PGF1 Mouse

Placental Growth Factor-1 Mouse Recombinant

PGF1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 138 amino acids (27-158a.a.) and having a molecular mass of 15.9kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).
PGF1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28053
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered clear solution.

PLGF 2 Human, Sf9

Recombinant Human Placental Growth Factor-2, Sf9

Placenta Growth Factor-2 Human Recombinant produced in insect cells is a homodimer, glycosylated polypeptide chain containing 2 x 152 amino acids and having a total molecular mass of 44 kDa.
The PLGF-2 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28156
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

PLGF Human, HEK

Placental Growth Factor Human Recombinant

PLGF Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 21-170) containing 160 amino acids and having a molecular mass of 18.3kDa.
PLGF is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT28219
Source

HEK293 cells.

Appearance

Sterile filtered colorless solution.

PLGF Human, His

Placental Growth Factor Human Recombinant, His Tag

PLGF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 19-131) containing 123 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 13.8kDa (calculated). 

Shipped with Ice Packs
Cat. No.
BT28301
Source
Escherichia Coli.
Appearance
Filtered White lyophilized (freeze-dried) powder.

PLGF1 Human

Placental Growth Factor-1 Human Recombinant

PLGF1 Human Recombinant (21-221 a.a.) produced in E.Coli is a disulfide-linked homodimeric, non-glycosylated, polypeptide chain containing 129 amino acids and having a molecular mass of 29kDa.
The PLGF-1 Human Recombinant protein is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28356
Source
Escherichia coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

PLGF1 Human, 132 a.a.

Placental Growth Factor-1, 132 a.a. Human Recombinant

Placental Growth Factor-1 Human Recombinant produced in E.Coli is a non-glycosylated, disulfide-linked homodimer consisting of 2x132 amino acid polypeptide chains, having a total molecular mass of approximately 29.7kDa.

PLGF1 is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT28435
Source

Escherichia Coli.

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

PLGF1 Human, HEK

Placental Growth Factor-1 Human Recombinant, HEK

PLGF1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 19-149) containing 137 amino acids and having a molecular mass of 15.5kDa. PLGF1 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT28518
Source

HEK293 cells.

Appearance

Sterile Filtered colorless solution.

PLGF1 Human, Sf9

Placental Growth Factor-1 Human Recombinant, Sf9

Placenta Growth Factor-1 Human Recombinant produced in insect cells is a homodimer, glycosylated polypeptide chain containing 2 x 131 amino acids and having a total molecular mass of approximately 34 kDa.
The PLGF-1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28596
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

PLGF2 Human

Placental Growth Factor-2 Human Recombinant

Placental Growth Factor-2 Human Recombinant produced in E.Coli is a non-glycosylated, disulfide-linked homodimer consisting of 2x152 amino acid polypeptide chains, having a total molecular mass of approximately 34.6kDa.

PLGF2 is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT28658
Source

Escherichia Coli.

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

PLGF2 Human, CHO

Placental Growth Factor-2 Human Recombinant, CHO

PLGF2 Human Recombinant (19-170 a.a.) produced in CHO is a disulfide-linked homodimeric, glycosylated, polypeptide chain containing 152 amino acids and having a molecular mass of 33kDa.
The PLGF-2 Human Recombinant protein is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28736
Source
Chinese Hamster Ovary cells (CHO).
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Definition and Classification

Placental Growth Factor (PlGF) is a protein encoded by the PGF gene in humans. It belongs to the vascular endothelial growth factor (VEGF) family, which is crucial for angiogenesis and vasculogenesis, particularly during embryogenesis . PlGF is primarily expressed in the placenta but is also found in other tissues .

Biological Properties

Key Biological Properties: PlGF is a heparin-binding protein that can form homodimers and heterodimers. It binds to receptors such as FLT1/VEGFR-1 and, in some isoforms, to NRP1/neuropilin-1 and NRP2/neuropilin-2 .

Expression Patterns: PlGF is predominantly expressed in the placental trophoblast during pregnancy. It is also expressed in various tissues, including the renal medulla, cardia, pylorus, and others .

Tissue Distribution: PlGF is found in the placenta, heart, lung, thyroid, liver, skeletal muscle, and bone . Its expression is particularly high in the placenta, where it plays a significant role in fetal development .

Biological Functions

Primary Biological Functions: PlGF is involved in angiogenesis, the formation of new blood vessels from pre-existing ones. It promotes the proliferation and migration of endothelial cells . PlGF also plays a role in the recruitment and maturation of bone marrow-derived progenitors involved in the angiogenic process .

Role in Immune Responses and Pathogen Recognition: PlGF has been shown to promote the differentiation and activation of monocyte-macrophage lineage cells, which support the angiogenic stimulus .

Modes of Action

Mechanisms with Other Molecules and Cells: PlGF interacts with receptors such as FLT1/VEGFR-1 and NRP1/neuropilin-1. These interactions trigger downstream signaling cascades that promote angiogenesis and endothelial cell growth .

Binding Partners: PlGF binds to FLT1/VEGFR-1 and, in some isoforms, to NRP1/neuropilin-1 and NRP2/neuropilin-2 in a heparin-dependent manner .

Downstream Signaling Cascades: The binding of PlGF to its receptors activates signaling pathways that lead to the proliferation and migration of endothelial cells, contributing to angiogenesis .

Regulatory Mechanisms

Transcriptional Regulation: The expression of PlGF is regulated at the transcriptional level. Factors such as hypoxia can induce the expression of PlGF .

Post-Translational Modifications: PlGF is secreted as a glycosylated homodimer. Isoforms PlGF-1 and PlGF-3 are diffusible, while PlGF-2 and PlGF-4 have heparin-binding domains and remain cell membrane-associated .

Applications

Biomedical Research: PlGF is used in research to understand its role in angiogenesis and its potential therapeutic applications .

Diagnostic Tools: PlGF levels in maternal blood are used to predict and diagnose pre-eclampsia, a pregnancy complication characterized by high blood pressure and damage to other organs .

Therapeutic Strategies: PlGF is being explored as a therapeutic target for conditions such as fetal growth restriction and preeclampsia. Gene therapy approaches are being investigated to enhance PlGF expression and improve placental function .

Role in the Life Cycle

Development: PlGF plays a crucial role in embryonic development by promoting angiogenesis and vasculogenesis .

Aging and Disease: Dysregulation of PlGF expression is associated with various diseases, including pre-eclampsia and other pregnancy-related complications . PlGF is also being studied for its potential role in cardiovascular diseases and cancer .

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