Recombinant Human PRAME Protein

Name: Recombinant Human PRAME Protein
Brand: Beta LifeScience
SKU: BLA-7258P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Accession	P78395
Synonym	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
Description	Recombinant Human PRAME Protein was expressed in E.coli. It is a Protein fragment
Source	E.coli
AA Sequence	MNPLETLSITNCRLSEGDVMHLSQSPSVSQLSVLSLSGVMLTDVSPEPLQ ALLERASATLQDLVFDECGITDDQLLALLPSLSHCSQLTTLSFYGNSISI
Molecular Weight	11 kDa
Purity	>98% SDS-PAGE.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Lyophilised
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 at 4°C. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target 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.
Subcellular Location	Nucleus. Chromosome. Cytoplasm. Golgi apparatus. Cell membrane.
Protein Families	PRAME family
Database References	HGNC: 9336 OMIM: 606021 KEGG: hsa:23532 STRING: 9606.ENSP00000381726 UniGene: Hs.30743
Tissue Specificity	Expressed in testis. Detected in samples of kidney, brain and skin.

Gene Functions References

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
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
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
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
Tumor antigen PRAME is up-regulated by MZF1 in cooperation with DNA hypomethylation in melanoma cells. PMID: 28634046
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
PRAME plays a role in preventing the invasion and metastasis of lung adenocarcinoma PMID: 27391090
PRAME is expressed in many primary and metastatic UMs, and about half of the metastatic UMs coexpress PRAME and HLA class I. PMID: 28448663
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
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
This study demonstrates that PRAME functions as a tumor suppressor in breast cancer. PMID: 27632898
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
Leukemias expressing high levels of PRAME had higher levels of cell death by regulating S100A4/p53 signaling. PMID: 27049257
Our results suggest that the leukemias expressing high levels of PRAME has favorable prognosis PMID: 26823776
PRAME expression is considered as a poor prognostic parameter in HL. PMID: 26044287
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
This study shows the prognostic significance of PRAME expression in diffuse large B-cell lymphoma patients treated with R-CHOP therapy. PMID: 24820636
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
elevated PRAME expression in head and neck squamous cell carcinoma PMID: 23905893
PRAME and WT1 transcripts constitute a good molecular marker combination for monitoring minimal residual disease in MDS. PMID: 23110703
PRAME impairs differentiation and increases proliferation likely via blocking retinoic acid receptor signaling. PMID: 23444226
PRAME is upregulated by signalling pathways that are activated in response to infection/inflammation. PMID: 23460923
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
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
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
Knock-down of PRAME increases retinoic acid signaling and cytotoxic drug sensitivity of Hodgkin lymphoma cells. PMID: 23409080
a novel link between the oncoprotein PRAME and the conserved EKC complex PMID: 22912744
PRAME as biomarkers for solid tumor PMID: 23075240
NYESO-1/LAGE-1s and PRAME are targets for antigen specific T cells in chondrosarcoma following treatment with 5-Aza-2-deoxycitabine PMID: 22384167
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
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
these results suggest that PRAME plays an important role in cell proliferation and disease progression in osteosarcoma. PMID: 22390931
the expansion of the PRAME family occurred in both autosomes and sex chromosomes PMID: 21347312
PRAME effectively differentiates mullerian carcinoma from malignant mesothelioma at the mRNA and protein levels. PMID: 22261449
PRAME expression might be related to distinct patterns of tumorigenesis PMID: 21691740
PRAME plays an important role in disease progression in acute leukemia. PMID: 21550659
The authors applied protein-complex purification strategies and identified PRAME as a substrate recognition subunit of a Cullin2-based E3 ubiquitin ligase. PMID: 21822215
The level of prame gene transcript increases in chronic myeloid leukemia which associates with disease progression. PMID: 20723287
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
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
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
The PRAME transcript was highly expressed in acute myeloid leukemia patients and was a favorable marker of prognosis. PMID: 20376794
PRAME mRNA could be used to monitor minimal residual disease in newly diagnosed acute myeloid leukemia patients. PMID: 19035174
E2F4, PHACTR3, PRAME family member and CDH12 most probably play important role in non-small-cell lung cancer geneses PMID: 19473719
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
PRAME gene expression in childhood acute lymphoblastic leukemia PMID: 12419593
PRAME is highly expressed in primary advanced neuroblastoma PMID: 15240516
The overexpression of PRAME protein frequently observed in human cancers confers growth or survival advantages by antagonizing retinoic acid receptor(RAR) signaling. PMID: 16179254
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
PRAME is expressed in acute myeloblastic leukaemia PMID: 16681423

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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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