hypothetical protein, A306_16176, Anapl_09380, AS27_04981, AS28_10071, BTB and CNC homolog 2, BTB and CNC homology 1, basic leucine zipper transcription facto, BTB and CNC homology 1, basic leucine zipper transcription factor 2, BTB and CNC homology 2, BTB and CNC homology, basic leucine zipper transcription factor 2, BTB and CNC-like protein 2, BTB and CNC-like proteiny 1, basic leucine zipper transcription factor 2, BTBD25, CB1_000371003, D623_10023882, EGK_15169, GW7_21221, H920_09183, M91_21520, N300_01162, N301_04236, N302_15591, N303_00283, N306_11786, N307_06313, N309_15054, N312_12567, N320_02542, N321_10716, N322_10547, N324_08521, N325_01813, N326_10621, N327_13435, N329_07672, N330_12030, N332_00603, N333_12747, N334_07268, N335_02849, N336_03526, N339_08762, N340_07775, N341_06653, PAL_GLEAN10025165, PANDA_014576, RGD1562865, Transcription regulator protein BACH2, Transcription regulator protein BACH2 (BTB and CNC homolog 2), transcription regulator protein BACH2-like protein, ...
Glucocorticoid-induced leucine zipper (GILZ) is a mediator of the anti-inflammatory activities of glucocorticoids. However, GILZ deletion does not impair the anti-inflammatory activities of exogenous glucocorticoids in mice arthritis models and GILZ could also mediate some glucocorticoid-related adverse events. Osteoarthritis (OA) is a metabolic disorder that is partly attributed to adipokines such as leptin, and we previously observed that glucocorticoids induced leptin secretion in OA synovial fibroblasts. The purpose of this study was to position GILZ in OA through its involvement in the anti-inflammatory activities of glucocorticoids and/or in the metabolic pathway of leptin induction. The influences of mineralocorticoids on GILZ and leptin expression were also investigated. Human synovial fibroblasts were isolated from OA patients during knee replacement surgery. Then, the cells were treated with a glucocorticoid (prednisolone), a mineralocorticoid (aldosterone), a glucocorticoid receptor (GR)
Glucocorticoid-induced leucine zipper (GILZ) is a mediator of the anti-inflammatory activities of glucocorticoids. However, GILZ deletion does not impair the anti-inflammatory activities of exogenous glucocorticoids in mice arthritis models and GILZ could also mediate some glucocorticoid-related adverse events. Osteoarthritis (OA) is a metabolic disorder that is partly attributed to adipokines such as leptin, and we previously observed that glucocorticoids induced leptin secretion in OA synovial fibroblasts. The purpose of this study was to position GILZ in OA through its involvement in the anti-inflammatory activities of glucocorticoids and/or in the metabolic pathway of leptin induction. The influences of mineralocorticoids on GILZ and leptin expression were also investigated. Human synovial fibroblasts were isolated from OA patients during knee replacement surgery. Then, the cells were treated with a glucocorticoid (prednisolone), a mineralocorticoid (aldosterone), a glucocorticoid receptor (GR)
The KP element can repress P element mobility in Drosophila melanogaster. Three mutant KP elements were made that had either two amino acid substitutions or a single amino acid deletion in the putative leucine zipper domain found in the KP polypeptide. Each KP element was expressed from the actin 5C proximal promoter. The wild-type control construct strongly repressed P element mobility, measured by the GD sterility and sn(w) mutability assays, in a position-independent manner. The single amino acid deletion mutant failed to repress P mobility by the double amino acid substitution mutants was position dependent. The results show that the leucine zipper of the KP polypeptide is important for P element regulation. This supports the multimer-poisoning model of P element repression, because leucine zipper motifs are involved in protein-protein interactions. ...
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Leucine zippers are oligomerization domains used in a wide range of proteins. Their structure is based on a highly conserved heptad repeat sequence in which two key positions are occupied by leucines. The leucine zipper of the cell cycle-regulated Nek2 kinase is important for its dimerization and activation. However, the sequence of this leucine zipper is most unusual in that leucines occupy only one of the two hydrophobic positions. The other position, depending on the register of the heptad repeat, is occupied by either acidic or basic residues. Using NMR spectroscopy, we show that this leucine zipper exists in two conformations of almost equal population that exchange with a rate of 17 s(-1). We propose that the two conformations correspond to the two possible registers of the heptad repeat. This hypothesis is supported by a cysteine mutant that locks the protein in one of the two conformations. NMR spectra of this mutant showed the predicted 2-fold reduction of peaks in the (15)N HSQC ...
TY - JOUR. T1 - Oligomerization properties of GCN4 leucine zipper e and g position mutants. AU - Zeng, Xiangang. AU - Zhu, Hai. AU - Lashuel, Hilal A.. AU - Hu, James C.. PY - 1997/10/1. Y1 - 1997/10/1. N2 - Putative intersubunit electrostatic interactions between charged amine acids on the surfaces of the dimer interfaces of leucine zippers (g-e ion pairs) have been implicated as determinants of dimerization specificity. To evaluate the importance of these ionic interactions in determining the specificity of dimer formation, we constructed a pool of ,65,000 GCN4 leucine zipper mutants in which all the e and g positions are occupied by different combinations of alanine, glutamic acid, lysine, or threonine. The oligomerization properties of these mutants were evaluated based on the phenotypes of cells expressing λ repressor-leucine zipper fusion proteins. About 90% of the mutants do not form stable homooligomers. Surprisingly, approximately 8% of the mutant sequences have phenotypes consistent ...
Expression of c-myc with constitutively active mutants of the ras gene results in the cooperative transformation of primary fibroblasts, although the precise mechanism by which these genes cooperate is unknown. Since c-Myc has been shown to function as a transcriptional activator, we have examined the ability of c-Myc and activated Ras (H-RasV-12) to cooperatively induce the promoter activity of cdc2, a gene which is critical for cell cycle progression. Microinjection of expression constructs encoding H-RasV-12 and c-Myc along with a cdc2 promoter-luciferase reporter plasmid into quiescent cells led to an increase in cdc2 promoter activity approximately 30 h after injection, a period which coincides with the S-to-G2/M transition in these cells. Expression of H-RasV-12 alone weakly activated the cdc2 promoter, while expression of c-Myc alone had no effect. Mutants of c-Myc lacking either the leucine zipper dimerization domain or the phosphoacceptor site Ser-62 could not cooperate with H-RasV-12 ...
The basic leucine zipper transcription factor ATF5 is overexpressed in many tumor types and interference with its expression or function inhibits cancer cell survival. As a potential therapeutic approach to exploit these findings, we created dominant-negative (DN) ATF5 forms lacking DNA-binding ability that retain the ATF5 leucine zipper, and thus associate with and sequester ATF5s requisite leucine zipper-binding partners. Preclinical studies with DN-ATF5, including a cell-penetrating form, show in vitro and in vivo efficacy in compromising cancer cell survival. However, DN-ATF5s targets, and particularly those required for tumor cell survival, have been unknown. We report that cells lacking ATF5 succumb to DN-ATF5, indicating that ATF5 itself is not DN-ATF5s obligate target. Unbiased pull-down assays coupled with mass spectrometry and immunoblotting revealed that DN-ATF5 associates in cells with the basic leucine zipper proteins CEBPB and CEBPD and coiled-coil protein CCDC6. Consistent with ...
We have recently isolated a human gene, ROX, encoding a new member of the basic helix-loop-helix leucine zipper protein family. ROX is capable of heterodimerizing with Max and acts as a transcriptional repressor in an E-box-driven reporter gene system, while it was found to activate transcription in HeLa cells. ROX expression levels vary during the cell cycle, being down-regulated in proliferating cells. These biological properties of ROX suggest a possible involvement of this gene in cell proliferation and differentiation. The ROX gene maps to chromosome 17p13.3, a region frequently deleted in human malignancies. Here we report the genomic structure of the human ROX gene, which is composed of six exons and spans a genomic region of less than 40 kb. In an attempt to identify possible inactivating mutations in the ROX gene in human breast cancer, we performed a single-strand conformation polymorphism analysis of its coding region in 16 sporadic breast carcinomas showing loss of heterozygosity in ...
JDP2 bound directly to the ARE core sequence, associated with NFE2L2 and MAFK (NFE2L2-MAFK) via basic leucine zipper domains, and increased DNA-binding activity of the NFE2L2-MAFK complex to the ARE and the transcription of ARE-dependent genes ...
Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a 216-Asp-|-Gly-217 bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Triggers cell adhesion in sympathetic neurons through RET cleavage (By similarity).
Hox genes control regional identity during segmentation of the vertebrate hindbrain into rhombomeres. A transgenic analysis as used to investigate the upstream mechanisms for regulation of Hoxb-3 in rhombomere (r)5. Enhancers were identified from the promoter sequences of mouse and chick Hoxb-3 sufficient for r5-restricted expression. Sequence comparisons reveal two blocks of similarity (of 19 and 45 base pairs), which each contain in vitro binding sites for the kreisler protein (Kmrl1), a Maf/b-Zip protein expressed in r5 and r6. Kreisler (Krml1) is a member of a distinct basic leucine zipper family with some sequence homology in the basic DNA binding region to fos, jun, CREB and C/EBP. Both kreisler binding sites are required for r5 activity, suggesting that Hoxb-3 is a direct target of kreisler. Multimers of the 19-base-pair (bp) block recreate a Krml1-like pattern in r5/r6, but the 45-bp block mediates expression only in r5. Therefore elements within the 45-bp block restrict the response to ...
The basic leucine zipper transcription factor C/EBPa, required for the in vivo transition of common myeloid progenitor-to-GM progenitor. Myelomonocyte... read full [Essay Sample] for free
Monoclonal antibody against BTB and CNC homology 1, basic leucine zipper transcription factor 2 expressed by BACH2 for use in Immunoprecipitation, Microarray against Human
BACH1 antibody [N2C1], Internal (BTB and CNC homology 1, basic leucine zipper transcription factor 1) for WB. Anti-BACH1 pAb (GTX110292) is tested in Human samples. 100% Ab-Assurance.
DNA-binding motifs formed from two alpha-helixes which intertwine for about eight turns into a coiled coil and then bifurcate to form Y shaped structures. Leucines occurring in heptad repeats end up on the same sides of the helixes and are adjacent to each other in the stem of the Y (the "zipper" region). The DNA-binding residues are located in the bifurcated region of the Y ...
Mareks disease virus (MDV) is one of several oncogenic herpesviruses and causes fatal lymphomas in chickens. The current "gold standard" vaccine is the live-attenuated MDV strain CVI988/Rispens (CVI), which is widely used and efficiently prevents tumor formation. Intriguingly, CVI expresses two predominant isoforms of the major MDV oncogene meq: one variant with a regular size of meq (Smeq) and one long... ...
Mutations, Bold: Linker sequences, Underscored: Leucine zipper sequences, Bold italic: GrpE33-197, Grey: Natural histidine affinity tag
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The KOMP Repository is located at the University of California Davis and Childrens Hospital Oakland Research Institute. Question? Comments? For Mice, Cells, and germplasm please contact us at [email protected], US 1-888-KOMP-MICE or International +1-530-752-KOMP, or for vectors [email protected] or +1-510-450-7917 ...
Schmidt, A, Annamalai K, Schmidt M, Grigorieff N, Marcus Fändrich M. 2016. Cryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibril. Proc Natl Acad Sci U S A. 113:6200-6205. Abstract ...
The addition of the new sequences to our analysis has provided additional support that the olfactomedin and TIGR proteins are related throughout the length of the molecule rather than only in the olfactomedin domain in the C terminus. In Fig. 2, the GXCXXT motif and the leucine-rich/leucine-zipper regions of the sequences are highlighted. All of the olfactomedin- and TIGR-related sequences possess a residual leucine zipper aligned with the leucine zipper of TIGR. The additional sequences have also helped to adjust our previous alignments (1). When we align only the TIGR and olfactomedin sequences the N-terminal region includes a (A/V)LEE(E/Y)K motif spanning residues 151 through 156 in HTIGR and 135 through 140 in MOLFA. With the addition of the more divergent sequences, that region appears to be only partially conserved among the HTIGR, COLFA, and HOLFC proteins and is significantly more divergent among the other sequences.. In addition to the support from our sequence analysis, structural ...
ATF2 (pT73/T55) Antibody is a Rabbit Polyclonal antibody against ATF2 (pT73/T55). This gene encodes a transcription factor that is a member of the leucine zipper family of DNA binding proteins. This protein binds to the cAMP-responsive element (CRE), an o
Im redoing my bug net. I had picked up a couple surplus bug tents to make my nets. My first generation was open on one end with a draw string so I could cinch it above my head. It turned out to be better in theory than practice. My thought now is to close the end with a zipper or Velcro so I can still pull the net back and use my hammock as a chair. To get in and out while it is in use I plan on putting a zipper in the middle of one side. The thing Im wondering about is what length zipper
Myc, Mad and Max proteins belong to the essential helix-loop-helix leucine zipper category of transcription elements. ~5-fold and ~2-fold higher level continuous than MaxMax and MadMax, respectively. The protein dimerization prices and also the dimer-DNA prices were discovered to be focus independent suggesting conformational adjustments were price limiting. The Arrhenius activation energies for the dimerization of Myc, Mad and Max conversation with Max had been 20.4 0.8, 29 0.6 and 40 0.2 kJ/mol, respectively. Further, price constants for MaxMax homodimer DNA binding are considerably greater than for MycMax and MadMax heterodimers binding to DNA. Monomer-DNA binding demonstrated a faster price than dimer-DNA binding. These studies also show the rate-limiting stage for the dimer pathway may be the development of proteins dimers which reaction is certainly slower than development of proteins dimers on the DNA user interface, kinetically favoring the monomer pathway. Myc, Max and Mad are people of ...
Sometimes called bZIP motifs. A quaternary structure|dimer of two long alpha helix|alpha helices which look like forceps pinching a piece of DNA. These ...
member of homeodomain-leucine zipper family, acting as a differentiation-promoting transcription factor of the vascular meristems ...
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Coiled-coil leucine zipper domains are well-studied molecular recognition motifs that are attractive candidates for incorporation into engineered self-assembly systems due to their modular nature and wide range of binding affinities. Here, we investigate the ability of this peptide family to induce and contr Emerging Investigators
MRG. This family consists of three different eukaryotic proteins (mortality factor 4 (MORF4/MRG15), male-specific lethal 3(MSL-3) and ESA1-associated factor 3(EAF3)). It is thought that the MRG family is involved in transcriptional regulation via histone acetylation. It contains 2 chromo domains and a leucine zipper motif. ...
The protein encoded by this gene contains 2 leucine zipper domains and a putative C-terminal nuclear targeting signal, but does not have any hydrophobic regions. This protein is expressed weakly in resting NK and T cells. The encoded protein modulates the activation of ARF genes by CYTH1. This protein interacts with CYTH1 and SNX27 proteins and may act to sequester CYTH1 protein in the cytoplasm.[provided by RefSeq, Aug 2008 ...
Complete information for LUZP2 gene (Protein Coding), Leucine Zipper Protein 2, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
The basic leucine zipper (bZIP) family is one of the largest transcription factor (TF) families in plants, which play crucial roles in plant growth and development. bZIP proteins are involved in multiple biological processes, as well as responses to various biotic/abiotic stresses. Although genome-wide analysis of the bZIP gene family has been conducted in several plant species, only few comprehen ...
The basic leucine zipper (bZIP) family is one of the largest transcription factor (TF) families in plants, which play crucial roles in plant growth and development. bZIP proteins are involved in multiple biological processes, as well as responses to various biotic/abiotic stresses. Although genome-wide analysis of the bZIP gene family has been conducted in several plant species, only few comprehen ...
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This gene encodes a transcription factor which is a member of a small family of basic leucine zipper (bZIP) proteins. The encoded transcription factor regulates genes which contain antioxidant response elements (ARE) in their promoters; many of these genes encode proteins involved in response to injury and inflammation which includes the production of free radicals. Multiple transcript variants encoding different isoforms have been characterized for this gene. [provided by RefSeq, Sep 2015 ...
BZW2 overexpression lysate, 0.1 mg. Transient overexpression lysate of basic leucine zipper and W2 domains 2 (BZW2), transcript variant 2
Complete information for BZW2 gene (Protein Coding), Basic Leucine Zipper And W2 Domains 2, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Gene target information for BZW2 - basic leucine zipper and W2 domains 2 (human). Find diseases associated with this biological target and compounds tested against it in bioassay experiments.
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In 2006 the McGill team attempted to use leucine zippers fused to split YFP to display on cells and cause the cells to adhere via the split YFP. See: http://parts.mit.edu/wiki/index.php/McGill_University_ ...
The following teams have used some component of our phage system previously. No other teams have used our method of polyphage with incorporated leucine zippers for polymerization (nor is it present in the literature ...
Fully Encapsulating Suit, Level B, expanded back, 20 mil PVC face shield, elastic wrists, rear entry, zipper/PVC zip lock closure, double storm flap over zipper, two exhaust vents, attached boots, outer boot flaps ...
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