Recombinant Human Melanoma antigen preferentially expressed in tumors (PRAME)

Code CSB-BP018603HU
MSDS
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Source Baculovirus
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Code CSB-EP018603HU-B
MSDS
Size Pls inquire
Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-MP018603HU
MSDS
Size Pls inquire
Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
PRAME
Uniprot No.
Research Area
Apoptosis
Alternative Names
4930534P07Rik; Cancer/testis antigen 130; CT130; MAPE; Melanoma antigen preferentially expressed in tumors; OIP 4; OIP-4; OIP4 ; OPA interacting protein 4; Opa interacting protein OIP4; OPA-interacting protein 4; PRAME; PRAME_HUMAN; Preferentially expressed antigen in melanoma ; Preferentially expressed antigen of melanoma; RP23-250F8.3
Species
Homo sapiens (Human)
Expression Region
1-509aa
Target Protein Sequence
MERRRLWGSIQSRYISMSVWTSPRRLVELAGQSLLKDEALAIAALELLPRELFPPLFMAAFDGRHSQTLKAMVQAWPFTCLPLGVLMKGQHLHLETFKAVLDGLDVLLAQEVRPRRWKLQVLDLRKNSHQDFWTVWSGNRASLYSFPEPEAAQPMTKKRKVDGLSTEAEQPFIPVEVLVDLFLKEGACDELFSYLIEKVKRKKNVLRLCCKKLKIFAMPMQDIKMILKMVQLDSIEDLEVTCTWKLPTLAKFSPYLGQMINLRRLLLSHIHASSYISPEKEEQYIAQFTSQFLSLQCLQALYVDSLFFLRGRLDQLLRHVMNPLETLSITNCRLSEGDVMHLSQSPSVSQLSVLSLSGVMLTDVSPEPLQALLERASATLQDLVFDECGITDDQLLALLPSLSHCSQLTTLSFYGNSISISALQSLLQHLIGLSNLTHVLYPVPLESYEDIHGTLHLERLAYLHARLRELLCELGRPSMVWLSANPCPHCGDRTFYDPEPILCPCFMPN
Mol. Weight
59.9kD
Protein Length
Full length
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4? for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex, which mediates ubiquitination of target proteins, leading to their degradation. The CRL2(PRAME) complex mediates ubiquitination and degradation of truncated MSRB1/SEPX1 selenoproteins produced by failed UGA/Sec decoding. In the nucleus, the CRL2(PRAME) complex is recruited to epigenetically and transcriptionally active promoter regions bound by nuclear transcription factor Y (NFY) and probably plays a role in chromstin regulation. Functions as a transcriptional repressor, inhibiting the signaling of retinoic acid through the retinoic acid receptors RARA, RARB and RARG: prevents retinoic acid-induced cell proliferation arrest, differentiation and apoptosis.
Gene References into Functions
  1. Knockdown PRAME in HCC cells, increased cell apoptosis was correlated with the proportion of cells in G0/G1 stage, activated p53 mediated apoptosis, and increased cyclin p21 expression. PMID: 29439259
  2. PRAME is frequently expressed in epithelial ovarian cancer at the mRNA and protein levels, and DNA methylation is a key mechanism regulating its expression. PMID: 27322684
  3. PRAME is aberrantly hypomethylated and activated in Class 1 and Class 2 uveal melanomas and is associated with increased metastatic risk in both classes PMID: 27486988
  4. To investigate the impact of gene copy number variation on PRAME expression, plasma cells were sorted from 50 newly diagnosed multiple myeloma patients and 8 healthy volunteers to measure PRAME transcript levels and gene copy numbers by real-time quantitative polymerase chain reaction. PMID: 28953414
  5. Tumor antigen PRAME is up-regulated by MZF1 in cooperation with DNA hypomethylation in melanoma cells. PMID: 28634046
  6. Results support the potential utility of NY-ESO-1, PRAME, and MAGEA4 as targets for immunotherapy and as ancillary prognostic parameters in synovial sarcomas. PMID: 27993576
  7. PRAME plays a role in preventing the invasion and metastasis of lung adenocarcinoma PMID: 27391090
  8. PRAME is expressed in many primary and metastatic UMs, and about half of the metastatic UMs coexpress PRAME and HLA class I. PMID: 28448663
  9. PRAME is a downstream factor of SOX17 and LIN28 in regulating pluripotency and suppressing somatic/germ cell differentiation in primordial germ cells, germ cell neoplasia in situ, and seminomas. PMID: 27441500
  10. In line with its roles in controlling cell growth, RPAME regulates multiple critical cell-growth related genes, including IGF1R oncogene. IGF1R up-regulation contributes to increase of cell growth upon the knockdown of PRAME. PMID: 27241212
  11. This study demonstrates that PRAME functions as a tumor suppressor in breast cancer. PMID: 27632898
  12. PRAME is an independent prognostic biomarker in Uveal melanoma , which identifies increased metastatic risk in patients with Class 1 or disomy 3 tumors. PMID: 26933176
  13. Leukemias expressing high levels of PRAME had higher levels of cell death by regulating S100A4/p53 signaling. PMID: 27049257
  14. Our results suggest that the leukemias expressing high levels of PRAME has favorable prognosis PMID: 26823776
  15. PRAME expression is considered as a poor prognostic parameter in HL. PMID: 26044287
  16. PRAME immunoreactivity in myeloid leukemia (ML) of Down syndrome (DS) is largely due to the non-blast components, while PRAME immunoreactivity in blasts of Transient abnormal myelopoiesis (TAM) is not restricted to cases that progress to ML of DS. PMID: 25887863
  17. This study shows the prognostic significance of PRAME expression in diffuse large B-cell lymphoma patients treated with R-CHOP therapy. PMID: 24820636
  18. results suggested that PRAME was a predictor for better outcome, could be a useful target for immunotherapy, and might represent a candidate marker for the monitoring of minimal residual disease PMID: 24600975
  19. elevated PRAME expression in head and neck squamous cell carcinoma PMID: 23905893
  20. PRAME and WT1 transcripts constitute a good molecular marker combination for monitoring minimal residual disease in MDS. PMID: 23110703
  21. PRAME impairs differentiation and increases proliferation likely via blocking retinoic acid receptor signaling. PMID: 23444226
  22. PRAME is upregulated by signalling pathways that are activated in response to infection/inflammation. PMID: 23460923
  23. The complex PRAME/EZH2 is able to repress TRAIL expression, in a cancer-specific manner; inhibition of PRAME/EZH2 releases apoptosis-mediating TRAIL. (Review) PMID: 23228130
  24. PRAME and its paralogs are leucine rich repeat proteins. Structure predictions suggest PRAME resembles the extracellular domains of TLR3 and TLR4, or intracellular NALP family. This suggests PRAME may have a role in sensing Pathogen Associated Molecular Patterns (PAMPs). PMID: 23460923
  25. PRAME expression in leukaemic cell lines is upregulated by IFN gamma and LPS, suggesting a possible role in immune responses. PRAME associates with Elongin BC complexes by binding Elongin C, and co-localises to the Golgi network. Nuclear PRAME interacts with Histone H3. The results suggest that PRAME has dual roles in gene regulation in the nucleus and protein turnover trafficking in the Golgi PMID: 23460923
  26. Knock-down of PRAME increases retinoic acid signaling and cytotoxic drug sensitivity of Hodgkin lymphoma cells. PMID: 23409080
  27. a novel link between the oncoprotein PRAME and the conserved EKC complex PMID: 22912744
  28. PRAME as biomarkers for solid tumor PMID: 23075240
  29. NYESO-1/LAGE-1s and PRAME are targets for antigen specific T cells in chondrosarcoma following treatment with 5-Aza-2-deoxycitabine PMID: 22384167
  30. PRAME expression is regulated at the epigenetic level. For this reason inhibitors of DNA methylation, such as 5-azacytidine, can modulate the expression of this tumor associated antigen. PMID: 22503131
  31. Studies suggest that activated human gammadelta T cells can efficiently present PRAME and STEAP1-derived epitopes and allow breaking tolerance against these tumor-associated self-antigens. PMID: 21928126
  32. these results suggest that PRAME plays an important role in cell proliferation and disease progression in osteosarcoma. PMID: 22390931
  33. the expansion of the PRAME family occurred in both autosomes and sex chromosomes PMID: 21347312
  34. PRAME effectively differentiates mullerian carcinoma from malignant mesothelioma at the mRNA and protein levels. PMID: 22261449
  35. PRAME expression might be related to distinct patterns of tumorigenesis PMID: 21691740
  36. PRAME plays an important role in disease progression in acute leukemia. PMID: 21550659
  37. The authors applied protein-complex purification strategies and identified PRAME as a substrate recognition subunit of a Cullin2-based E3 ubiquitin ligase. PMID: 21822215
  38. The level of prame gene transcript increases in chronic myeloid leukemia which associates with disease progression. PMID: 20723287
  39. The cytotoxic activity of our PRAME-specific CTLs was directed not only against leukemic blasts, but also against leukemic progenitor cells as assessed by colony-forming-inhibition assays, which have been implicated in leukemia relapse. PMID: 21278353
  40. PRAME may be involved in the tumorigenic process in a wide range of cancers, at least in part by blocking the tumor suppressor pathway mediated by TRAIL expression. PMID: 20838376
  41. Results showed the expression of MCSP and PRAME in conjunctival melanoma and benign conjunctival nevi and showed that MCSP and PRAME were differentially expressed in both and can help to differentiate the lesions diagnostically. PMID: 20805128
  42. The PRAME transcript was highly expressed in acute myeloid leukemia patients and was a favorable marker of prognosis. PMID: 20376794
  43. PRAME mRNA could be used to monitor minimal residual disease in newly diagnosed acute myeloid leukemia patients. PMID: 19035174
  44. E2F4, PHACTR3, PRAME family member and CDH12 most probably play important role in non-small-cell lung cancer geneses PMID: 19473719
  45. expression of PRAME is an indicator of favorable prognosis and could be a useful tool for monitoring minimal residual disease in childhood AML. PMID: 11943337
  46. PRAME gene expression in childhood acute lymphoblastic leukemia PMID: 12419593
  47. PRAME is highly expressed in primary advanced neuroblastoma PMID: 15240516
  48. The overexpression of PRAME protein frequently observed in human cancers confers growth or survival advantages by antagonizing retinoic acid receptor(RAR) signaling. PMID: 16179254
  49. The results suggest that the analysis of PRAME protein may contribute for the distinction between normal and leukemic cells in chronic lymphoproliferative disorders(CLD), and that PRAME may be a potential target for therapy. PMID: 16620968
  50. PRAME is expressed in acute myeloblastic leukaemia PMID: 16681423

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Subcellular Location
Nucleus. Chromosome. Cytoplasm. Golgi apparatus. Cell membrane.
Protein Families
PRAME family
Tissue Specificity
Expressed in testis. Detected in samples of kidney, brain and skin.
Database Links

HGNC: 9336

OMIM: 606021

KEGG: hsa:23532

STRING: 9606.ENSP00000381726

UniGene: Hs.30743

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