Recombinant Mouse Perforin-1 (PRF1) Protein (His)

Beta LifeScience SKU/CAT #: BLC-02995P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Mouse Perforin-1 (PRF1) Protein (His)

Beta LifeScience SKU/CAT #: BLC-02995P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description Recombinant Mouse Perforin-1 (PRF1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P10820
Target Symbol PRF1
Synonyms Prf1; Pfp; Perforin-1; P1; Cytolysin; Lymphocyte pore-forming protein
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-6His
Target Protein Sequence PCYTATRSECKQKHKFVPGVWMAGEGMDVTTLRRSGSFPVNTQRFLRPDRTCTLCKNSLMRDATQRLPVAITHWRPHSSHCQRNVAAAKVHSTEGVAREAAANINNDWRVGLDVNPRPEANMRASVAGSHSKVANFAAEKTYQDQYNFNSDTVECRMYSFRLVQKPPLHLDFKKALRALPRNFNSSTEHAYHRLISSYGTHFITAVDLGGRISVLTALRTCQLTLNGLTADEVGDCLNVEAQVSIGAQASVSSEYKACEEKKKQHKMATSFHQTYRERHVEVLGGPLDSTHDLLFGNQATPEQFSTWTASLPSNPGLVDYSLEPLHTLLEEQNPKREALRQAISHYIMSRARWQNCSRPCRSGQHKSSHDSCQCECQDSKVTNQDCCPRQRGLAHLVVSNFRAEHLWGDYTTATDAYLKVFFGGQEFRTGVVWNNNNPRWTDKMDFENVLLSTGGPLRVQVWDADYGWDDDLLGSCDRSPHSGFHEVTCELNHGRVKFSYHAKCLPHLTGGTCLEYAPQGLLGDPPGNRSGAVW
Expression Range 21-554aa
Protein Length Full Length of Mature Protein
Mol. Weight 63.9 kDa
Research Area Immunology
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 Plays a key role in secretory granule-dependent cell death, and in defense against virus-infected or neoplastic cells. 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

KEGG: mmu:18646

STRING: 10090.ENSMUSP00000041483

UniGene: PMID: 28537251

  • levetiracetam can still protect neurons with perforin knockout mice. PMID: 26454821
  • These studies indicate that CD8+ T cells against a single antigen can restrict Y. pseudotuberculosis colonization in a perforin-dependent manner, but ultimately are insufficient in their ability to provide sterilizing immunity and protect against death. PMID: 27268148
  • Furthermore, perforin production specifically by CD8 T cells was required to cause fatal edema during experimental cerebral malaria. PMID: 28264905
  • Our study suggests that perforin plays a role in dopaminergic neuron loss in PD. PMID: 28137589
  • study shows that perforin is essential to facilitate beta cell destruction in mouse models of type 1 diabetes PMID: 26446877
  • Released granzyme B induces DNA fragmentation in intraepithelial lymphocytes independently of Perforin PMID: 25750028
  • serglycin plays a critical role in the maturation of dense-core cytotoxic granules in cytotoxic lymphocytes and the trafficking and storage of perforin and granzyme B, whereas granzyme A is unaffected PMID: 26756195
  • This suggests that LPS alters UNK cell migration and activates cytotoxic granule release. PMID: 26066976
  • it is proposed that Ca(2+) binding at the weakest affinity site triggers changes in the perforin C2 domain that facilitate its interaction with lipid membranes PMID: 26306037
  • a lack of perforin and absence of the specific activation of NK cells during acute MCMV infection lead to an unleashed CD8(+) T cell response that is detrimental for the host. PMID: 25809566
  • CD8 T cells are sufficient as a sole perforin-expressing cell type to cause BBB disruption in the PIFS model. PMID: 25337791
  • The rate and proportion of donor lymphoid cell engraftment and expansion of effector memory donor T cells were significantly increased within 5 to 7 days post-bone marrow transplantation in perforin-deficient recipients, compared with wild-type. PMID: 25459639
  • Regulatory effects of perforin on glucose tolerance are mechanistically linked to the control of T-cell proliferation and cytokine production in inflamed visceral adipose tissue. PMID: 25048196
  • Perforin (and granzyme B)-dependent apoptosis increases postapoptotic necrosis and inflammation in atherosclerosis. PMID: 25398236
  • Perforin has a role in atherosclerotic plaque development. PMID: 24205352
  • Defining the interaction of perforin with calcium and the phospholipid membrane. PMID: 24070258
  • miR-150 is a common post-transcriptional regulator for Prf1 in mouse and human NK cells that represses NK cell lytic activity. PMID: 24698324
  • Perforin and granzymes have complementary roles mediating epithelial injury by NK and CD8 T cells. The prevention of experimental biliary atresia can only be achieved by inhibiting both granules. PMID: 24096050
  • Multiple roles of perforin in hampering ERBB-2 (Her-2/neu) carcinogenesis in transgenic male mice. PMID: 24790144
  • perforin preferentially delivers cationic molecules while anionic and neutral cargoes are delivered inefficiently PMID: 24558045
  • perforin's contribution to bacterial clearance in vivo is not though enhancing CD4 T cell termination of Chlamydia replication in epithelial cells PMID: 23691028
  • These findings demonstrate that perforin-mediated immunoregulation functions in trans and are consistent with a feedback model in which cytotoxic T cells control immune activation by killing dendritic cells. PMID: 23974195
  • These data suggest that perforin expression is not required for normal immune regulation. PMID: 23883515
  • Distinct severity of HLH in both human and murine mutants with complete loss of cytotoxic effector PRF1, RAB27A, and STX11. PMID: 23160464
  • Perforin facilitates viral antigen uptake by pulmonary dendritic cells by inducing apoptosis in mice with influenza infection. PMID: 22869906
  • Perforin/FasL-independent functions of hapten-primed CD8 T cells in a contact hypersensitivity model identify new functions for neutrophils in regulating effector CD8 T cell recruitment and immune responses in the skin. PMID: 22815291
  • deficiency of T-cells, NKT-cells, perforin, Fas-ligand, TNF-alpha-receptor failed to reveal significant differences in tumor development. PMID: 22212899
  • CD8+ T-cells expressing interferon gamma or perforin play antagonistic roles in heart injury in experimental Trypanosoma cruzi-elicited cardiomyopathy PMID: 22532799
  • CD4 cells expressing gamma interferon and perforin mediate protection against lethal influenza virus infection. PMID: 22491469
  • A perforin-dependent pathwy plays a role to mediate contraction of antigen-specific CD8+ and CD4+ T cells during prolonged Listeria monocytogenes infection. PMID: 22161269
  • Data show that transitional stage 1, 2 and splenic marginal zone B cells were clearly reduced after transfer of CD4+ T cells from TNFalpha-/-, IFNgamma-/-, perforin-/-, or FasLgld mice. PMID: 21966366
  • Structures that PFN oligomers form in the membrane bilayer may include arcs previously observed by electron microscopy and these unusual structures represent an incomplete mixture of plasma membrane lipid. PMID: 21931672
  • We conclude that perforin-dependent cytotoxicity has an immunoregulatory role that is distinguishable from its pathogen clearance function and limits T-cell activation in the physiologic context by suppressing antigen presentation. PMID: 21606480
  • intact C terminus and N-linked glycosylation provide accurate and efficient export of perforin from the endoplasmic reticulum to the secretory granules and are critical for cytotoxic lymphocyte survival PMID: 21658975
  • Data suggest that an interdependent relationship between parasite burden and CD8(+) T cells dictates the onset of perforin/GzmB-mediated ECM. PMID: 21525386
  • Transcription and translation products of the cytolysin gene psm-mec on the mobile genetic element SCCmec regulate Staphylococcus aureus virulence. PMID: 21304931
  • At the Prf1 locus, clear areas of reduced nucleosomal density are detected in effector CD8-positive T cells surrounding the transcription start site but not in downstream areas of the genes, during lymphocytic choriomeningitis viral infection. PMID: 21278341
  • Perforin was dispensable for efficient clearance of antigen-bearing cells from immunized mice, but only if CD95/CD95L was functional; however, there was a delay in target cell clearance in the absence of perforin. PMID: 20309009
  • Granule-bound cathepsins are essential for processing perforin to its active form, and that CatL is an important, but not exclusive, participant in this process. PMID: 20497254
  • elucidation of the mechanism of perforin pore formation by determining the X-ray crystal structure of monomeric murine perforin, together with a cryo-electron microscopy reconstruction of the entire perforin pore PMID: 21037563
  • Perforin-mediated cytotoxicity by CD8 T cells is definitively responsible for muscle injury in C protein-induced myositis (CIM) PMID: 20583106
  • Perforin deficiency attenuates inflammation and tumor growth in colitis-associated cancer. PMID: 19785028
  • Pathogenetically relevant immune reactions in proteolipid protein-overexpressing mice are TCR-dependent and mediated by the classical components of CD8+ T-cell cytotoxicity, perforin, and Gzmb. PMID: 20042681
  • role for perforin-, Fas/FasL-, and TNFR1-mediated cytotoxic pathways in down-regulation of antigen-specific T cells during persistent viral infection PMID: 11752172
  • Using perforin-knockout (PKO) mice, we have seen that the granule exocytosis pathway can play a major role in NK cell-mediated rejection of allogeneic and MHC class I-deficient BMC, depending upon the genetics of the recipient and housing conditions. PMID: 11870623
  • An intronic silencer of the mouse perforin gene. PMID: 11911476
  • the genes for perforin, the three major T cell granzymes (A-C) and IFN-gamma are differentially expressed during primary activation of naive CD8(+) T cells, kinetically and at the single-cell level PMID: 12039912
  • The immunodominance hierarchy of influenza virus-specific T(CD8+) was not greatly perturbed by the absence of either perforin or T-helper cells or by interference with B7 (CD80)-mediated signaling. PMID: 12239309
  • Perforin protein expression is severely impaired in MEF-deficient NK cells PMID: 12387738
  • FAQs

    Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

    Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

    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.

    Recently viewed