Recombinant Human Perforin Protein

Beta LifeScience SKU/CAT #: BLA-6848P

Recombinant Human Perforin Protein

Beta LifeScience SKU/CAT #: BLA-6848P
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Product Overview

Host Species Human
Accession P14222
Synonym Cytolysin FLH2 HPLH2 Lymphocyte pore-forming protein P1 PERF_HUMAN Perforin 1 perforin 1 (pore forming protein) Perforin-1 PFP PGFL PIGF PIGF-2 PLGF Pore forming protein prf1 SHGC-10760
Description Recombinant Human Perforin Protein was expressed in Wheat germ. It is a Full length protein
Source Wheat germ
Molecular Weight 85 kDa including tags
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped on dry ice. Upon delivery aliquot and store at -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function Pore-forming protein that plays a key role in secretory granule-dependent cell death, and in defense against virus-infected or neoplastic cells. Plays an important role in killing other cells that are recognized as non-self by the immune system, e.g. in transplant rejection or some forms of autoimmune disease. Can insert into the membrane of target cells in its calcium-bound form, oligomerize and form large pores. Promotes cytolysis and apoptosis of target cells by facilitating the uptake of cytotoxic granzymes.
Subcellular Location Cytolytic granule. Secreted. Cell membrane; Multi-pass membrane protein. Endosome lumen.
Protein Families Complement C6/C7/C8/C9 family
Database References
Associated Diseases Familial hemophagocytic lymphohistiocytosis 2 (FHL2)

Gene Functions References

  1. Perforin binds to membranes and undergoes substantial structural re-arrangement to form pores that enable diffusion of granzyme into the target cell [Review]. PMID: 28757431
  2. findings show that N-linked glycosylation of the perforin C-terminus at Asn549 within the endoplasmic reticulum inhibits oligomerisation of perforin monomers and protects the host cell from premature pore formation; studies reveal a post-translational regulatory mechanism essential for maintaining perforin in an inactive state until its secretion from the inhibitory acidic environment of the secretory granule PMID: 28808112
  3. Study focuses on the role of perforin in both protecting and promoting human disease. It concludes with a novel hypothesis that diversity observed in the PRF1 gene may be an example of selective advantage that protects an individual from perforin-mediated pathology, such as blood-brain barrier disruption. [review] PMID: 28757574
  4. Our studies suggest that although moderate levels of expression can result in partial amelioration of the hemophagocytic lymphohistiocytosis (HLH)phenotype, high levels of perforin expression per cell are required for complete correction of HLH. PMID: 27471778
  5. Findings support an association between childhood DNA methylation patterns in PRF1 and a record of severe respiratory syncytial virus bronchiolitis in infancy. PMID: 28253869
  6. our data provide the first evidence of a strict link between the absence of CD28 and the expression of perforin, which is likewise enhanced by the expression of NKG2D, within selected CD4(+) T cells from cervical cancer patients. PMID: 28087292
  7. A girl with neurological manifestations of familial hemophagocytic lymphohistiocytosis 2 had reduced perforin 1 expression and was found to be homozygous for a mutation in PRF1 at codon 637 in exon 3 (c.673C>T p.Arg225Trp). Her non-consanguineous parents were both heterozygous carriers of this mutation. PMID: 27271812
  8. Mutation in PRF1 gene is associated with hemophagocytic lymphohistiocytosis. PMID: 27781387
  9. Increased TIM3+CD8+T cells with lower perforin and granzyme B expression and higher CD95 expression in MDS patients were observed. PMID: 27846431
  10. ITP patients displayed an increased frequency of rare missense variations of the PRF1 gene PMID: 27391055
  11. The decreased expression of perforin in circulating CD3+CD8+ positive T cells is an important biomarker of damaged antitumor immunity in advanced lung cancer. PMID: 26586704
  12. Letter/Case Report: recurrent episodes of macrophage activation syndrome in peripheral spondyloarthritis with monoallelic missense mutations in PRF1. PMID: 26752080
  13. A new heterozygous mutation (c.916G>A and c.65delC) was identified as familial hemophagocytic lymphohistiocytosis type 2 causing defect. PMID: 26739415
  14. mutations result in severe chronic active Epstein-Barr virus disease PMID: 25947952
  15. mutations result in hemophagocytic lymphohistiocytosis PMID: 25975970
  16. PRF delivers granulysin and granzymes into parasite infected cells to kill the parasite. PMID: 26752517
  17. Among SLAMF4+ cells, the T cell fraction positive for perforin and granzyme B was higher in those obtained from healthy donors compared to SLE patients. PMID: 26314831
  18. elevated in the inflammatory lesions of placentas with villitis of unknown etiology PMID: 25725937
  19. monoallelic mutations of PRF1 decrease NK-cell cytotoxicity should be considered in individuals presenting with the manifestations of immune deficiency states that impinge on NK-cell cytotoxicity. PMID: 25776844
  20. Calcific aortic valve disease is characterized by increased expression of granzymes and perforin. PMID: 26897841
  21. linking PRF1 missense mutations to lymphoma susceptibility and highlighting clinical variability within families. PRF1 mutations should, therefore, be considered as a cause of several diseases disparate to HLH. PMID: 26184781
  22. identified among the key genes in circulating monocytes that were altered by exercise PMID: 26207425
  23. PRF1 mutations are associated with hemophagocytic lymphohistiocytosis. PMID: 26450956
  24. There is no association between gene polymorphisms of PRF1 gene and the susceptibility to hemophagocytic lymphohistiocytosis PMID: 26182270
  25. A wide heterogeneity was observed in the nature of perforin gene mutations in familial hemophagocytic lymphohistiocytosis patients in India. PMID: 25577959
  26. Synthetic consensus HIV-1 DNA induces potent cellular immune responses and synthesis of granzyme B, perforin in HIV infected individuals. PMID: 25531694
  27. analysis of the differential expression by sex of perforin in relapsed multiple sclerosis in CD4+ regulatory T cells PMID: 22837658
  28. The entire coding region of PRF1 was sequenced in 94 patients and 158 controls; missense variations leading to amino acid substitutions and one nonsense variation resulting in a premature stop codon found, data suggest that PRF1 variations may influence chronic inflammatory demyelinating polyradiculoneuropathy development and course PMID: 25354579
  29. PFN appears to form arc structures on target membranes that serve as minimally disrupting conduits for GzmB translocation. PMID: 25146929
  30. Perforin expression in CD4+ and CD8+ cells is a prognostic biomarker for head and neck cancer patient survival. PMID: 25344268
  31. Defining the interaction of perforin with calcium and the phospholipid membrane. PMID: 24070258
  32. findings suggest that the g.272C>T PRF1 gene single-nucleotide variation in combination with other gene alterations could increase the risk of developing nasal NK/T-cell lymphoma, at least in a subgroup of the Spanish population PMID: 24632576
  33. This study shows variety of clinical manifestations of perforin deficiency and although the onset of hemophagocytic lymphohistiocytosis is delayed in these patients. PMID: 24390453
  34. our data indicate that the co-expression of perforin and granzyme B genes exhibits anticancer potential PMID: 24696715
  35. miR-150 is a common post-transcriptional regulator for Prf1 in mouse and human NK cells that represses NK cell lytic activity. PMID: 24698324
  36. Synergistic defects of different molecules in the cytotoxic pathway lead to clinical familial hemophagocytic lymphohistiocytosis. PMID: 24916509
  37. PRF1 is overexpressed in systemic lupus erythematosus CD4+ T cells, but expression is not linked to the typical clinical and serological parameters associated with the disease. PMID: 24238281
  38. These data show that monoallelic germline mutations of PRF1 are frequent in patients with childhood anaplastic large cell lymphoma, suggesting that partially impaired cytotoxic machinery may represent a predisposing factor for it. PMID: 24309606
  39. Exome sequencing identified a biallelic perforin1 mutation (PRF1; p.R225W) previously associated with familial hemophagocytic lymphohistiocytosis. PMID: 23443029
  40. Data suggest that acidic pH microenvironment of natural killer (NK) cells enhances Cryptococcus-induced perforin degranulation suggesting that perforin degranulation is involved in the greater immunologic cytotoxic activity of NK cells in acidic pH. PMID: 23853583
  41. The increased percentage of CD3(-)CD56(dim) NK cells expressing perforin in patients affected by the progressive forms of MS suggests a possible role of this NK cell subpopulation in the pathogenesis of the disease. PMID: 24157130
  42. Perforin I polymorphism is associated with graft rejection in kidney transplant recipients. PMID: 23528102
  43. Missense mutations of Perforin codon His222 may lead to intrauterine presentation of familial hemophagocytic lymphohistiocytosis PMID: 23073042
  44. Calculated stability (free energy) changes show that the mutations mainly destabilize the protein structure, interestingly however, A91V polymorphism, leads to a more stable one. PMID: 23592409
  45. The mRNA and protein expression of perforin significantly increases in CD4(+) and CD8(+) T cells treated with 5-azaC, which is associated with DNA hypomethylation of perforin promoter in T cells. PMID: 17213580
  46. This study defines the final sequence of events controlling cytotoxic lymphocyte immune defense, in which perforin pores assemble on the target cell plasma membrane, ensuring efficient delivery of lethal granzymes. PMID: 23377437
  47. Chlamydia trachomatis-infected tissues have significantly higher numbers of CD3 and CD8 T cells compared to non-infected tissues (p<0.01), and that the majority of CD8+ cells do not express perforin in situ. PMID: 23216954
  48. FCgammaR3A and PRF1 may participate in the pathogenesis and progression of primary biliary cirrhosis. PMID: 23179144
  49. Distinct severity of HLH in both human and murine mutants with complete loss of cytotoxic effector PRF1, RAB27A, and STX11. PMID: 23160464
  50. study identified a common PRF1 haplotype in unrelated families with atypical presentation of Familial hemophagocytic lymphohistiocytosis type 2 in Colombia PMID: 22437823


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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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