PFN1 Human

Profilin-1 Human Recombinant
Cat. No.
BT7175
Source
Escherichia Coli.
Synonyms
Profilin-1, Profilin I, PFN1.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

PFN1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 140 amino acids (1-140 a.a.) and having a molecular mass of 15kDa.
The PFN1 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Profilin1 (PFN1), a member of the profilin family, is a ubiquitous actin monomer-binding protein. It plays a significant role in promoting skin wound healing both in vitro and in vivo, potentially through the mediation of purinergic receptors. PFN1 is also involved in endothelial cell migration and vessel sprouting. It is believed to regulate actin polymerization in response to extracellular signals, binding to actin and influencing cytoskeleton formation. Furthermore, PFN1 plays a crucial role in regulating epithelial cell-cell adhesion. At high concentrations, profilin prevents actin polymerization, while at low concentrations, it enhances it. Deletion of the PFN1 gene is associated with Miller-Dieker syndrome.
Description
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.
Physical Appearance
The product is a sterile, colorless solution that has been filtered for sterility.
Formulation
The PFN1 protein solution is supplied in a 20mM Tris-HCl buffer with a pH of 8.0 and contains 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product should be kept at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To ensure stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is advisable. It is important to avoid repeated cycles of freezing and thawing.
Purity
The purity of the product is greater than 95.0% as determined by SDS-PAGE analysis.
Synonyms
Profilin-1, Profilin I, PFN1.
Source
Escherichia Coli.
Amino Acid Sequence
MAGWNAYIDN LMADGTCQDA AIVGYKDSPS VWAAVPGKTF VNITPAEVGV LVGKDRSSFY VNGLTLGGQK CSVIRDSLLQ DGEFSMDLRT KSTGGAPTFN VTVTKTDKTL VLLMGKEGVH GGLINKKCYE MASHLRRSQY.

Product Science Overview

Structure and Function

Profilin-1 binds to actin monomers (G-actin) and promotes the exchange of ADP for ATP, which is necessary for actin polymerization. This interaction is critical for the dynamic remodeling of the actin cytoskeleton, which is essential for various cellular functions such as cell motility, division, and intracellular transport .

Pathological Conditions

Under pathological conditions, such as diabetes, the levels of Profilin-1 are increased in the vascular endothelium. Elevated levels of Profilin-1 have been associated with endothelial dysfunction and atherosclerosis. Studies have shown that Profilin-1 overexpression can trigger indicators of endothelial dysfunction downstream of LDL signaling, and attenuated expression of Profilin-1 can confer protection from atherosclerosis in vivo .

Recombinant Profilin-1

Recombinant Profilin-1 is produced using recombinant DNA technology, which involves inserting the gene encoding Profilin-1 into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of Profilin-1 for research and therapeutic purposes. Recombinant Profilin-1 has been used in various studies to investigate its role in cellular processes and its potential as a therapeutic target for diseases such as atherosclerosis .

Research and Therapeutic Potential

Research has shown that Profilin-1 expression is significantly enhanced in human atherosclerotic plaques compared to the normal vessel wall. The serum levels of Profilin-1 correlate with the degree of atherosclerosis in humans, suggesting that Profilin-1 might critically contribute to atherogenesis and may represent a novel therapeutic target . Additionally, recombinant Profilin-1 has been used to study its effects on atherogenic signaling pathways and cellular responses such as DNA synthesis and chemotaxis in vascular smooth muscle cells .

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THE BIOTEK
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