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2-Bromo-3,6-dimethoxybenzoic+acid


16,909  results were found

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Supplier:  Bioss
Description:   Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization <i>in vitro</i> by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. Required for proper localization of non-farnesylated prelamin-A/C.Tissue specificity; Skeletal muscle, heart, colon, testis, ovary and pancreas.
Catalog Number: (10750-186)

Supplier:  Prosci
Description:   Syntaphilin Antibody: Syntaphilin was initially identified in a yeast two-hybrid screen with the carboxy terminal region of Syntaxin-1 as bait. Syntaxin-1 is a key component of the synaptic vesicle docking machinery that forms the SNARE complex with synaptobrevin and SNAP-25. Syntaphilin competes with SNAP-25 for binding to syntaxin-1 and inhibits the formation of the SNARE complex, thereby potentially regulating synaptic vesicle exocytosis. Syntaphilin also binds dynamin-1 and inhibits dynamin-dependent endocytosis. Mice lacking syntaphilin show an increased level of mitochondrial motility and a reduced density of axonal mitochondria. This correlates with an enhanced short-term facilitation and significant impairments in motor ability, suggesting syntaphilin plays a major role in presynaptic function. Multiple isoforms are known to exist.
Supplier:  Bioss
Description:   CESK1, also known as CCT8L2 (chaperonin containing TCP1, subunit 8 theta-like 2), is a 557 amino acid protein that localizes to the cytoplasm and is thought to function as a molecular chaperone, possibly assisting protein folding after ATP hydrolysis. CESK1 belongs to the TCP-1 chaperonin family and is encoded by a gene which maps to human chromosome 22. Mutations in several of the genes that map to chromosome 22 are involved in the development of Phelan-McDermid syndrome, neurofibromatosis type 2, autism and schizophrenia. Additionally, translocations between chromosomes 9 and 22 may lead to the formation of the Philadelphia chromosome and the subsequent production of the novel fusion protein Bcr-Abl, a potent cell proliferation activator found in several types of leukemias.
Supplier:  Biotium
Description:   This MAb recognizes extracellular epitope of human CD147. It is expressed more intensely on thymocytes than on mature peripheral blood T cells. CD147 is important in spermatogenesis, embryo implantation, neural network formation, and tumor progression. It stimulates the production of interstitial collagenase, gelatinase A, stromelysin-1 and various metalloproteinases (MMPs) by fibroblasts. These enzymes are important factors in cancer invasion and metastasis.

CF® dyes are Biotium's next-generation fluorescent dyes. CF®488A is a green fluorescent dye (Ex/Em 490/515 nm) with excellent brightness and photostability. The dye is minimally charged for less non-specific binding. CF®488A also is compatible with super-resolution imaging by TIRF.
Supplier:  Bioss
Description:   CESK1, also known as CCT8L2 (chaperonin containing TCP1, subunit 8 theta-like 2), is a 557 amino acid protein that localizes to the cytoplasm and is thought to function as a molecular chaperone, possibly assisting protein folding after ATP hydrolysis. CESK1 belongs to the TCP-1 chaperonin family and is encoded by a gene which maps to human chromosome 22. Mutations in several of the genes that map to chromosome 22 are involved in the development of Phelan-McDermid syndrome, neurofibromatosis type 2, autism and schizophrenia. Additionally, translocations between chromosomes 9 and 22 may lead to the formation of the Philadelphia chromosome and the subsequent production of the novel fusion protein Bcr-Abl, a potent cell proliferation activator found in several types of leukemias.
Supplier:  Invitrogen
Description:   Thermo Scientific™ Peptide Digest Assay Standard is a validated protein digest reference sample optimized for use in quantitative peptide assays to improve reproducibility and accuracy.Robust peptide assay standard—the only commercially available peptide digest standard that has been developed for use in a quantitative peptide assayValidated—validated for both the Pierce Quantitative Fluorometric Peptide Assay and the Pierce Quantitative Colorimetric Peptide Assay with comparable standard curves using both assaysStable—liquid formulation is stored at 4⁰C, eliminating variability due to freeze-thawsEasy-to-use—provided in a liquid format with a known peptide concentrationThe Peptide Digest Assay Standard was designed as reference standard for use with the Pierce Quantitative Fluorometric and Colorimetric Peptide Assays to augment the reproducibility and accuracy of peptide quantitation in a microplate-based assay.The reference protein has been digested with MS-grade trypsin to minimize missed cleavages
Catalog Number: (10749-244)

Supplier:  Prosci
Description:   PDIA1 (protein disulfide isomerase family A member 1) is the beta subunit of prolyl 4-hydroxylase, a highly abundant multifunctional enzyme that belongs to the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, this enzyme is involved in hydroxylation of prolyl residues in preprocollagen. PDIA1 is also a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds. Other known functions include its ability to act as a chaperone that inhibits aggregation of misfolded proteins in a concentration-dependent manner, its ability to bind thyroid hormone, its role in both the influx and efflux of S-nitrosothiol-bound nitric oxide, and its function as a subunit of the microsomal triglyceride transfer protein complex.

Supplier:  Bioss
Description:   Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L (By similarity). Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. 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. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E
Supplier:  Bioss
Description:   Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L (By similarity). Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. 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. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E

Supplier:  Bioss
Description:   ZPI, also known as SERPINA10 (serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 10) or PZI, is a 444 amino acid secreted protein that functions as a Protein Z-dependent protease inhibitor. Expressed by the liver, ZPI is secreted into the plasma where, in the presence of calcium, Protein Z and phospholipids, it inhibits the activated pro-coagulation factors X and XI (Factor X and Factor XI). This inhibition helps properly regulate intravenous blood clotting. ZPI, a member of the serpin protein family, contains five potential N-linked glycosylation sites and a tyrosine at position 387 which, when disrupted, renders ZPI inactive. Defects in the gene encoding ZPI may increase susceptibility to venous thrombosis, the formation of blood clots within a vein.

Supplier:  Bioss
Description:   ZPI, also known as SERPINA10 (serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 10) or PZI, is a 444 amino acid secreted protein that functions as a Protein Z-dependent protease inhibitor. Expressed by the liver, ZPI is secreted into the plasma where, in the presence of calcium, Protein Z and phospholipids, it inhibits the activated pro-coagulation factors X and XI (Factor X and Factor XI). This inhibition helps properly regulate intravenous blood clotting. ZPI, a member of the serpin protein family, contains five potential N-linked glycosylation sites and a tyrosine at position 387 which, when disrupted, renders ZPI inactive. Defects in the gene encoding ZPI may increase susceptibility to venous thrombosis, the formation of blood clots within a vein.
Catalog Number: (10748-816)

Supplier:  Prosci
Description:   MPYS Antibody: MPYS is a recently identified plasma membrane tetraspanner that is associated with major histocompatibility complex class II (MHC-II) and mediates its transduction of apoptotic signals. It has also been found to be associated with VISA, a mitochondrial protein that acts as an adaptor in virus-triggered signaling. MPYS also interacts with IRF3 and recruits the kinase TBK1 to the VISA-associated complex, acting as a critical mediator of virus-triggered IRF3 activation and interferon (IFN) expression. It is thought that the binding of nucleic acid to the innate immune protein RIG-I causes complex formation between RIG-I, VISA, and MPYS. This complex then recruits TBK1 to phosphorylate IRF3 which then directly activates IFN transcription. At least three isoforms of MPYS are known to exist.
Catalog Number: (75789-540)

Supplier:  Prosci
Description:   Interleukin-1 Receptor Accessory Protein (IL-1RAcP) is a member of the interleukin-1 receptor family. It contains three Ig-like C2-type domains in the extracellular region and a long cytoplasmic domain implicated in signal transduction. IL-1RAcP acts as a non-ligand binding accessory component of the receptors for IL1 alpha, IL1 beta and IL33. IL-1RAcP mediates interleukin-1-dependent activation of NF-kappa-B. It is part of the membrane-bound form of the IL-1 receptor. IL-1 RAcP takes part in the Signaling ways by the formation of a ternary complex containing IL1R1, TOLLIP, MYD88, and IRAK1 or IRAK2. In addition, IL-1RAcP modulates the response to interleukins by associating with soluble IL1R1 and enhancing interleukin-binding to the decoy receptor.

Supplier:  Bioss
Description:   Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses).
Supplier:  Bioss
Description:   Contactin 2 is a neuronal cell adhesion molecule (CAM) that influences the formation of axon connections in the developing nervous system. Contactin 2 is a member of the immunoglobulin superfamily (IgSF) and contains a glycosylphosphatidylinositol-anchor, six immunogobulin (Ig)-like and four Fibronectin type III (FNIII)-like domains. Contactin 2 is expressed predominantly during neural development on the cell membrane of axons in nerve fiber tracts in order to guide commissural axons without promoting their growth. Contactin 2 binds with NgCAM in the plane of the same membrane (cis-binding). The Contactin 2 heterophilic (Contactin 2/NgCAM and Contactin 2/NrCAM) binding sites are localized to the first four Ig domains. The Contactin 2 homophilic (Contactin 2/Contactin 2) binding site is localized to the FNIII domain.
Catalog Number: (10353-856)

Supplier:  Bioss
Description:   Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fibre is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. Covalent modifications of the canonical core histones, including acetylation, phosphorylation, methylation, and monoubiquitination are used to mark nucleosomes to create chromatin domains with a range of functions. The information encoded by histone modifications can contribute to the formation and/or maintenance of transcriptionally active and inactive chromatin in response to various signalling pathways.
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