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

Beta LifeScience SKU/CAT #: BLC-02350P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

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

Beta LifeScience SKU/CAT #: BLC-02350P
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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
Associated Diseases Amyotrophic lateral sclerosis 18 (ALS18)
Tissue Specificity Expressed in epididymis (at protein level).

Gene Functions References

  1. Variants of rs238243 and rs238238 might regulate profilin1 expression by epigenetic modification and indirectly affects the susceptible threshold of hypertension in Chinese Han population. PMID: 28541412
  2. Results suggested that the RhoA/ROCK1 pathway activated by excessive ROS is responsible for profilin-1-mediated endothelial damage. PMID: 29849894
  3. 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
  4. 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
  5. Guttiferone K effectively suppresses the motility and metastasis of hepatocellular carcinoma cells mainly by restoration of aberrantly reduced PFN1 protein expression PMID: 27494863
  6. Results collectively suggest that PFN1 promotes cell migration and adhesion in bladder cancer models. PMID: 27683119
  7. 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
  8. 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
  9. 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
  10. 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
  11. this study shows that in pancreatic cancer patients, PFN1 expression is substantially decreased in peripheral CD8(+) T cells PMID: 28688208
  12. mutant profilin1 in various diseases with an emphasis on its contribution to the pathogenesis of amyotrophic lateral sclerosis (Review) PMID: 27669692
  13. 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
  14. novel profilin-1 variants associated with amyotrophic lateral sclerosis PMID: 27101547
  15. 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
  16. 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
  17. 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
  18. 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
  19. Gain-of-toxic-function PFN1 gene mutation leads to conformational change of TDP-43 and to neurodegeneration in amyotrophic lateral sclerosis. PMID: 26908597
  20. 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
  21. 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
  22. evidence, which suggests that Profilin increases tumour suppressor activity by regulating NF-kappaB. PMID: 26787927
  23. Profilin-1 folding process occurs in the absence of thermodynamically stable partially folded states. PMID: 26227615
  24. Actin independent mechanisms contribute to the pathogenicity of PFN1 T109M and possibly other PFN1 mutations. PMID: 26572741
  25. 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
  26. PFN1 is a rare cause of ALS. PMID: 25499087
  27. findings suggest that a destabilized form of PFN1 underlies PFN1-mediated ALS pathogenesis PMID: 26056300
  28. 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
  29. Data indicated that No PFN1 mutations were identified in the Catalan population with amyotrophic lateral sclerosis. PMID: 25249294
  30. 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
  31. 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
  32. 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
  33. Pfn1 is a tumor suppressor in pancreatic cancer that acts via a novel mechanism of regulating the SIRT3-HIF1alpha axis. PMID: 25103363
  34. Higher messenger RNA expression of Profilin-1 is associated with significantly lower survival PMID: 25704627
  35. the exchange of bound actin between Tbeta4 and profilin involves both steric and allosteric components. PMID: 25313062
  36. 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
  37. This review summarize the PFN1 most recently discovered 'high risk' genes in ALS. PMID: 24780888
  38. association of cortactin with Pfn-1 is regulated by c-Abl-mediated cortactin phosphorylation PMID: 24700464
  39. Raising the intracellular levels of Profilin I decreased the mobile fraction ratio of actin filaments and slowed their polymerization rate. PMID: 24465723
  40. In glioblastomas endothelial cell-specific Pfn-1 phosphorylation elevates HIF-1alpha expression leading to vascular abnormalities and tumor progression. PMID: 24747440
  41. 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
  42. CHIP regulates Pfn1 levels as an E3 ligase, and possibly plays a role in cell migration and metastasis of breast cancer. PMID: 24661873
  43. Data indicate that lower profilin1 (Pfn1) expression is associated with increased metastatic potential in breast cancer. PMID: 23686314
  44. PFN1 mutations were identified in autosomal dominant FALS patients. PMID: 24085347
  45. 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
  46. 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
  47. up-regulation of profilin1 facilitated apoptosis and repressed autophagy induced by irradiation. PMID: 23826918
  48. PFN1 mutations lead to ubiquitin-positive inclusions and impairment of cytoskeletal pathways, in which, a pathophysioloy of familial and sporadic ALS lays. PMID: 23635659
  49. 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
  50. 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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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