e1 activating enzyme

UBE1, also known as UBA1, belongs to the ubiquitin-activating E1 family. UBE1 gene complements an X-linked mouse temperature-sensitive defect in DNA synthesis, and thus may function in DNA repair. It is part of a gene cluster on chromosome Xp11.23. UBE1 catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation. It also catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Defects in UBA1 can cause spinal muscular atrophy X-linked type 2 (SMAX2), also known as X-linked lethal infantile spinal muscular atrophy, distal X-linked arthrogryposis multiplex congenita or X-linked arthrogryposis type 1 (AMCX1). Spinal muscular atrophy refers to a group of neuromuscular disorders characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. SMAX2 is a lethal infantile form presenting with hypotonia, areflexia, and multiple congenital contractures.

UBA5 is a member of the ubiquitin-activating E1 family and UBA5 subfamily. Ubiquitin and ubiquitin-like proteins are recognized as covalently conjugated to various cellular substrates by a three-step enzymatic pathway. The ubiquitin-activating enzyme (E1) has a vital role in the first step of ubiquitination pathway to activate ubiquitin or ubiquitin-like proteins. UBA5 activates ubiquitin-fold modifier 1, a ubiquitin-like post-translational modifier protein, via the formation of a high-energy thioester bond. UBA5 is located primarily in cytoplasm, while it generally localizes to the nucleus in presence of SUMO2.

UBA6 (Ubiquitin Like Modifier Activating Enzyme 6) is a Protein Coding gene. The UBA6 gene, located on 4q13.2, is conserved in chimpanzee, Rhesus monkey, dog, cow, mouse, rat, chicken, zebrafish, and frog. Uba6 is a homolog of the ubiquitin-activating enzyme, Uba1, and activates two ubiquitin-like proteins (UBLs), ubiquitin and FAT10. UBA6 is an alternative enzyme for ubiquitin activation in vertebrates that plays a pivotal role in early mouse development. UBA6 is widely expressed in the lymph node, appendix, and other tissues. Diseases associated with UBA6 include Ichthyosis, Congenital, Autosomal Recessive 4A, and Johanson-Blizzard Syndrome. Among its related pathways are the Metabolism of proteins and the Innate Immune System.

IL-1 alpha is a member of the interleukin 1 cytokine family. Cytokines are proteinaceous signaling compounds that are major mediators of the immune response. They control many different cellular functions including proliferation, differentiation, and cell survival/apoptosis but are also involved in several pathophysiological processes including viral infections and autoimmune diseases. Cytokines are synthesized under various stimuli by a variety of cells of both the innate (monocytes, macrophages, dendritic cells) and adaptive (T- and B-cells) immune systems. Cytokines can be classified into two groups: pro- and anti-inflammatory. Pro-inflammatory cytokines, including IFNgamma, IL-1, IL-6, and TNF-alpha, are predominantly derived from the innate immune cells and Th1 cells. Anti-inflammatory cytokines, including IL-10, IL-4, IL-13, and IL-5, are synthesized from Th2 immune cells. IL-1 alpha is a pleiotropic cytokine involved in various immune responses, inflammatory processes, and hematopoiesis. It is produced by monocytes and macrophages as a proprotein, which is proteolytically processed and released in response to cell injury, and thus induces apoptosis. IL-1 alpha stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity.

Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the 2 position. This enzyme can utilize either acyl-CoA or acyl-ACP as the fatty acyl donor. 1-AGPAT Protein, E. coli, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 29.5 kDa and the accession number is P26647.

Bovine viral diarrhea virus (strain SD-1) Genome polyprotein (E. coli, His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 25.0 kDa and the accession number is Q01499.

Insulin-1 Protein, Mouse, Recombinant (E. coli, His & Myc) is expressed in E. coli.

N/A. Anionic trypsin-1 Protein, Rat, Recombinant (E. coli, His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 27.2 kDa and the accession number is P00762.

NY-ESO-1 or New York esophageal squamous cell carcinoma 1 is a well-known cancer-testis antigen (CTAs) with re-expression in numerous cancer types. Its ability to elicit spontaneous humoral and cellular immune responses, together with its restricted expression pattern, have rendered it a good candidate target for cancer immunotherapy.

E-Cadherin/Cadherin-1 Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 87.1 kDa and the accession number is P12830-1.

Met e 1 Protein, Metapenaeus ensis, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 32.7 kDa.

E-Cadherin/Cadherin-1 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 78 kDa and the accession number is P09803.

E-Cadherin/Cadherin-1 Protein, Human, Recombinant (hFc), Biotinylated is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 87.1 kDa and the accession number is P12830-1.

E-cadherin is the core component of epithelial adherens junctions, essential for tissue development, differentiation, and maintenance. It is also fundamental for tissue barrier formation, a critical function of epithelial tissues.

Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions.

This colicin is a channel-forming colicin. This class of transmembrane toxins depolarize the cytoplasmic membrane, leading to dissipation of cellular energy.; Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.

This colicin is a channel-forming colicin. This class of transmembrane toxins depolarize the cytoplasmic membrane, leading to dissipation of cellular energy.; Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.

Broad spectrum beta-lactamase which confers resistance to penicillins, as well as first, second and third-generation cephalosporins.

Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. Acts also as a viroporin and forms ion conductive pores allowing viral particle release. Impairs the generation of type I interferon by downregulating host TLR3 and TLR7 as well as their downstream signaling pathways. Hepatitis E virus genotype 1 (HEV-1) Protein ORF3 (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 27.8 kDa and the accession number is O90299.

PAI-1 Protein, Horse, Recombinant (E. coli) is expressed in E. coli expression system. The predicted molecular weight is 32.1 kDa and the accession number is Q8MI31.

Mcr-1 Protein, E. coli, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 56.7 kDa and the accession number is A0A0R6L508.

Recognizes the ribosomal RNA gene promoter and activates transcription mediated by RNA polymerase I through cooperative interactions with the transcription factor SL1/TIF-IB complex. It binds specifically to the upstream control element. Nucleolar transcription factor 1 Protein, Human, Recombinant (E. coli, His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 95.2 kDa and the accession number is P17480.

Sulfated glycoprotein widely distributed in basement membranes and tightly associated with laminin. Also binds to collagen IV and perlecan. It probably has a role in cell-extracellular matrix interactions. Nidogen-1 Protein, Mouse, Recombinant (E. coli, His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 30.3 kDa and the accession number is P10493.

NY-ESO-1 or New York esophageal squamous cell carcinoma 1 is a well-known cancer-testis antigen (CTAs) with re-expression in numerous cancer types. Its ability to elicit spontaneous humoral and cellular immune responses, together with its restricted expression pattern, have rendered it a good candidate target for cancer immunotherapy.

E-Cadherin/Cadherin-1 Protein, Rat, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 103.8 kDa and the accession number is Q9R0T4.

E-Cadherin/Cadherin-1 Protein, Rat, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 78.4 kDa and the accession number is Q9R0T4.

Interferon tau-1/IFNT1 Protein, Bovine, Recombinant (E. coli, His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 23.8 kDa and the accession number is P15696.

Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Thioredoxin-1 Protein, E. coli, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 15.7 kDa and the accession number is P0AA25.

Plays a role in the inhibition of host antibody-mediated neutralization without blocking viral cell entry.; Forms an icosahedral capsid with a T=1 symmetry and a 34 nm diameter. The capsid is composed of 60 copies linked to each other. Binds to the 5' end of the genomic RNA to mediate genome encapsidation. Binds to heparin surface proteoglycans (HSPGs) to mediate viral entry. Additionally, the interactions with host ASGR1 and ASGR2 facilitate viral infection of hepatocytes. Hepatitis E virus genotype 1 (HEV-1) Secreted protein ORF2 (His) is expressed in Baculovirus insect cells with N-10xHis tag. The predicted molecular weight is 71.3 kDa and the accession number is Q68985.

May inhibit NODAL and BMP signaling during neural patterning. May be a tumor suppressor in brain cancers.

Ber e 1 Protein, Brazil nut, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 14.2 kDa.

Broad spectrum beta-lactamase which confers resistance to penicillins, as well as first, second and third-generation cephalosporins.

IL-1 beta Protein, Sheep, Recombinant (E. coli, His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 21.7 kDa and the accession number is P21621.

West Nile Virus (WNV) (lineage 1, strain NY99) E/Envelope Protein (His) is expressed in yeast with His tag. The predicted molecular weight is 12.9 kDa and the accession number is ABA62343.1.

Dengue virus (DENV) (type 1, strain US/Hawaii/1944) E/Envelope Protein (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 12.4 kDa and the accession number is ACF49259.1.

E-Cadherin/Cadherin-1 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 62 kDa and the accession number is A0A0U2ZQU7.

UBE2M is a member of the ubiquitin-conjugating E2 family whose members perform the second step in the ubiquitination reaction. Initially identified as the main process for protein degradation, ubiquitination is believed nowadays to be crucial for a wider range of cellular processes. The outcome of the ubiquitin-conjugation reaction, and thereby the fate of the substrate, is heavily dependent on the number of ubiquitin molecules attached and how these ubiquitin molecules are inter-connected. To deal with this complexity and to allow adequate ubiquitination in time and space, a highly sophisticated conjugation machinery has been developed. In a sequential manner, ubiquitin becomes activated by an ubiquitin-activating enzyme (E1), which then transfers the ubiquitin to a group of ubiquitin-conjugating enzymes (E2s). Next, ubiquitin-loaded E2s are interacting with ubiquitin-protein ligases (E3s) and ubiquitin is conjugated to substrates on recruitment by the E3. These three key enzymes are operating in a hierarchical system, wherein two E1s and 35 E2s have been found and hundreds of E3s have been identified in humans.

UBE2H is a member of the ubiquitin-conjugating E2 family whose members perform the second step in the ubiquitination reaction. Initially identified as the main process for protein degradation, ubiquitination is believed nowadays to be crucial for a wider range of cellular processes. The outcome of the ubiquitin-conjugation reaction, and thereby the fate of the substrate, is heavily dependent on the number of ubiquitin molecules attached and how these ubiquitin molecules are inter-connected. To deal with this complexity and to allow adequate ubiquitination in time and space, a highly sophisticated conjugation machinery has been developed. In a sequential manner, ubiquitin becomes activated by a ubiquitin-activating enzyme (E1), which then transfers the ubiquitin to a group of ubiquitin-conjugating enzymes (E2s). Next, ubiquitin-loaded E2s are interacting with ubiquitin-protein ligases (E3s) and ubiquitin is conjugated to substrates on recruitment by the E3. These three key enzymes are operating in a hierarchical system, wherein two E1s and 35 E2s have been found and hundreds of E3s have been identified in humans.

Ubiquitin-conjugating enzymes, also known as UBE2W, E2 enzymes and more rarely as ubiquitin-carrier enzymes, perform the second step of protein ubiquitination. The modification of protein with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. UBE2W is a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is required for post-replicative DNA damage repair. It accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. It also catalyzes monoubiquitination and Lys-11 -linked polyubiquitination. UBE2W is also considered to regulate FANCD2 monoubiquitination. UBE2W exhibits ubiquitin conjugating enzyme activity and catalyzes the monoubiquitination of PHD domain of Fanconi anemia complementation group L (FANCL). Over-expression of UBE2W in cells promotes the monoubiquitination of FANCD2 and down-regulated UBE2W markedly reduces the UV irradiation-induced but not MMC-induced FANCD2 monoubiquitination.

UBE2I is a member of the ubiquitin-conjugating E2 family whose members perform the second step in the ubiquitination reaction. Initially identified as the main process for protein degradation, ubiquitination is believed nowadays to be crucial for a wider range of cellular processes. The outcome of the ubiquitin-conjugation reaction, and thereby the fate of the substrate, is heavily dependent on the number of ubiquitin molecules attached and how these ubiquitin molecules are inter-connected. To deal with this complexity and to allow adequate ubiquitination in time and space, a highly sophisticated conjugation machinery has been developed. In a sequential manner, ubiquitin becomes activated by a ubiquitin-activating enzyme (E1), which then transfers the ubiquitin to a group of ubiquitin-conjugating enzymes (E2s). Next, ubiquitin-loaded E2s are interacting with ubiquitin-protein ligases (E3s) and ubiquitin is conjugated to substrates on recruitment by the E3. These three key enzymes are operating in a hierarchical system, wherein two E1s and 35 E2s have been found and hundreds of E3s have been identified in humans.

SUMO-Conjugating Enzyme UBC9 (UBC9) belongs to the ubiquitin-conjugating enzyme family. UBC9 is homologous to ubiquitin-conjugating enzymes (E2s). However, instead of conjugating ubiquitin, UBC9 conjugates a ubiquitin homologue, Small Ubiquitin-Like Modifier 1 (SUMO-1). The conjugation of ubiquitin requires the activities of ubiquitin-activating (E1) and conjugating (E2) enzymes. It is suggested that UBC9 might play a role in DNA repair and perhaps even in aging.

UBE2D4 is a member of the ubiquitin-conjugating E2 family whose members perform the second step in the ubiquitination reaction. Initially identified as the main process for protein degradation, ubiquitination is believed nowadays to be crucial for a wider range of cellular processes. The outcome of the ubiquitin-conjugation reaction, and thereby the fate of the substrate, is heavily dependent on the number of ubiquitin molecules attached and how these ubiquitin molecules are inter-connected. To deal with this complexity and to allow adequate ubiquitination in time and space, a highly sophisticated conjugation machinery has been developed. In a sequential manner, ubiquitin becomes activated by a ubiquitin-activating enzyme (E1), which then transfers the ubiquitin to a group of ubiquitin-conjugating enzymes (E2s). Next, ubiquitin-loaded E2s are interacting with ubiquitin-protein ligases (E3s) and ubiquitin is conjugated to substrates on recruitment by the E3. These three key enzymes are operating in a hierarchical system, wherein two E1s and 35 E2s have been found and hundreds of E3s have been identified in humans. It has been identified the UBE2D family (UBE2D1-4) as E2 partners for IDOL that support both autoubiquitination and IDOL-dependent ubiquitination of the LDLR in a cell-free system.

Ubiquitin-conjugating enzyme E2 D1（UBE2D1）belongs to the ubiquitin-conjugating enzyme family. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This enzyme is closely related to a stimulator of iron transport (SFT), and is up-regulated in hereditary hemochromatosis. It also functions in the ubiquitination of the tumor-suppressor protein p53 and the hypoxia-inducible transcription factor HIF1alpha by interacting with the E1 ubiquitin-activating enzyme and the E3 ubiquitin-protein ligases.

UBE2F is a member of the ubiquitin-conjugating E2 family whose members perform the second step in the ubiquitination reaction. Initially identified as the main process for protein degradation, ubiquitination is believed nowadays to be crucial for a wider range of cellular processes. The outcome of the ubiquitin-conjugation reaction, and thereby the fate of the substrate, is heavily dependent on the number of ubiquitin molecules attached and how these ubiquitin molecules are inter-connected. To deal with this complexity and to allow adequate ubiquitination in time and space, a highly sophisticated conjugation machinery has been developed. In a sequential manner, ubiquitin becomes activated by a ubiquitin-activating enzyme (E1), which then transfers the ubiquitin to a group of ubiquitin-conjugating enzymes (E2s). Next, ubiquitin-loaded E2s are interacting with ubiquitin-protein ligases (E3s) and ubiquitin is conjugated to substrates on recruitment by the E3. These three key enzymes are operating in a hierarchical system, wherein two E1s and 35 E2s have been found and hundreds of E3s have been identified in humans.

UBE2G1 is a member of the ubiquitin-conjugating E2 family whose members perform the second step in the ubiquitination reaction. Initially identified as the main process for protein degradation, ubiquitination is believed nowadays to be crucial for a wider range of cellular processes. The outcome of the ubiquitin-conjugation reaction, and thereby the fate of the substrate, is heavily dependent on the number of ubiquitin molecules attached and how these ubiquitin molecules are inter-connected. To deal with this complexity and to allow adequate ubiquitination in time and space, a highly sophisticated conjugation machinery has been developed. In a sequential manner, ubiquitin becomes activated by a ubiquitin-activating enzyme (E1), which then transfers the ubiquitin to a group of ubiquitin-conjugating enzymes (E2s). Next, ubiquitin-loaded E2s are interacting with ubiquitin-protein ligases (E3s) and ubiquitin is conjugated to substrates on recruitment by the E3. These three key enzymes are operating in a hierarchical system, wherein two E1s and 35 E2s have been found and hundreds of E3s have been identified in humans.