Text Search >
[4-(Thien-2-yl)phenyl]methanol
Print…
You Searched For:
128,600 results were found
[4-(Thien-2-yl)phenyl]methanol
Catalog Number:
(10283-768)
Supplier:
Bioss
Description:
ATF2 is a member of the ATF/CREB family of basic region leucine zipper DNA binding proteins that regulates transcription by binding to a consensus cAMP response element (CRE) in the promoter of various viral and cellular genes. Many of these genes are important in cell growth and differentiation, and in stress and immune responses. ATF2 is a nuclear protein that binds DNA as a dimer and can form dimers with members of the ATF/CREB and Jun/Fos families. It is a stronger activator as a heterodimer with cJun than as a homodimer. Several isoforms of ATF2 arise by differential splicing. The stable native full length ATF2 is transcriptionally inactive as a result of an inhibitory direct intramolecular interaction of its carboxy terminal DNA binding domain with the amino terminal transactivation domain. Following dimerization ATF2 becomes a short lived protein that undergoes ubiquitination and proteolysis, seemingly in a protein phosphatase-dependent mechanism. Stimulation of the transcriptional activity of ATF2 occurs following cellular stress induced by several genotoxic agents, inflammatory cytokines, and UV irradiation. This activation requires phosphorylation of two threonine residues in ATF2 by both JNK/SAP kinase and p38 MAP kinase. ATF2 is abundantly expressed in brain.
Catalog Number:
(10281-028)
Supplier:
Bioss
Description:
ATF2 is a member of the ATF/CREB family of basic region leucine zipper DNA binding proteins that regulates transcription by binding to a consensus cAMP response element (CRE) in the promoter of various viral and cellular genes. Many of these genes are important in cell growth and differentiation, and in stress and immune responses. ATF2 is a nuclear protein that binds DNA as a dimer and can form dimers with members of the ATF/CREB and Jun/Fos families. It is a stronger activator as a heterodimer with cJun than as a homodimer. Several isoforms of ATF2 arise by differential splicing. The stable native full length ATF2 is transcriptionally inactive as a result of an inhibitory direct intramolecular interaction of its carboxy terminal DNA binding domain with the amino terminal transactivation domain. Following dimerization ATF2 becomes a short lived protein that undergoes ubiquitination and proteolysis, seemingly in a protein phosphatase-dependent mechanism. Stimulation of the transcriptional activity of ATF2 occurs following cellular stress induced by several genotoxic agents, inflammatory cytokines, and UV irradiation. This activation requires phosphorylation of two threonine residues in ATF2 by both JNK/SAP kinase and p38 MAP kinase. ATF2 is abundantly expressed in brain.
Catalog Number:
(501809-BL)
Supplier:
Biolegend
Description:
APC anti-human IL-12/IL-23 p40 (monomer, dimer, heterodimer) [C11.5]; Isotype: Mouse IgG1, κ; Reactivity: Human, IL-12/IL-23 p40 subunit (monomer, homodimer and heterodimer IL-12 p35/p40 or IL-23 p19/p40); Apps: ICFC; Size: 25 tests
Catalog Number:
(76288-420)
Supplier:
Enzo Life Sciences
Description:
Produced in <i>E. coli.</i> Contains 153/306 amino acids.
Catalog Number:
(10107-458)
Supplier:
Prosci
Description:
NFYC is one subunit of a trimeric complex, forming a highly conserved transcription factor that binds with high specificity to CCAAT motifs in the promoter regions in a variety of genes. NFYC forms a tight dimer with the B subunit, a prerequisite for subunit A association. The resulting trimer binds to DNA with high specificity and affinity.The protein encoded by this gene is one subunit of a trimeric complex, forming a highly conserved transcription factor that binds with high specificity to CCAAT motifs in the promoter regions in a variety of genes. This gene product, subunit C, forms a tight dimer with the B subunit, a prerequisite for subunit A association. The resulting trimer binds to DNA with high specificity and affinity. Subunits B and C each contain a histone-like motif. Observation of the histone nature of these subunits is supported by two types of evidence; protein sequence alignments and experiments with mutants. Additional regulation, preliminarily supported by the EST database, may be represented by alternative splicing in this subunit.
Catalog Number:
(10236-494)
Supplier:
Bioss
Description:
NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p15, NFKB1/p5, REL and NFKB2/p52 and the heterodimeric p65-p5 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p5 and p65-c-Rel complexes are transcriptional activators. The NF-kappa-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. The inhibitory effect of I-kappa-B upon NF-kappa-B the cytoplasm is exerted primarily through the interaction with p65. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1.
Catalog Number:
(10355-690)
Supplier:
Bioss
Description:
The Fos gene family consists of 4 members: FOS, FOSB, FOSL1, and FOSL2. These genes encode leucine zipper proteins that can dimerize with proteins of the JUN family, thereby forming the transcription factor complex AP-1. As such, the FOS proteins have been implicated as regulators of cell proliferation, differentiation, and transformation. [provided by RefSeq].
Catalog Number:
(77437-002)
Supplier:
Bioss
Description:
The protein encoded by this gene is a transmembrane glycoprotein that is a member of the protein kinase superfamily. This protein is a receptor for members of the epidermal growth factor family. EGFR is a cell surface protein that binds to epidermal growth factor. Binding of the protein to a ligand induces receptor dimerization and tyrosine autophosphorylation and leads to cell proliferation. Mutations in this gene are associated with lung cancer. Multiple alternatively spliced transcript variants that encode different protein isoforms have been found for this gene. (provided by RefSeq, Jul 2010).
Catalog Number:
(10405-344)
Supplier:
Bioss
Description:
Twist2 (Twist homolog 2) is a basic helix-loop-helix (bHLH) transcription factor which acts as a transcriptional repressor. It binds to the E-box consensus sequence 5'-CANNTG-3' and inhibits transcriptional activation by MYOD1, MYOG, MEF2A and MEF2C. Efficient DNA binding requires dimerization with another bHLH protein. Twist2 inhibits the premature or ectopic differentiation of preosteoblast cells during osteogenesis.
Catalog Number:
(76195-634)
Supplier:
Prosci
Description:
This antibody recognizes a polypeptide of ~6.5kDa, identified as Estrogen Inducible Protein pS2. The antibody's epitope is localized between amino acids 57-84. pS2 is a trefoil peptide. Trefoil peptides are protease resistant molecules secreted throughout the gut that play a role in mucosal healing. These peptides contain three intrachain disulfide bonds, forming the trefoil motif, or P-domain. Estrogen Inducible Protein pS2 is known to form dimers and this dimerization is thought to play a role in its protective and healing properties. About 60% of breast carcinomas are positive for estrogen inducible protein pS2. Staining is cytoplasmic, often with localization to the Golgi apparatus. It is shown to be localized in normal stomach mucosa, gastric fluid, goblet cells in the colon and small intestine, and in ulcerations of the gastrointestinal tract. Several studies have shown that estrogen inducible protein pS2 is primarily expressed in estrogen receptor-positive breast tumors and it may define a subset of estrogen-dependent tumors that displays an increased likelihood of response to endocrine therapy.
Supplier:
Biotium
Description:
Eukaryotic histones are basic and water-soluble nuclear proteins. They form hetero-octameric nucleosome particles by wrapping 146 base pairs of DNA in a left-handed super-helical turn sequentially to form chromosomal fiber. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form the octamer; formed of two H2A-H2B dimers and two H3-H4 dimers, forming two nearly symmetrical halves by tertiary structure. Over 80% of nucleosomes contain the linker Histone H1, derived from an intronless gene that interacts with linker DNA between nucleosomes and mediates compaction into higher order chromatin. Histones are subject to posttranslational modification by enzymes primarily on their N-terminal tails, but also in their globular domains. Such modifications include methylation, citrullination, acetylation, phosphorylation, sumoylation, ubiquitination and ADP-ribosylation.
CF® dyes are Biotium's next-generation fluorescent dyes. CF®640R is a far-red fluorescent dye (Ex/Em 642/662 nm) with excellent brightness, and the best photostabiity among spectrally-similar dyes.
Supplier:
Enzo Life Sciences
Description:
The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.
Supplier:
Biotium
Description:
Thyroglobulin is a 660 kDa dimeric pre-protein with mutiple glycosylation sites. It is produced by and processed within the thyroid gland to produce the hormone thyroxine and triiodothyronine. Prior to forming dimers, thyroglobulin monomers undergo conformational maturation in the endoplasmic reticulation. The vast majority of follicular carcinomas of the thyroid will give positive immunoreactivity for anti-thyroglobulin even though sometimes only focally. Poorly differentiated carcinomas of the thyroid are frequently anti-thyroglobulin negative. Adenocarcinomas of other-than-thyroid origin do not react with this antibody. This antibody is useful in identification of thyroid carcinoma of the papillary and follicular types. Presence of thyroglobulin in metastatic lesions establishes the thyroid origin of tumor. Anti-thyroglobulin, combined with anti-calcitonin, can identify medullary carcinomas of the thyroid. Furthermore, anti-thyroglobulin, combined with anti-TTF1, can be a reliable marker to differentiate between primary thyroid and lung neoplasms.
Supplier:
Biotium
Description:
Eukaryotic histones are basic and water-soluble nuclear proteins. They form hetero-octameric nucleosome particles by wrapping 146 base pairs of DNA in a left-handed super-helical turn sequentially to form chromosomal fiber. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form the octamer; formed of two H2A-H2B dimers and two H3-H4 dimers, forming two nearly symmetrical halves by tertiary structure. Over 80% of nucleosomes contain the linker Histone H1, derived from an intronless gene that interacts with linker DNA between nucleosomes and mediates compaction into higher order chromatin. Histones are subject to posttranslational modification by enzymes primarily on their N-terminal tails, but also in their globular domains. Such modifications include methylation, citrullination, acetylation, phosphorylation, sumoylation, ubiquitination and ADP-ribosylation.
CF® dyes are Biotium's next-generation fluorescent dyes. CF®594 is a deep red fluorescent dye (Ex/Em 593/614 nm). It yields the brightest conjugates among spectrally similar dyes, and has excellent photostability.
Supplier:
Biotium
Description:
Eukaryotic histones are basic and water-soluble nuclear proteins. They form hetero-octameric nucleosome particles by wrapping 146 base pairs of DNA in a left-handed super-helical turn sequentially to form chromosomal fiber. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form the octamer; formed of two H2A-H2B dimers and two H3-H4 dimers, forming two nearly symmetrical halves by tertiary structure. Over 80% of nucleosomes contain the linker Histone H1, derived from an intronless gene that interacts with linker DNA between nucleosomes and mediates compaction into higher order chromatin. Histones are subject to posttranslational modification by enzymes primarily on their N-terminal tails, but also in their globular domains. Such modifications include methylation, citrullination, acetylation, phosphorylation, sumoylation, ubiquitination and ADP-ribosylation.
CF® dyes are Biotium's next-generation fluorescent dyes. CF®640R is a far-red fluorescent dye (Ex/Em 642/662 nm) with excellent brightness, and the best photostabiity among spectrally-similar dyes.
Catalog Number:
(10106-160)
Supplier:
Prosci
Description:
The C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein: a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. The C/EBP family consist of several related proteins, C/EBP alpha, C/EBP beta, C/EBP gamma, and C/EBP delta, that form homodimers and that form heterodimers with each other. CCAAT/enhancer binding protein gamma (CEBPG) may cooperate with Fos to bind PRE-I enhancer elements.The C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein: a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. The C/EBP family consist of several related proteins, C/EBP alpha, C/EBP beta, C/EBP gamma, and C/EBP delta, that form homodimers and that form heterodimers with each other. CCAAT/enhancer binding protein gamma may cooperate with Fos to bind PRE-I enhancer elements.
Inquire for Price
Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the
 is still displayed and you need assistance, please call us at 1-800-932-5000.
Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the
is still displayed and you need assistance, please call us at 1-800-932-5000.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at Regulatory_Affairs@vwr.com
-Additional Documentation May be needed to purchase this item. A VWR representative will contact you if needed.
This product has been blocked by your organization. Please contact your purchasing department for more information.
The original product is no longer available. The replacement shown is available.
This product is no longer available. Alternatives may be available by searching with the VWR Catalog Number listed above. If you need further assistance, please call VWR Customer Service at 1-800-932-5000.
|
|||||||||
List View
