Recombinant Human Profilin-1 (PFN1) Protein (GST)

Name: Recombinant Human Profilin-1 (PFN1) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-02350P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Profilin-1 (PFN1) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P07737
Target Symbol	PFN1
Synonyms	Actin binding protein ; ALS18; Epididymis tissue protein Li 184a; OTTHUMP00000125244; PFN 1; Pfn; PFN1; PROF1_HUMAN; Profilin I; Profilin-1; Profilin1; ProfilinI
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	AGWNAYIDNLMADGTCQDAAIVGYKDSPSVWAAVPGKTFVNITPAEVGVLVGKDRSSFYVNGLTLGGQKCSVIRDSLLQDGEFSMDLRTKSTGGAPTFNVTVTKTDKTLVLLMGKEGVHGGLINKKCYEMASHLRRSQY
Expression Range	2-140aa
Protein Length	Full Length of Mature Protein
Mol. Weight	41.9kDa
Research Area	Neuroscience
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR.
Subcellular Location	Cytoplasm, cytoskeleton.
Protein Families	Profilin family
Database References	HGNC: 8881 OMIM: 176610 KEGG: hsa:5216 STRING: 9606.ENSP00000225655 UniGene: PMID: 28541412 Results suggested that the RhoA/ROCK1 pathway activated by excessive ROS is responsible for profilin-1-mediated endothelial damage. PMID: 29849894 PFN1 could promote autophagy through taking part in Beclin1 complex and contribute to bortezomib resistance, which may become a novel molecular target in the therapy of MM. PMID: 29945297 Loss of PFN1 in tumor cells has been associated with lymph node invasion and metastasis in other tumor types, strengthening the argument that the protein has the potential to be a tumor suppressor in late-stage oral squamous cell carcinoma. PMID: 27862305 Guttiferone K effectively suppresses the motility and metastasis of hepatocellular carcinoma cells mainly by restoration of aberrantly reduced PFN1 protein expression PMID: 27494863 Results collectively suggest that PFN1 promotes cell migration and adhesion in bladder cancer models. PMID: 27683119 These results suggest that although mutant PFN1 aggregation may contribute to neurodegeneration, it does not trigger its onset. Importantly, these experiments establish a progressive disease model that can contribute toward identifying the mechanisms of ALS pathogenesis and the development of therapeutic treatments. PMID: 27681617 One potential mechanism for C71G-PFN1 to initiate Amyotrophic lateral sclerosis might be the abnormal interaction with membranes as recently established for SOD1 mutants. PMID: 28847504 Expression of PFN1 mutants induces accumulation of TDP-43, and promotes conversion of normal TDP-43 into an abnormal form. These results provide new insight into the mechanisms of TDP-43 proteinopathies and other diseases associated with amyloid-like protein deposition. PMID: 27432186 We suggest that reduction of PFN-1 expression by elevated levels of PrP(c) may contribute to protective effects PrP(c)-overexpressing SH-SY5Y cells confer against STS-induced apoptosis PMID: 28102851 this study shows that in pancreatic cancer patients, PFN1 expression is substantially decreased in peripheral CD8(+) T cells PMID: 28688208 mutant profilin1 in various diseases with an emphasis on its contribution to the pathogenesis of amyotrophic lateral sclerosis (Review) PMID: 27669692 Data suggest 2 major isoforms of profilin (Pfn1 and Pfn2) are co-regulated by a common mechanism involving the action of MKL1 [megakaryoblastic leukemia (translocation) 1 protein] that is independent of its SRF- (serum-response factor)-related activity; cellular externalization of Pfn1, rather than transcription, is affected by the perturbations of MKL1; MKL1 can influence cell migration by modulating Pfn1 expression. PMID: 28546428 novel profilin-1 variants associated with amyotrophic lateral sclerosis PMID: 27101547 We found that ARP3 and profilin1 were 2 binding partners of LMO2, primarily in cytoplasm. LMO2. LMO2 mediated the assembly of a complex including ARP3, profilin1, and actin monomer, increased actin monomer binding to profilin1, and promoted lamellipodia/filopodia formation in basal-type breast cancer cells. PMID: 28170369 These observations indicate that our novel profilin1 mutant mouse line may provide a new ALS model with the opportunity to gain unique perspectives into mechanisms of neurodegeneration that contribute to ALS pathogenesis. PMID: 28040732 These data suggest that Familial Amyotrophic Lateral Sclerosis-linked PFN1 mutations exacerbate TDP-43-induced neurodegeneration in a gain-of-function manner, possibly by shifting the localization of TDP-43 from nuclei to cytoplasm. PMID: 27634045 Homo-oligomerization of the actin-binding protein PFN1 has been characterized by the relaxation dispersion profiles of the protein as a function of concentration. PMID: 28052669 Gain-of-toxic-function PFN1 gene mutation leads to conformational change of TDP-43 and to neurodegeneration in amyotrophic lateral sclerosis. PMID: 26908597 Profilin synergizes with chemotherapeutic drugs to induce tumor cell death by regulating NF-kappaB and p53. Thus, modulation of Profilin may be a useful strategy for effective combination therapy. PMID: 26842845 Mutations of profilin-1, associated with familial amyotrophic lateral sclerosis, increase the tendency of profilin-1 to aggregate and that such aggregation behavior is largely determined by the mutation-induced structural changes occurring in the folded state of the protein. PMID: 26226631 evidence, which suggests that Profilin increases tumour suppressor activity by regulating NF-kappaB. PMID: 26787927 Profilin-1 folding process occurs in the absence of thermodynamically stable partially folded states. PMID: 26227615 Actin independent mechanisms contribute to the pathogenicity of PFN1 T109M and possibly other PFN1 mutations. PMID: 26572741 expression of the ALS-associated actin-binding deficient mutant of PFN1 (PFN1(C71G)) results in increased dendritic arborisation and spine formation, and cytoplasmic inclusions in cultured mouse hippocampal neurons PMID: 26499959 PFN1 is a rare cause of ALS. PMID: 25499087 findings suggest that a destabilized form of PFN1 underlies PFN1-mediated ALS pathogenesis PMID: 26056300 Suggest that PFN1 plays a critical role in gastric carcinoma progression, and these effects are likely mediated through the integrin beta1/FAK pathway. PMID: 25741138 Data indicated that No PFN1 mutations were identified in the Catalan population with amyotrophic lateral sclerosis. PMID: 25249294 Profilin-1 overexpression in MDA-MB-231 breast cancer cells is associated with alterations in proteomics biomarkers of cell proliferation, survival, and motility as revealed by global proteomics analyses PMID: 25454514 Profilin1 acts as a molecular regulator of the levels of PI(3,4)P2 and Tks5 recruitment in invadopodia to control the invasion efficiency of invadopodia. PMID: 25613364 Collective expression pattern of tensin/profilin-1/villin-1/talin could be a biomarker to estimate the prognosis of esophageal squamous cell carcinoma patients. PMID: 25337239 Pfn1 is a tumor suppressor in pancreatic cancer that acts via a novel mechanism of regulating the SIRT3-HIF1alpha axis. PMID: 25103363 Higher messenger RNA expression of Profilin-1 is associated with significantly lower survival PMID: 25704627 the exchange of bound actin between Tbeta4 and profilin involves both steric and allosteric components. PMID: 25313062 effects of profilin-1 and profilin-2, the two major isoforms of profilin, on actin cytoskeletal regulation, motility, and invasion of breast cancer cells PMID: 23827010 This review summarize the PFN1 most recently discovered 'high risk' genes in ALS. PMID: 24780888 association of cortactin with Pfn-1 is regulated by c-Abl-mediated cortactin phosphorylation PMID: 24700464 Raising the intracellular levels of Profilin I decreased the mobile fraction ratio of actin filaments and slowed their polymerization rate. PMID: 24465723 In glioblastomas endothelial cell-specific Pfn-1 phosphorylation elevates HIF-1alpha expression leading to vascular abnormalities and tumor progression. PMID: 24747440 The ALS-linked mutations in profilin 1 alter stress granule dynamics, providing further evidence for the potential role of stress granules in ALS pathogenesis. PMID: 24920614 CHIP regulates Pfn1 levels as an E3 ligase, and possibly plays a role in cell migration and metastasis of breast cancer. PMID: 24661873 Data indicate that lower profilin1 (Pfn1) expression is associated with increased metastatic potential in breast cancer. PMID: 23686314 PFN1 mutations were identified in autosomal dominant FALS patients. PMID: 24085347 Profilin-1 might act as an ultimate and common cellular effector in the process of metabolic memory (endothelial abnormalities) mediated by AGEs via the ROS/PKC or ROS/NF-B signalling pathways. PMID: 24090212 Wanted to identify estrogen receptor alpha (ERalpha) interacting proteins in Tamoxifen treated MCF7 cells. Using a GST-pull down assay with ERalpha ligand-binding domain and MS-based proteomics approach we identified Profilin1 as a novel ERalpha interacting protein. PMID: 23576398 up-regulation of profilin1 facilitated apoptosis and repressed autophagy induced by irradiation. PMID: 23826918 PFN1 mutations lead to ubiquitin-positive inclusions and impairment of cytoskeletal pathways, in which, a pathophysioloy of familial and sporadic ALS lays. PMID: 23635659 The single nucleotide polymorphism (SNP) rs13204 of the PFN1 gene has an important function in the development of amyotrophic lateral sclerosis in Han Chinese. PMID: 23428184 PFN1 mutations are not a common cause of frontotemporal lobar degeneration and amyotrophic lateral sclerosis in this cohort of patients from France. PMID: 23182804

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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