like Protein 4 Human Recombinant

The ANGPTL4 Human Recombinant protein is produced with a His Tag fused to its N-terminus. This fusion protein, Angiopoietin-like Protein 4 His-Tagged Fusion Protein, has a molecular weight of 25 kDa and comprises 204 amino acid residues of Angiopoietin-like Protein 4 along with 16 additional amino acid residues forming the His Tag (underlined).
Shipped with Ice Packs
Cat. No.
BT10038
Source
Escherichia Coli.
Appearance
White powder obtained after filtration and lyophilization.

ANGPT2 Human

Angiopoietin 2 Human Recombinant

Recombinant human ANGPT2 is produced in Chinese hamster ovary (CHO) cells using recombinant DNA technology. It is a single polypeptide chain encompassing amino acids 19 to 496 of the ANGPT2 protein sequence. A 6-amino acid histidine tag (His-tag) is fused to the C-terminus for purification purposes. The resulting protein consists of 484 amino acids and has a molecular weight of 55.7 kilodaltons (kDa). When analyzed by SDS-PAGE under reducing conditions, ANGPT2 appears as multiple bands ranging from 50 to 100 kDa. The protein is purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT9125
Source

Chinese Hamster Ovary Cells (CHO).

Appearance

The product is a sterile-filtered solution that appears colorless.

ANGPTL2 Human

Angiopoietin-like Protein 2 Human Recombinant

Recombinant Human ANGPTL2, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 493 amino acids (22-493 a.a.). This includes a 20 a.a. N-terminal His tag, resulting in a total molecular mass of 57.1kDa (calculated).

Shipped with Ice Packs
Cat. No.
BT9233
Source
Escherichia Coli.
Appearance

The product appears as a clear, colorless solution that has been sterilized by filtration.

ANGPTL3 (17-460) Human

Angiopoietin-like Protein 3 (17-460 a.a.) Human Recombinant

ANGPTL3, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain with 453 amino acids (17-460 a.a.). It has a molecular mass of 52.9kDa and appears between 25-70kDa on SDS-PAGE under reducing conditions. This protein is expressed with a 6 amino acid His tag at its C-Terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9322
Source
Sf9, Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.

ANGPTL3 (243-460) Human

Angiopoietin-like Protein 3 (243-460 a.a.) Human Recombinant

Recombinant Human ANGPTL3, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 239 amino acids (243-460). It has a molecular weight of 27.7 kDa. The protein is purified using proprietary chromatographic techniques and is expressed with a 21 amino acid His-tag at the N-terminus.
Shipped with Ice Packs
Cat. No.
BT9785
Source
E.coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

ANGPTL7 Human

Angiopoietin-like Protein 7 Human Recombinant

Recombinant human ANGPTL7, produced in HEK293 cells, is a single, glycosylated polypeptide chain containing 553 amino acids (27-346a.a) with a molecular weight of 63.2kDa. It is fused to a 233 amino acid hIgG-His-Tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10609
Source

HEK293 cells.

Appearance
Sterile filtered colorless solution.

ANGPTL7 Mouse

Angiopoietin-like Protein 7 Mouse Recombinant

ANGPTL7, produced in Sf9 insect cells, is a single, glycosylated polypeptide chain containing 324 amino acids (residues 22-337) with a molecular weight of 37.5 kDa. It contains an 8 amino acid His tag at the C-terminus. This protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10692
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless, and sterile-filtered solution.

ANGPT1 Human

Angiopoietin-1 Human Recombinant

Recombinant human ANGPT1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 480 amino acids (residues 20-498). It has a molecular weight of 55.6 kDa. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9019
Source
E.coli.
Appearance
Clear, colorless solution, sterile-filtered.

ANGPTL3 Human

Angiopoietin Like Protein 3 Human Recombinant

Recombinant human ANGPTL3 is produced with an N-terminal His-Tag fusion. This His-tagged fusion protein has a molecular weight of 26kDa and consists of 207 amino acid residues from human ANGPTL3 (amino acids 26-233) and an additional 16 amino acid residues from the His-Tag (underlined).
Shipped with Ice Packs
Cat. No.
BT9862
Source
Escherichia Coli.
Definition and Classification

Angiopoietins are a family of secreted glycoproteins that play a crucial role in vascular development and angiogenesis. They are primarily involved in the maturation, stability, and remodeling of blood vessels . The angiopoietin family consists of four main members: Angiopoietin-1 (Ang1), Angiopoietin-2 (Ang2), Angiopoietin-3 (Ang3), and Angiopoietin-4 (Ang4) . These proteins act as ligands for the Tie2 receptor, a receptor tyrosine kinase predominantly expressed on endothelial cells .

Biological Properties

Key Biological Properties: Angiopoietins are characterized by their ability to regulate blood vessel formation and maintenance. Ang1 is known for promoting vessel maturation and stability, while Ang2 acts as an antagonist to Ang1, promoting vascular remodeling and destabilization .

Expression Patterns and Tissue Distribution: Ang1 is widely expressed in various tissues, including the heart, lungs, and kidneys, and is secreted by pericytes and smooth muscle cells . Ang2 is primarily expressed in the endothelium and is stored in Weibel-Palade bodies, allowing for rapid release in response to stimuli . Ang3 and Ang4 have more restricted expression patterns and are less well-characterized .

Biological Functions

Primary Biological Functions: Angiopoietins are essential for angiogenesis, the process of forming new blood vessels from pre-existing ones. Ang1 promotes endothelial cell survival, migration, and adhesion, contributing to vessel maturation and stability . Ang2, on the other hand, facilitates vascular remodeling by promoting endothelial cell apoptosis and loosening cell-cell junctions .

Role in Immune Responses and Pathogen Recognition: Angiopoietins also play a role in immune responses by regulating the permeability of blood vessels, which can influence the migration of immune cells to sites of infection or inflammation . Ang2, in particular, has been implicated in promoting inflammation by increasing vascular permeability .

Modes of Action

Mechanisms with Other Molecules and Cells: Angiopoietins interact with the Tie2 receptor to mediate their effects. Ang1 binding to Tie2 leads to receptor dimerization and autophosphorylation, activating downstream signaling pathways that promote cell survival and vessel stability . Ang2 can act as a competitive inhibitor of Ang1, preventing Tie2 activation and promoting vascular remodeling .

Binding Partners and Downstream Signaling Cascades: The primary binding partner for angiopoietins is the Tie2 receptor. Upon binding, Ang1 activates several downstream signaling cascades, including the PI3K/Akt and MAPK pathways, which are involved in cell survival, proliferation, and migration . Ang2, by inhibiting Tie2 activation, can disrupt these signaling pathways and promote vascular destabilization .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: The expression of angiopoietins is tightly regulated at both the transcriptional and post-transcriptional levels. Hypoxia and inflammatory cytokines can upregulate Ang2 expression, while Ang1 expression is more constitutive . Post-translational modifications, such as phosphorylation, also play a role in modulating the activity of angiopoietins .

Transcriptional Regulation and Post-Translational Modifications: Transcription factors such as HIF-1α (hypoxia-inducible factor 1-alpha) can induce the expression of Ang2 under hypoxic conditions . Additionally, proteolytic cleavage and glycosylation are post-translational modifications that can affect the stability and activity of angiopoietins .

Applications

Biomedical Research: Angiopoietins are extensively studied in the context of cancer, where they are involved in tumor angiogenesis and metastasis. Targeting angiopoietin signaling pathways is a promising strategy for developing anti-angiogenic therapies .

Diagnostic Tools: Elevated levels of Ang2 have been associated with various pathological conditions, including cancer and inflammatory diseases, making it a potential biomarker for diagnosis and prognosis .

Therapeutic Strategies: Therapeutic approaches targeting angiopoietin signaling, such as Ang2 inhibitors, are being developed to treat diseases characterized by abnormal angiogenesis, including cancer and diabetic retinopathy .

Role in the Life Cycle

Role Throughout the Life Cycle: Angiopoietins play a critical role throughout the life cycle, from embryonic development to aging. During embryogenesis, they are essential for the formation and maturation of the vascular system . In adults, they maintain vascular homeostasis and are involved in tissue repair and regeneration . Dysregulation of angiopoietin signaling is associated with various age-related diseases, including cardiovascular diseases and cancer .

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