Text Search >
6-(Cyclopropylmethoxy)[1,1\'-biphenyl]-3-carbaldehyde
Print…
You Searched For:
127,981 results were found
6-(Cyclopropylmethoxy)[1,1\'-biphenyl]-3-carbaldehyde
|
Your search request has been modified to limit number of results. Your search was - N\\\\\\\'-[1-Cyclobutylaminopropylidene]hydrazinecarboxylic+acid-tert-b |
|||||||||
Supplier:
Enzo Life Sciences
Description:
Recommended Applications: ELISA, Flow Cytometry, ICC, IF, IHC (PS), IP, WB, Electron microscopy
Catalog Number:
(77436-940)
Supplier:
Bioss
Description:
Dosage compensation ensures that males with a single X chromosome and females with two X chromosomes have the same amount of most X-linked gene products. In Drosophila, this is acheived by enhancing the level of transcription of the X chromosome in males. Proteins such as maleless, male specific lethal 1, 2 and 3, and males absent on the first (MOF) form a dosage compensation complex (DCC) that is required for the twofold increase of transcription of the male X chromosome. The DCC is preferentially associated with many sites on the X chromosome in somatic cells of males. The binding of the DCC to the X chromosome is dependent upon histone 4 acetylation at lysine 16, which is accomplished by MOF. In mammals, MOF (also designated hMOF, MYST1, or MOZ) belongs to the MYST family of histone acetyl transferases which are characterized by a unique C2HC-type zinc finger close to their HAT domains. MOF utilizes the zinc finger domain to contact the globular part of the nucleosome as well as the histone H4 N-terminal tail substrate. The carboxy terminal domain of human MOF also has histone acetyltransferase activity directed against histones H3 and H2A, a characteristic shared with other MYST family histone acetyltransferases.
Catalog Number:
(89359-106)
Supplier:
Genetex
Description:
Histone methyltransferase. Preferentially methylates 'Lys-9' of histone H3 and 'Lys-27' of histone H3 (in vitro). H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also methylates histone H1.
Catalog Number:
(75882-520)
Supplier:
Biotium
Description:
This antibody reacts with a protein of ~66 kDa, identified as bovine serum albumin (BSA). It is a high affinity antibody and can be used for detection of traces of BSA. Bovine serum albumin (BSA) is an abundant plasma protein in cows that is important for maintaining osmotic pressure in blood plasma for proper distribution of body fluids between intravascular compartments and body tissues. BSA is a common buffer component for immunoglobulin type assays due to good solubility characteristics for water, Ca2 , Na , K , fatty acids, hormones and bilirubin. BSA makes up about half of the protein in plasma and represents the most stable and soluble protein in the plasma. It is a suitable reagent for laboratories developing immunoassays, mostly due to its availability, solubility and the numerous functional groups present for coupling. The BSA component contains several lysines that are capable of reacting with conjugation sites of linkers, making it applicable as a carrier protein for antigenic compounds.
Catalog Number:
(10304-102)
Supplier:
Bioss
Description:
Fyb (Fyn binding protein) and the anchoring proteins SKAP55 and SKAP55-R (SKAP55-related protein) associate with the tyrosine kinase p59fyn. SKAP55 and SKAP55-R bind to Fyb through their SH3 domains and function as substrates for p59Fyn in resting T cells. SKAP55 contains an N-terminal pleckstrin homology domain and a C-terminal SH3 domain binding motif of adjacent arginine and lysine residues followed by tandem tyrosines. SKAP55-R, similar in overall structure to SKAP55, contains a coiled-coil N-terminal domain. SKAP55 associates with SLAP-130, another component of the Fyn complex, which plays a role in the regulation of signaling events initiated by lymphocyte antigen receptors leading up to T cell activation. The human SKAP55 gene maps to chromosome 17q21.32 and encodes a 359 amino acid protein.
Catalog Number:
(10359-830)
Supplier:
Bioss
Description:
Tripartite motif-containing protein 32 (TRIM32) belongs to the tripartite motif (TRIM) protein family. TRIM32, like all TRIM proteins, contains a domain structure composed of a B-box, a RING-finger and a coiled-coil motif. Additionally, TRIM32 has six C-terminal NHL domains; it is expressed mainly in the skeletal muscle. The TRIM32 gene encodes an E3 ubiquitin ligase, a protein that attaches ubiquitin to a lysine residue on a target protein and acts in conjunction with ubiquitin-conjugating enzymes UbcH5a, UbcH5c and UbcH6. Mutations in the TRIM32 gene cause two forms of autosomal recessive muscular dystrophy designated limb girdle muscular dystrophy type 2H (LGMD2H) and sarcotubular myopathy (STM). TRIM32 mutations can also result in Bardet-Biedl syndrome (BBS), an autosomal recessive disorder characterized by pigmentary retinopathy, polydactyly, hypogenitalism, renal abnormalities, learning disabilities and obesity.
Catalog Number:
(10359-472)
Supplier:
Bioss
Description:
Tripartite motif-containing protein 32 (TRIM32) belongs to the tripartite motif (TRIM) protein family. TRIM32, like all TRIM proteins, contains a domain structure composed of a B-box, a RING-finger and a coiled-coil motif. Additionally, TRIM32 has six C-terminal NHL domains; it is expressed mainly in the skeletal muscle. The TRIM32 gene encodes an E3 ubiquitin ligase, a protein that attaches ubiquitin to a lysine residue on a target protein and acts in conjunction with ubiquitin-conjugating enzymes UbcH5a, UbcH5c and UbcH6. Mutations in the TRIM32 gene cause two forms of autosomal recessive muscular dystrophy designated limb girdle muscular dystrophy type 2H (LGMD2H) and sarcotubular myopathy (STM). TRIM32 mutations can also result in Bardet-Biedl syndrome (BBS), an autosomal recessive disorder characterized by pigmentary retinopathy, polydactyly, hypogenitalism, renal abnormalities, learning disabilities and obesity.
Catalog Number:
(10294-412)
Supplier:
Bioss
Description:
Fyb (Fyn binding protein) and the anchoring proteins SKAP55 (src kinase-associated phosphoprotein) and SKAP55-R (SKAP55-related protein) associate with the tyrosine kinase p59fyn (1–3). SKAP55 and SKAP55-R bind to Fyb through their SH3 domains and function as substrates for p59Fyn in resting T cells (1–3). SKAP55 contains an amino-terminal pleckstrin homology domain and a carboxy-terminal SH3 domain binding motif of adjacent arginine and lysine residues followed by tandem tyrosines (i.e. RKxxYxxY) (4,5). SKAP55-R, similar in overall structure to SKAP55, contains a coiled-coil N-terminal domain (1,2). SKAP55 associates with SLAP-130, another component of the Fyn complex, which plays a role in the regulation of signaling events initiated by lymphocyte antigen receptors leading up to T cell activation (6). The human Fyb gene maps to chromosome 5p13.1 and encodes a 783 amino acid protein (7).
Catalog Number:
(10293-810)
Supplier:
Bioss
Description:
Fyb (Fyn binding protein) and the anchoring proteins SKAP55 (src kinase-associated phosphoprotein) and SKAP55-R (SKAP55-related protein) associate with the tyrosine kinase p59fyn (1–3). SKAP55 and SKAP55-R bind to Fyb through their SH3 domains and function as substrates for p59Fyn in resting T cells (1–3). SKAP55 contains an amino-terminal pleckstrin homology domain and a carboxy-terminal SH3 domain binding motif of adjacent arginine and lysine residues followed by tandem tyrosines (i.e. RKxxYxxY) (4,5). SKAP55-R, similar in overall structure to SKAP55, contains a coiled-coil N-terminal domain (1,2). SKAP55 associates with SLAP-130, another component of the Fyn complex, which plays a role in the regulation of signaling events initiated by lymphocyte antigen receptors leading up to T cell activation (6). The human Fyb gene maps to chromosome 5p13.1 and encodes a 783 amino acid protein (7).
Catalog Number:
(10329-708)
Supplier:
Bioss
Description:
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation. Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A.
Catalog Number:
(10304-098)
Supplier:
Bioss
Description:
Fyb (Fyn binding protein) and the anchoring proteins SKAP55 and SKAP55-R (SKAP55-related protein) associate with the tyrosine kinase p59fyn. SKAP55 and SKAP55-R bind to Fyb through their SH3 domains and function as substrates for p59Fyn in resting T cells. SKAP55 contains an N-terminal pleckstrin homology domain and a C-terminal SH3 domain binding motif of adjacent arginine and lysine residues followed by tandem tyrosines. SKAP55-R, similar in overall structure to SKAP55, contains a coiled-coil N-terminal domain. SKAP55 associates with SLAP-130, another component of the Fyn complex, which plays a role in the regulation of signaling events initiated by lymphocyte antigen receptors leading up to T cell activation. The human SKAP55 gene maps to chromosome 17q21.32 and encodes a 359 amino acid protein.
Catalog Number:
(10800-618)
Supplier:
Rockland Immunochemical
Description:
The mammalian cbl family of ubiquitin ligases consists of three homologs known as cbl (also known as c-Cbl), Cbl-B, and Cbl-3 which share highly conserved a tyrosine-kinase-binding domain, linker and RING finger domain in their amino-terminal halves. Similar to other E3 ubiquitin ligases, Cbl catalyzes the transfer of ubiquitin from an E2 or Ubc (ubiquitin-conjugating) enzyme to the e-amino group of a lysine residue of the substrate protein. Cbl acts to negatively regulate many types of cell-surface receptors, including the Syk protein tyrosine kinase family. Cbl is thought to be involved in T- and B-cell signaling, in addition to thymus development. Of the three known homologs in the cbl family, cbl antibody reacts specifically with cbl. Multiple isoforms of cbl have been reported.
Catalog Number:
(10303-900)
Supplier:
Bioss
Description:
Fyb (Fyn binding protein) and the anchoring proteins SKAP55 and SKAP55-R (SKAP55-related protein) associate with the tyrosine kinase p59fyn. SKAP55 and SKAP55-R bind to Fyb through their SH3 domains and function as substrates for p59Fyn in resting T cells. SKAP55 contains an N-terminal pleckstrin homology domain and a C-terminal SH3 domain binding motif of adjacent arginine and lysine residues followed by tandem tyrosines (i.e. RKxxYxxY). SKAP55-R, similar in overall structure to SKAP55, contains a coiled-coil N-terminal domain. SKAP55 associates with SLAP-130, another component of the Fyn complex, which plays a role in the regulation of signaling events initiated by lymphocyte antigen receptors leading up to T cell activation. The human SKAP55 gene maps to chromosome 17q21.32 and encodes a 359 amino acid protein.
Catalog Number:
(89358-378)
Supplier:
Genetex
Description:
This gene encodes a nuclear protein containing a SWIRM domain, a FAD-binding motif, and an amine oxidase domain. This protein is a component of several histone deacetylase complexes, though it silences genes by functioning as a histone demethylase. Alternative splicing results in multiple transcript variants. [provided by RefSeq]
Catalog Number:
(75928-476)
Supplier:
Rockland Immunochemical
Description:
Histones are the main constituents of the protein part of chromosomes of eukaryotic cells. They are rich in the amino acids arginine and lysine and have been greatly conserved during evolution. Histones pack the DNA into tight masses of chromatin. Two core histones of each class H2A, H2B, H3 and H4 assemble and are wrapped by 146 base pairs of DNA to form one octameric nucleosome. Histones play a internal role in the regulation of transcription, DNA repair, DNA replication and chromosomal stability. These different functions are established via a complex set of post-translational modifications which either directly or indirectly alter chromatin structure and DNA accessibility to facilitate transcriptional activation or repression or other nuclear processes. Anti-Histone H4 pan Antibody is ideal for research in Chromatin Remodeling, Gene Expression and Epigenetics.
Catalog Number:
(76011-320)
Supplier:
Prosci
Description:
Similar to acetylation and phosphorylation, histone methylation at the N-terminal tail has emerged as an important role in regulating chromatin dynamics and gene activity. Histone methylation occurs on arginine and lysine residues and is catalyzed by two families of proteins, the protein arginine methyltransferase family and the SET-domain-containing methyltransferase family. Five members have been identified in the arginine methyltransferase family. About 27 are grouped into the SET-domain family, and another 17 make up the PR domain family that is related to the SET domain family. The retinoblastoma protein-interacting zinc finger geneRIZ1 is a tumor suppressor gene and a FOUNDING member of the PR domain family. RIZ1 inactivation is commonly found in many types of human cancers and occurs through loss of mRNA expression, frame shift mutation, chromosomal deletion, and missense mutation. RIZ1 is also a tumor susceptibility gene in mice. The loss of RIZ1 mRNA in human cancers was shown to associate with DNA methylation of its promoter CpG island. Methylation of the RIZ1 promoter strongly correlated with lost or decreased RIZ1 mRNA expression in breast, liver, colon, and lung cancer cell lines as well as in liver cancer tissues.
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
