Recombinant Human Major Vault Protein (MVP) Protein (His-SUMO)

Name: Recombinant Human Major Vault Protein (MVP) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09888P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Major Vault Protein (MVP) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q14764
Target Symbol	MVP
Synonyms	LRP; Lung resistance related protein; Lung resistance-related protein; Major vault protein; Major vault protein; rat; homolog of; MVP; MVP_HUMAN; testicular secretory protein Li 30; VAULT 1; VAULT1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	ATEEFIIRIPPYHYIHVLDQNSNVSRVEVGPKTYIRQDNERVLFAPMRMVTVPPRHYCTVANPVSRDAQGLVLFDVTGQVRLRHADLEIRLAQDPFPLYPGEVLEKDITPLQVVLPNTALHLKALLDFEDKDGDKVVAGDEWLFEGPGTYIPRKEVEVVEIIQATIIRQNQALRLRARKECWDRDGKERVTGEEWLVTTVGAYLPAVFEEVLDLVDAVILTEKTALHLRARRNFRDFRGVSRRTGEEWLVTVQDTEAHVPDVHEEVLGVVPITTLGPHNYCVILDPVGPDGKNQLGQKRVVKGEKSFFLQPGEQLEQGIQDVYVLSEQQGLLLRALQPLEEGEDEEKVSHQAGDHWLIRGPLEYVPSAKVEVVEERQAIPLDENEGIYVQDVKTGKVRAVIGSTYMLTQDEVLWEKELPPGVEELLNKGQDPLADRGEKDTAKSLQPLAPRNKTRVVSYRVPHNAAVQVYDYREKRARVVFGPELVSLGPEEQFTVLSLSAGRPKRPHARRALCLLLGPDFFTDVITIETADHARLQLQLAYNWHFEVNDRKDPQETAKLFSVPDFVGDACKAIASRVRGAVASVTFDDFHKNSARIIRTAVFGFETSEAKGPDGMALPRPRDQAVFPQNGLVVSSVDVQSVEPVDQRTRDALQRSVQLAIEITTNSQEAAAKHEAQRLEQEARGRLERQKILDQSEAEKARKELLELEALSMAVESTGTAKAEAESRAEAARIEGEGSVLQAKLKAQALAIETEAELQRVQKVRELELVYARAQLELEVSKAQQLAEVEVKKFKQMTEAIGPSTIRDLAVAGPEMQVKLLQSLGLKSTLITDGSTPINLFNTAFGLLGMGPEGQPLGRRVASGPSPGEGISPQSAQAPQAPGDNHVVPVLR
Expression Range	2-893aa
Protein Length	Full Length of Mature Protein
Mol. Weight	115.2kDa
Research Area	Transport
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	Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport. Down-regulates IFNG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases.
Subcellular Location	Cytoplasm. Nucleus, nuclear pore complex. Cytoplasm, perinuclear region. Note=5% found in the nuclear pore complex (PubMed:15133037). Translocates from the nucleus to the cytoplasm upon EGF treatment (PubMed:16441665).
Database References	HGNC: 7531 OMIM: 605088 KEGG: hsa:9961 STRING: 9606.ENSP00000349977 UniGene: PMID: 27664836 Knockout of MVP leads to miR-193a accumulation in the exosomal donor cells instead of exosomes, inhibiting tumour progression. PMID: 28211508 The expression levels of LRP and GSTP1 in primary epithelial ovarian cancer were the highest, followed by borderline adenoma tissues, and lowest levels in benign tumor tissues. The difference between resistant gene negative-expression and positive-expression of chemotherapy efficiency, disease free survival time, and recurrence time were statistically significant. PMID: 30313031 KIF4A promotes drug resistance of lung adenocarcinoma cells through transporting LRP-based vaults along microtubules towards the cell membrane PMID: 29204984 Major vault protein is important in the drug resistance of cancer cells, but it requires the presence of vPARP for full activity PMID: 28551640 involved in doxorubicin resistance of non-small cell lung cancer PMID: 27817195 Study found significant upregulation of MVP and BCRP whereas MRP1 and UGT1A4 were unaltered in drug resistant epilepsy brains. While upregulation of BCRP was significantly higher in mesial temporal lobe epilepsy (9.34+/-0.45; p<0.05), upregulation of MVP was significantly higher in focal cortical dysplasia (2.94+/-0.65; p<0.01). PMID: 28273590 Taxus chinensis var.-mediated downregulation of MRP1, MDR1, and LRP might contribute to the reversal of drug resistance in non-small cell lung cancer stem cells. PMID: 27706681 We believe that for the first time, genetic variants at XRCC6 and MVP genes are associated with risk of more aggressive disease, and would be taken into account when assessing the malignancy of prostate cancer PMID: 26754263 MVP genetic polymorphisms and haplotypes may not be associated with drug resistance of partial epilepsy in the Chinese Han population. PMID: 26476776 NSCLCs [ non-small cell lung cancer ] expressing P-gp [P-glycoprotein ]/LRP [ lung resistance-related protein] bear the EGFR [epidermal growth factor receptor] mutation in exon 19 or 21 easily. PMID: 26632382 The association of MVP amplification and PTEN deletion could be a potential biomarker in glioblastoma. PMID: 25869624 Bag3-MVP is an important complex that regulates a potent prosurvival signaling pathway and contributes to chemotherapy resistance in breast cancer PMID: 24997994 LDL increases ABCB1, ABCC1, and LRP expression in a human doxorubicin-resistant uterine sarcoma cell line. PMID: 25603048 Study demonstrates that vaults have a tumour-promoting potential by stabilizing EGFR/PI3K-mediated migration and survival pathways in human glioblastoma. PMID: 24243798 USF1 binding to an E-box element may be critical for basal MVP promoter activation. PMID: 24173679 hyperosmotic stress upregulates Sp1 expression levels by inhibiting ubiquitination through the activation of JNK, and the induction of Sp1 expression directly enhances MVP transcription. PMID: 23820674 the protein levels of MVP, TEP1 and vPARP are actually increased in the highergrade tumors suggesting existence of post-transcriptional regulation of vault component production. PMID: 23739867 Lung resistance-related protein is associated with malignant ascitic cells and recurrence in ovarian serous carcinoma. PMID: 23525731 The phosphorylation-dependent binding between 14-3-3epsilon and MVP inhibits the drug-resistant activity of MVP. PMID: 23590642 rs4788187, rs3815824, rs3815823 variants of the MVP gene are associated neither with predisposition for epilepsy nor with AED-resistance in the population that we have studied. PMID: 23751308 MVP and IGF-1R expression are related in oral squamous cell carcinoma and conferred reduced long-term survival in patients suffering from advanced stages of the disease PMID: 22931894 TRAIL may reduce the expression of drug-resistant genes MDR1, LRP and GST-pi, thereby participating in the reversion of the multidrug resistance of gastric cancer. PMID: 23178631 GSTP1 and LRP have different effects on multi-drug resistance in adult acute leukemia. PMID: 22391170 results suggest that the high expression of LRP in patients with tongue carcinoma indicates that intrinsic drug resistance may exist in tongue carcinoma, and is associated with tumor differentiation and cisplatin resistance in tongue carcinoma. PMID: 21793937 These findings suggest MVP as a novel player in resistance against EGFR inhibition. PMID: 22261339 MVP (major vault protein) expression increases dramatically in tissue samples from the frontal cortex of patients with surgically treated refractory epilepsy patients compared to histologically normal frontal lobe samples from controls. PMID: 21683962 LRP and MRP play a role in multidrug resistance in non-small cell lung cancer (NSCLC) and are related to prognosis in patients with NSCLC PMID: 22117969 Histopathology demonstrated increased amount of MVP/LRP proteins in cancer and showed translocation possibility between cytoplasm and nuclear envelope, which can be crucial in the prevention of nucleus against anticancer drugs. [review] PMID: 22235652 MVP is hijacked by L. monocytogenes in order to counteract the autophagy process, a finding that could have major implications in deciphering the cellular role of vault particles. PMID: 21829365 Loss of p53-related suppression of lung resistance-related protein through Y-box binding protein 1 may be the reason for LRP expression increase, and, therefore, chemotherapy resistance in tumor cells. PMID: 21344396 The nasopharyngeal carcinoma patients with positive LRP and TS expression may be less sensitive to chemotherapy with DDP + 5-FU. PMID: 15952572 Patients expressing both lung resistance protein and multidrug resistance-related protein genes had poorer outcomes and had worse 2-year survivalts. PMID: 19969624 mRNA expression predicts chemotherapy response and survival in patients with non-small cell lung cancer who received neoadjuvant cisplatin-based chemotherapy PMID: 19875192 P-gp and LRP expressions but not MRP expression are important in the mechanism of drug resistance associated with a poor clinical outcome in previously untreated non-Hodgkin's lymphoma. PMID: 19615260 Data show that major vault protein (MVP), a lung resistance associated protein, is a binding partner of YPEL4. PMID: 20555386 The expression of EGFR and LRP could be used to predict chemotherapy resistance and prognosis of ovarian cancer. PMID: 19080004 findings suggest that Tax-related drug resistance of ATL cells is due to LRP and not MDR1, as reported previously. PMID: 11937269 relationship between the expression of lung resistance-related protein (lrp) gene or multidrug resistance-associated protein (mrp) gene and prognosis in untreated acute leukemia (AL) patients PMID: 11940320 LRP/MVP mRNA expression decreased as AML disease evolved, suggesting it is not associated with clinical resistant disease in AML. PMID: 11986944 identification as a dominant PTEN-binding protein in a yeast two-hybrid screen PMID: 12177006 RNA expression of this protein in breast cancer correlates with response to chemotherapy. PMID: 12576456 expression of lung resistance-related protein in differentiated cells and subsequent expression after chemotherapy suggests that it plays a role in therapy-induced differentiation PMID: 12612883 neither the presence nor the degree of immunoreactivity to MVP/LRP showed any correlation with either tumor grade or the presence of brain invasion PMID: 12622134 In gangliogliomas, western blot analysis showed a consistent increase in major vault protein expression compared with control cortex. PMID: 12919388 MVP and BCRP were expressed ubiquitously in brain capillary endothelium. Ectopic upregulation of MVP was seen in hilar neurons in HS, dysplastic neurons in FCD, and lesional neurons in DNT. Only in HS cases were rare extralesional neurons immunoreactive. PMID: 14636345 Results suggest that major vault protein functions as a novel scaffold protein for both SHP-2 and Erk. PMID: 15133037 The inverted MED1 element and the LRP130 protein have a role in transcription of the MVP gene. PMID: 15272088 Expression of LRP tended to be down-regulated in carcinomas. Moreover, the expression of LRP inversely correlated with tumor grades. PMID: 15379935 Vaults play no direct role in the multiple drug resistance phenotype in non-small cell lung carcinoma cells; their cellular function remains unknown. PMID: 15709737

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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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