Text Search >
4-Benzyloxy-3,5-dimethylphenylboronic+acid
Print…
You Searched For:
125,034 results were found
4-Benzyloxy-3,5-dimethylphenylboronic+acid
Catalog Number:
(76110-250)
Supplier:
Bioss
Description:
The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localizes to cytosol but shifts to mitochondria upon co-localization with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.
Catalog Number:
(10257-864)
Supplier:
Bioss
Description:
A mutation of the DYT1 gene, which codes for TorsinA, has been identified as the cause of one form of autosomal dominantly inherited dystonia. Early-onset torsion dystonia is a movement disorder, characterized by twisting muscle contractures, that begins in childhood. Symptoms are believed to result from altered neuronal communication in the basal ganglia. TorsinA comprises 332 amino acids. TorsinA is widely expressed throughout the mouse central nervous system and is detected in the majority of neurons in nearly all regions. The proteins display cytoplasmic distribution, although in some types of neurons localization is perinuclear. TorsinA often performs chaperone-like functions that assist in the assembly, operation, or dis-assembly of protein complexes. The gene which encodes TorsinA has high homology to three additional mammalian genes and a nematode gene and distal similarity to the family of heat-shock proteins and the Clp protease family. The gene which encodes TorsinA maps to human chromosome 9q34.
Catalog Number:
(10295-136)
Supplier:
Bioss
Description:
The Gab family of adaptor proteins function as molecular scaffolds that mediate protein recruit-ment to RTKs. Cytokine/growth factor triggering of protein tyrosine kinase receptors (RTKs) initiates signaling cascades that progress to the nucleus where signals for activation, proliferation and differentiation occur. This scaffolding mechanism represents a critical link in cytokine/growth factor signaling routes. Gab 1-4 contain Pleckstrin homology and potential binding sites for SH2 and SH3 domain-containing proteins. The recruitment of signaling partners to Gab family members is phosphorylation-dependent. Insulin receptor and EGF receptor signaling are among the cascades that rely on Gab family members to elicit a nuclear response to an extracellular stimulus. Gab 4 (GRB2-associated-binding protein 4), also designated GRB2-associated-binding protein 2-like (Gab 2-like), is a 574 amino acid protein that shares 62% sequence similarity with Gab 2 and contains one Pleckstrin homology domain.
Catalog Number:
(10749-136)
Supplier:
Prosci
Description:
Apaf-1 Monoclonal Antibody: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. The mammalian homologous of the key cell death gene CED-4 in C. elegans was identified recently from human and mouse and designated Apaf1 for apoptosis protease-activating factor 1. Apaf1 binds to cytochrome c (Apaf2) and caspase-9 (Apaf3), which leads to caspase-9 activation. Activated caspase-9 in turn cleaves and activates caspase-3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. Apaf1 can also associate with caspase-4 and caspase-8. Apaf1 transcript is ubiquitously expressed in human tissues.
Catalog Number:
(10247-660)
Supplier:
Bioss
Description:
The cadherins are a family of Ca2+-dependent adhesion molecules that function to mediate cell-cell binding events that are critical to the maintenance of cell structure and morphogenesis. EY-cadherin, also known as CDH18 (cadherin 18), CDH14 (cadherin 14), CDH24 or CDH14L, is a 790 amino acid single-pass type I membrane protein that contains five cadherin domains. One of several members of the cadherin superfamily, EY-cadherin functions as a type II classical cadherin that is expressed specifically in the central nervous system (CNS), where it plays a role in cell-cell binding events. Specifically, EY-cadherin is thought to be involved in axon guidance and outgrowth, as well as synaptic adhesion within the CNS. EY-cadherin contains a highly conserved C-terminal domain characteristic of all cadherins, but lacks the HAV cell adhesion sequence that is specific to type I cadherins. The gene encoding EY-cadherin is located within a region on chromosome five that is commonly deleted in carcinomas, implicating EY-cadherin as a potential tumor suppressor.
Catalog Number:
(10248-204)
Supplier:
Bioss
Description:
The cadherins represent a family of Ca2+-dependent adhesion molecules that function to mediate cell to cell binding that is critical for the maintenance of structure and morphogenesis. Cadherins each contain a large extracellular domain at the N-terminus, which is characterized by a series of five homologous repeats, the most distal of which is thought to be responsible for binding specificity. The relatively short C-terminal intracellular domain interacts with a variety of cytoplasmic proteins, including ∫-catenin, to regulate cadherin function. The cadherin superfamily includes cadherins, protocadherins, desmogleins and desmocollins. FAT3 (FAT tumor suppressor homolog 3, also known as CDHF15 or CDHR10, is a 4,589 amino acid single-pass type I membrane protein expressed in ES cells, primitive neuroectoderm, fetal brain, infant brain, adult neural tissues and prostate. Containing thirty-three cadherin domains, four EGF-like domains and one laminin G-like domain, FAT3 may participate in the interactions between neurites derived from specific subsets of neurons during development.
Catalog Number:
(10276-520)
Supplier:
Bioss
Description:
Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc-finger proteins contain a Kruppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. As a member of the krueppel C2H2-type zinc-finger protein family, ZNF131 (Zinc finger protein 131) is a 623 amino acid nuclear protein that contains one BTB (POZ) domain and six C2H2-type zinc fingers. With predominant expression found in brain, it is likely that ZNF131 plays a role as a transcription regulator during development and organogenesis of the adult central nervous system. ZNF131 also represses ER Alpha (Estrogen receptor alpha)-mediated transactivation by interrupting ER?binding to the estrogen-response element. There are two isoforms of ZNF131 that are produced as a result of alternative splicing events.
Catalog Number:
(10276-526)
Supplier:
Bioss
Description:
Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc-finger proteins contain a Kruppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. As a member of the krueppel C2H2-type zinc-finger protein family, ZNF131 (Zinc finger protein 131) is a 623 amino acid nuclear protein that contains one BTB (POZ) domain and six C2H2-type zinc fingers. With predominant expression found in brain, it is likely that ZNF131 plays a role as a transcription regulator during development and organogenesis of the adult central nervous system. ZNF131 also represses ER Alpha (Estrogen receptor alpha)-mediated transactivation by interrupting ER?binding to the estrogen-response element. There are two isoforms of ZNF131 that are produced as a result of alternative splicing events.
Catalog Number:
(10257-868)
Supplier:
Bioss
Description:
A mutation of the DYT1 gene, which codes for TorsinA, has been identified as the cause of one form of autosomal dominantly inherited dystonia. Early-onset torsion dystonia is a movement disorder, characterized by twisting muscle contractures, that begins in childhood. Symptoms are believed to result from altered neuronal communication in the basal ganglia. TorsinA comprises 332 amino acids. TorsinA is widely expressed throughout the mouse central nervous system and is detected in the majority of neurons in nearly all regions. The proteins display cytoplasmic distribution, although in some types of neurons localization is perinuclear. TorsinA often performs chaperone-like functions that assist in the assembly, operation, or dis-assembly of protein complexes. The gene which encodes TorsinA has high homology to three additional mammalian genes and a nematode gene and distal similarity to the family of heat-shock proteins and the Clp protease family. The gene which encodes TorsinA maps to human chromosome 9q34.
Catalog Number:
(10301-484)
Supplier:
Bioss
Description:
Nolz 1 is a 646 amino acid nuclear protein that is thought to function as a transcriptional repressor and is highly expressed in developing striatum. Additionally, Nolz-1 has been suggested to play a role in neural differentiation. A member of the Elbow/Noc family, Nolz-1 exists as three alternatively spliced isoforms and contains one C2H2-type zinc finger. The gene encoding Nolz-1 maps to human chromosome 10, which makes up approximately 4.5% of total DNA in cells and encodes nearly 1,200 genes. Several protein-coding genes, including those that encode for chemokines, cadherins, excision repair proteins, early growth response factors (Egrs) and fibroblast growth receptors (FGFRs), are located on chromosome 10. Defects in some of the genes that map to chromosome 10 are associated with Charcot-Marie Tooth disease, Jackson-Weiss syndrome, Usher syndrome, nonsyndromatic deafness, Wolman’s syndrome, Cowden syndrome, multiple endocrine neoplasia type 2 and porphyria.
Catalog Number:
(10279-932)
Supplier:
Bioss
Description:
The Notch signaling pathway is an evolutionary conserved system that is involved in intracellular communication. Notch receptors play an important role in development and cell-fate decisions. Notchless is a loss-of-function mutant allele that encodes for protein NLE1 (notchless homolog 1). NLE1 is a 485 amino acid WD40-repeat protein that binds to the cytoplasmic domain of Notch, regulating its signaling activity in Drosophila melanogaster and in mice. Deletion of the NLE1 gene in mice during the early stages of development results in embryonic death, while gene deletion in the late stages of development leads to activation of a caspase-3-dependent apoptotic pathway. In plants, NLE1 is crucial for normal cellular growth and development. Under-expression during shoot proliferation causes pleiotropic defects such as delayed flowering and abnormal organ maturation. It may also play a role in 60S ribosomal subunit biogenesis in yeast. NLE1 contains eight WD40 domains and produces one isoform due to alternative splicing.
Catalog Number:
(10257-866)
Supplier:
Bioss
Description:
A mutation of the DYT1 gene, which codes for TorsinA, has been identified as the cause of one form of autosomal dominantly inherited dystonia. Early-onset torsion dystonia is a movement disorder, characterized by twisting muscle contractures, that begins in childhood. Symptoms are believed to result from altered neuronal communication in the basal ganglia. TorsinA comprises 332 amino acids. TorsinA is widely expressed throughout the mouse central nervous system and is detected in the majority of neurons in nearly all regions. The proteins display cytoplasmic distribution, although in some types of neurons localization is perinuclear. TorsinA often performs chaperone-like functions that assist in the assembly, operation, or dis-assembly of protein complexes. The gene which encodes TorsinA has high homology to three additional mammalian genes and a nematode gene and distal similarity to the family of heat-shock proteins and the Clp protease family. The gene which encodes TorsinA maps to human chromosome 9q34.
Catalog Number:
(76333-998)
Supplier:
Biosensis
Description:
Visinin (sometimes known as hippocalcin-like protein 3, HLP3, HPCAL3, HUVISL1, VLP-1, VILIP and VILIP-1) was originally isolated biochemically from chicken retina as a major protein of about 24kDa on SDS-PAGE (1). Following cloning and sequencing of visinin, several visinin like proteins were discovered by homology screening (2, 3). One of these, Visinin-like protein 1 is a small Calcium binding protein which is very abundant in the nervous system and is found only in neurons, though different neurons have different levels of expression (4, 5). It is particularly concentrated in cerebellar Purkinje cells, and tends to be most abundant in perikarya and dendrites. The protein belongs to the large superfamly of calmodulin and paravalbumin type proteins which function by binding Calcium ions. Calcium binding alters the confomation of these proteins and allow them to interact with other binding partners, the properties of which they may alter. Visinin-like protein 1 has four "EF hand" domains, which are negatively charged helix-turn-helix peptides which are responsible for Calcium binding. Visinin-like protein 1 is 191 amino acids in size and has a molecular weight on SDS-PAGE of 22kDa. The protein has recently been suggested to be a useful biomarker of Alzheimer's disease and traumatic brain injury (6, 7, 8).
Catalog Number:
(10749-840)
Supplier:
Prosci
Description:
DRAM Antibody: Damage-regulated autophagy modulator (DRAM) is a p53 target gene encoding a lysosomal protein that induces autophagy, a process that degrades cytosolic proteins and organelles. It has been suggested that activation of DRAM by p53 is simultaneous to the activation by p53 of one or more proapoptotic genes such as PUMA, Bax, etc., and that the signaling pathways regulated by these genes promote a full cell death response. By itself, DRAM cannot induce apoptosis, but the fact that it is inactivated in certain cancers highlights the importance of DRAM and suggests that autophagy may play a more important role in cancer than initially suspected. At least two different isoforms of DRAM are known to exist.
Catalog Number:
(10301-486)
Supplier:
Bioss
Description:
Nolz 1 is a 646 amino acid nuclear protein that is thought to function as a transcriptional repressor and is highly expressed in developing striatum. Additionally, Nolz-1 has been suggested to play a role in neural differentiation. A member of the Elbow/Noc family, Nolz-1 exists as three alternatively spliced isoforms and contains one C2H2-type zinc finger. The gene encoding Nolz-1 maps to human chromosome 10, which makes up approximately 4.5% of total DNA in cells and encodes nearly 1,200 genes. Several protein-coding genes, including those that encode for chemokines, cadherins, excision repair proteins, early growth response factors (Egrs) and fibroblast growth receptors (FGFRs), are located on chromosome 10. Defects in some of the genes that map to chromosome 10 are associated with Charcot-Marie Tooth disease, Jackson-Weiss syndrome, Usher syndrome, nonsyndromatic deafness, Wolman’s syndrome, Cowden syndrome, multiple endocrine neoplasia type 2 and porphyria.
Catalog Number:
(89359-260)
Supplier:
Genetex
Description:
SIR2, one of the silent information regulator genes, encodes a protein that promotes a compact chromatin structure, thereby preventing or silencing gene transcription at selected loci. SIR2 belongs to a family of proteins that is found in organisms ranging from bacteria to complex eukaryotes. Members of this family contain a 250 amino acid core domain that shares about 25-60% sequence identity. Silencing occurs as a series of events initiated by formation of Sir complexes (Sir2, Sir3, Sir4). The complexes are recruited to their chromosome targets via interactions with DNA-binding proteins, followed by deacetylation of histones H3 and H4. A final step required for telomeric silencing is binding of the complex to the deacetylated histones and recruitment of the telosome to the nuclear periphery. Sir2 protein is an NAD-dependent histone deacetylase, an enzyme that removes acetyl groups from lysine residues of histone proteins and possibly other substrates. Sir2 transfers acetyl groups from its protein substrates to ADP-ribose and synthesizes o-acetyl-ADP-ribose. Through histone deacetylation, Sir2 may silence chromatin. The maintenance or silencing of chromatin may be at the center of processes leading to aging of cells and development of cancer.
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
