Recombinant Human Ubiquitin D (UBD) Protein (His-SUMO)

Name: Recombinant Human Ubiquitin D (UBD) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10154P
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 Ubiquitin D (UBD) 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	O15205
Target Symbol	UBD
Synonyms	Diubiquitin; FAT10; GABBR1; UBD 3; Ubd; UBD_HUMAN; Ubiquitin D; Ubiquitin like protein FAT10; Ubiquitin-like protein FAT10
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MAPNASCLCVHVRSEEWDLMTFDANPYDSVKKIKEHVRSKTKVPVQDQVLLLGSKILKPRRSLSSYGIDKEKTIHLTLKVVKPSDEELPLFLVESGDEAKRHLLQVRRSSSVAQVKAMIETKTGIIPETQIVTCNGKRLEDGKMMADYGIRKGNLLFLACYCIGG
Expression Range	1-165aa
Protein Length	Full Length
Mol. Weight	34.5kDa
Research Area	Cell Biology
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	Ubiquitin-like protein modifier which can be covalently attached to target protein and subsequently leads to their degradation by the 26S proteasome, in a NUB1-dependent manner. Probably functions as a survival factor. Conjugation ability activated by UBA6. Promotes the expression of the proteasome subunit beta type-9 (PSMB9/LMP2). Regulates TNF-alpha-induced and LPS-mediated activation of the central mediator of innate immunity NF-kappa-B by promoting TNF-alpha-mediated proteasomal degradation of ubiquitinated-I-kappa-B-alpha. Required for TNF-alpha-induced p65 nuclear translocation in renal tubular epithelial cells (RTECs). May be involved in dendritic cell (DC) maturation, the process by which immature dendritic cells differentiate into fully competent antigen-presenting cells that initiate T-cell responses. Mediates mitotic non-disjunction and chromosome instability, in long-term in vitro culture and cancers, by abbreviating mitotic phase and impairing the kinetochore localization of MAD2L1 during the prometaphase stage of the cell cycle. May be involved in the formation of aggresomes when proteasome is saturated or impaired. Mediates apoptosis in a caspase-dependent manner, especially in renal epithelium and tubular cells during renal diseases such as polycystic kidney disease and Human immunodeficiency virus (HIV)-associated nephropathy (HIVAN).
Subcellular Location	Nucleus. Cytoplasm. Note=Accumulates in aggresomes under proteasome inhibition conditions.
Database References	HGNC: 18795 OMIM: 606050 KEGG: hsa:10537 STRING: 9606.ENSP00000366249 UniGene: PMID: 30127417 Overexpression of FAT10 promotes cisplatinresistant bladder cancer formation. These results indicated FAT10 may be a novel target for the treatment of bladder cancer. PMID: 29749526 the results of the present study suggest that FAT10 may be involved in DDR and therefore the progression of tumorigenesis. PMID: 29620277 Up-Regulation of UBD Transcript is associated with focal segmental glomerulosclerosis. PMID: 29531077 FAT10 promotes tumor proliferation by directly stabilizing Survivin protein in breast cancer cells. PMID: 27806337 our data suggest that FAT10 was upregulated via retinoic acid-induced protein I and NF-kappaB during H5N1 avian influenza virus infection. And the upregulated FAT10 promoted H5N1 viral replication by inhibiting type I IFN. PMID: 27354218 we show how FAT10 stabilizes the translation elongation factor eEF1A1, which contributes to cancer cell proliferation PMID: 27312528 this study revealed a novel function of LMO2 involving in the regulatory hierarchy of UBA6-USE1-FAT10ylation pathway by targeting the E1 enzyme UBA6. PMID: 27569286 unlike ISG15, ubiquitin and FAT10 are conjugated to a similar degree to newly translated and pre-existing proteins. PMID: 27926780 We also found that FAT10 may act its oncogenic functions through regulating HOXB9. Collectively, the results suggested that FAT10 may be a novel therapeutic target for osteosarcoma patients PMID: 27279480 High expression of FAT10 is associated with glioma. PMID: 26733179 Study demonstrates how the coordinated interplay of RIG-I, TRIM25, and FAT10 regulate the antiviral innate inflammatory response. PMID: 26996158 Data suggest that ubiquitin D (UBD) provides a negative feedback on cytokine-induced activation of the endoplasmic reticulum to nucleus signaling 1 (IRE1alpha)/c-Jun N-terminal kinase (JNK) pro-apoptotic pathway in cytokine-exposed beta cells. PMID: 27044747 FAT10 can induce malignant transformation as evidenced from the anchorage-independent growth as well as in vivo tumor-forming abilities of FAT10-overexpressing NeHepLxHT cells. PMID: 24325913 repertoire of peptides eluted from MHC class I molecules was influenced by FAT10 expression PMID: 26401002 FAT10 is the only ubiquitin-like modifier known to date which directly targets its hundreds of substrates for degradation by the proteasome. (Review) PMID: 25983082 Conjugation of the ubiquitin activating enzyme UBE1 with the ubiquitin-like modifier FAT10 targets it for proteasomal degradation PMID: 25768649 the interaction of FAT10 with MAD2 is a key mechanism underlying the promalignant property of FAT10 PMID: 25422469 Results identified a novel HCC regulatory circuit involving FAT10, beta-catenin/TCF4, and HOXB9, the dysfunction of which drives invasive and metastatic character in HCC. PMID: 25056121 STAT3 and NFkappaB synergistically act for maximum induction of FAT10 expression. PMID: 24518302 transcription downregulation of the Ufm1 and FAT10 conjugation system in liver Mallory-Denk bodies formation PMID: 24893112 functional distribution of the FAT10 targets suggests that FAT10 participates in various biological processes, such as translation, protein folding, RNA processing, and macromolecular complex assembly PMID: 23862649 FAT10 expression in pancreatic ductal adenocarcinoma (PDAC) was an independent prognostic factor of patients, which might be a potential diagnostic and therapeutic target of PDAC PMID: 24492942 These results suggest that knockdown of FAT10 by adenovirus-delivered siRNA may be a promising therapeutical strategy for treatment of hepatocellular carcinoma. PMID: 24440736 FAT10 has a central role in regulating diverse aspects of the pathogenesis of hepatocellular carcinoma. PMID: 23812429 FAT10 protects cardiac myocytes against apoptosis. PMID: 23416168 Immunohistochemistry showed that FAT10 protein was over-expressed in glioma tissues. Expression level of FAT10 increase from grade I to grade IV glioma according to the results of real-time PCR, immunohistochemistry analysis and Western blot. PMID: 22402871 p62 becomes covalently mono-FAT10ylated at several lysines, and FAT10 colocalizes with p62 in p62 bodies. PMID: 22797925 FATylation of LRRFIP2 occurs on two distinct sites, each being modified by a single FAT10 moiety. PMID: 23036196 These data reveal that VHS domain of Stam2 enters the hydrophobic pocket of K48-linked diubiquitin and binds the two ubiquitin subunits with different affinities. PMID: 21121635 This study identified eEF1A1 as a FAT10-specific binding protein, and when the expression of FAT10 was reduced by siRNA knockdown, this resulted in downregulation of eEF1A1 expression in hepatoma cells. PMID: 22569823 FAT10 modification of the HCMV-derived antigen pp65 (FAT10-pp65) enhances the presentation of the HLA-A2-restricted pp65495-509 antigenic peptide and provide evidence that FAT10- pp65 differs from Ub-modified pp65 in using the proteasome machinery. PMID: 22349260 Ten SNPs in FAT10 were identified. PMID: 22292662 Data indicate the potential role of cytokine-induced FAT10 expression in regulating Uba6 pathways. PMID: 22427669 findings show how FAT10 and NUB1L dock with the 26S proteasome to initiate proteolysis; identified the 26S proteasome subunit hRpn10/S5a as the receptor for FAT10, whereas NUB1L can bind to both Rpn10 and Rpn1/S2. PMID: 22434192 implicate FAT10 in retinal cell biology and Leber congenital amaurosis pathogenesis, and reveal a new role of AIPL1 in regulating the FAT10 pathway. PMID: 22347407 In this study a crystal structure of linear diubiquitin at a resolution of 2.2 A degrees is reported. PMID: 22281738 Degradation of FAT10 is accelerated after induction of apoptosis, suggesting that it plays a role in prosurvival pathways PMID: 22072791 FAT10 plays an important role in mediating the function of TNF-alpha during tumorigenesis by inducing cell cycle deregulation and chromosomal instability. PMID: 22025632 An extract of bark from the tropical rainforest plant Byrsonima crassifolia was screened for inhibition of diubiquitin formation by the human ubiquitin-conjugating enzyme E2-25K. PMID: 22164771 Data indicate that the 20,000-bp region is telomeric of the UBD gene and contains LOC729653, a hypothetical gene. PMID: 21631897 new role for FAT10 in the pathogenesis of polyglutamine diseases. PMID: 21757738 The p53 transcriptional activity was found to be substantially enhanced in FAT10-overexpressing cells. PMID: 21396347 USE1 is not only the first E2 enzyme but also the first known substrate of FAT10 conjugation, as it was efficiently auto-FAT10ylated in cis but not in trans. PMID: 20975683 Genetic polymorphism in UBD is associated with colorectal cancer. PMID: 21351261 Reverse transcriptase-polymerase chain reaction analysis of intestinal biopsy sample pairs (at diagnosis vs treated) from 30 celiac disease patients confirmed overexpression of UBD in active disease tissue. PMID: 19808075 FAT10 may modulate tumorigenesis through its reported interaction with the MAD2 spindle-assembly checkpoint protein. PMID: 12730673 FAT10 is degraded by the proteasome in ubiqitin-independent manner. PMID: 15831455 high levels of FAT10 protein in cells lead to increased mitotic nondisjunction and chromosome instability, which is mediated by an abbreviated mitotic phase and reduction in the kinetochore localization of MAD2 during prometaphase PMID: 16495226 Immunohistochemical studies demonstrated increased FAT10 expression in HIV-associated nephropathy and in autosomal dominant polycystic kidney disease. PMID: 16495380

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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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