Recombinant Proteins

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PFN1 Human

Profilin-1 Human Recombinant

Recombinant human PFN1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 140 amino acids (1-140 a.a.). It has a molecular mass of 15 kDa. The purification of PFN1 is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7175
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless solution that has been filtered for sterility.

PFN1 Rat

Profilin-1 Rat Recombinant

Recombinant rat PFN1, produced in E. coli, is a single polypeptide chain that lacks glycosylation. It comprises 164 amino acids (specifically, amino acids 1 to 140) and has a molecular weight of 17.5 kDa. A 24-amino acid His-tag is fused to the N-terminus of PFN1. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7258
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

PFN2 Human

Profilin-2 Human Recombinant

Recombinant human PFN2, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 160 amino acids (including a 20 amino acid His-tag at the N-terminus, spanning residues 1-140 of the PFN2 sequence). With a molecular weight of 17.2 kDa, the protein has been purified using standard chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7329
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless solution that has been filtered.

PFN4 Human

Profilin-4 Human Recombinant

Recombinant human PFN4, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 149 amino acids (residues 1-129) with a molecular weight of 16.4 kDa. The protein includes a 20 amino acid His tag at the N-terminus and is purified using standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT7396
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.
Definition and Classification

Profilin is a small actin-binding protein found in most eukaryotic organisms. It plays a crucial role in the dynamic turnover and reconstruction of the actin cytoskeleton, which is essential for cellular locomotion and shape changes . Profilins are classified based on their molecular weight, which ranges from 14 to 19 kDa . In mammals, there are four isoforms of profilin: profilin-I, profilin-II, profilin-III, and profilin-IV .

Biological Properties

Profilin is ubiquitously expressed in eukaryotic cells and is involved in various cellular processes. It is predominantly found in tissues such as the brain and kidney . Profilin binds to monomeric actin, catalyzing the exchange of actin-bound ADP to ATP, thus promoting actin polymerization . It also interacts with polyphosphoinositides and proline-rich domains in proteins, linking it to signaling pathways between the cell membrane and the cytoskeleton .

Biological Functions

Profilin’s primary function is to regulate actin polymerization, which is vital for cell motility, cytokinesis, and membrane trafficking . It also plays a role in immune responses by facilitating the hunting down of infectious intruders by immune cells . Profilin is essential for host cell invasion by pathogens such as Toxoplasma gondii, where it acts as a pathogen-associated molecular pattern recognized by toll-like receptors .

Modes of Action

Profilin interacts with various molecules and cells through its binding partners, including actin, polyphosphoinositides, and proline-rich proteins . It enhances actin growth by binding to monomeric actin and catalyzing nucleotide exchange, converting ADP-actin to ATP-actin . Profilin-actin complexes are then fed into growing actin polymers by proteins such as formin and vasodilator-stimulated phosphoprotein . This mode of action is crucial for rapid actin polymerization and cellular functions .

Regulatory Mechanisms

The expression and activity of profilin are regulated at multiple levels. Transcriptional regulation involves various signaling pathways that control profilin gene expression . Post-translational modifications, such as phosphorylation, also play a role in modulating profilin’s activity and interactions with other proteins . Changes in profilin expression levels can impact cellular processes and are associated with various pathologies, including cancer .

Applications

Profilin has significant applications in biomedical research, particularly in studying actin dynamics and cell motility . It is also used as a diagnostic tool for certain allergies, as profilin is a major allergen in birch, grass, and other pollen . Therapeutically, targeting profilin interactions and functions holds potential for treating diseases related to actin dysregulation, such as cancer and neurodegenerative disorders .

Role in the Life Cycle

Profilin plays a vital role throughout the life cycle, from development to aging and disease . During development, profilin is essential for processes such as organ development and wound healing . In aging, changes in profilin expression and function can contribute to age-related diseases and conditions . Profilin’s involvement in various cellular processes makes it a critical protein for maintaining cellular health and function throughout life .

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