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4-(4-Chlorophenyl)butyric+acid
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4-(4-Chlorophenyl)butyric+acid
Catalog Number:
(77440-362)
Supplier:
Bioss
Description:
This gene encodes a protein belonging to the vacuolar-protein-sorting-13 gene family. In yeast, vacuolar-protein-sorting-13 proteins are involved in trafficking of membrane proteins between the trans-Golgi network and the prevacuolar compartment. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. These two represent the major variants of this gene and encode distinct isoforms. [provided by RefSeq, Jul 2008].
Catalog Number:
(10419-082)
Supplier:
Bioss
Description:
Members of the protein kinase C (PKC) family function in many extracellular receptor-mediated signal transduction pathways. See PRKCA (MIM 176960) for further background information. The PRKCM gene encodes a cytosolic serine-threonine kinase that binds to the trans-Golgi network and regulates the fission of transport carriers specifically destined to the cell surface.[supplied by OMIM]
Catalog Number:
(75791-540)
Supplier:
Prosci
Description:
Mouse ULBP1, also known as RAET1I and NKG2DL1, is a member of the ULBP/RAET1 gene family. ULBP1 plays an important role in immune responses, especially in cancer and infectious diseases, and is well-known to bind to NKG2D together with at least ULBP 2 and 3. These proteins are distantly related to major histocompatibility class I (MHC I) molecules, possessing the alpha 1 and alpha 2 Ig-like domains, but lacking the alpha 3 domain. Unlike MHC Class I, they have no capacity to bind peptide or interact with beta2-microglobulin. It can activate multiple signaling pathways in primary NK cells, gamma delta T cells, and CD8+ alpha beta T cells, resulting in the production of cytokines and chemokines.ULBP1 is expressed in wide range of tissues including heart, brain, lung, liver, bone marrow and some tumor cells, T-cells, B-cells, As an unconventional member of the MHC class I family, ULBP1 is able to interact with soluble CMV glycoprotein UL16 in CMV infected cells. The interaction with UL16 blocked the interaction with the NKG2D receptor, and thus might escape the immune surveillance. Furthermore, UL16 also causes ULBP1 to be retained in the ER and cis-Golgi apparatus so that it does not reach the cell surface. The ULBP1 regulation may have implications for development of new therapeutic strategies against cancer cells.
Catalog Number:
(10397-450)
Supplier:
Bioss
Description:
Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN and DAXX. Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation. Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53-dependent cell growth repression and apoptosis. Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity. In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML. Involved in cell proliferation during early embryonic development. Involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage: recruited to DNA damage sites following interaction with KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing UV-induced degradation of ERCC6. Contributes to the overall stabilization and trans-activation capability of the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 during HSV-1 infection. Involved in maintenance of DNA methylation via its interaction with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1, preventing their degradation and promoting DNA methylation by DNMT1. Exhibits a preference towards 'Lys-48'-linked ubiquitin chains. Increases regulatory T-cells (Treg) suppressive capacity by deubiquitinating and stabilizing the transcription factor FOXP3 which is crucial for Treg cell function (PubMed:23973222).
Catalog Number:
(10397-446)
Supplier:
Bioss
Description:
Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN and DAXX. Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation. Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53-dependent cell growth repression and apoptosis. Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity. In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML. Involved in cell proliferation during early embryonic development. Involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage: recruited to DNA damage sites following interaction with KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing UV-induced degradation of ERCC6. Contributes to the overall stabilization and trans-activation capability of the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 during HSV-1 infection. Involved in maintenance of DNA methylation via its interaction with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1, preventing their degradation and promoting DNA methylation by DNMT1. Exhibits a preference towards 'Lys-48'-linked ubiquitin chains. Increases regulatory T-cells (Treg) suppressive capacity by deubiquitinating and stabilizing the transcription factor FOXP3 which is crucial for Treg cell function (PubMed:23973222).
Catalog Number:
(89141-386)
Supplier:
Enzo Life Sciences
Description:
Lysosome-associated membrane proteins (LAMP1 and LAMP2) are type I integral membrane protein that are transported from the trans-Golgi network to endosomes and then lysosomes. Following activation of platelets, T-cells, neutrophils, or endothelium, LAMP1 and LAMP2 are expressed on the cell surface. Cell surface LAMP1 and LAMP2 have been shown to promote adhesion of human peripheral blood mononuclear cells (PBMC) to vascular endothelium, and loss of LAMP2 expression is associated with impaired autophagy observed in Danons disease.
Catalog Number:
(10664-568)
Supplier:
Bioss
Description:
p53, a DNA-binding, oligomerization domain- and transcription activation domain-containing tumor suppressor, upregulates growth arrest and apoptosis-related genes in response to stress signals, thereby influencing programmed cell death, cell differentiation, and cell cycle control mechanisms. p53 localizes to the nucleus, yet can be chaperoned to the cytoplasm by the negative regulator, MDM2. MDM2 is an E3 ubiquitin ligase that is upregulated in the presence of active p53, where it poly-ubiquitinates p53 for proteasome targeting. p53 fluctuates between latent and active DNA-binding conformations and is differentially activated through posttranslational modifications, including phosphorylation and acetylation. Mutations in the DNA-binding domain (DBD) of p53, amino acids 110-286, can compromise energetically-favorable association with cis elements and are implicated in several human cancers.
Catalog Number:
(10664-566)
Supplier:
Bioss
Description:
p53, a DNA-binding, oligomerization domain- and transcription activation domain-containing tumor suppressor, upregulates growth arrest and apoptosis-related genes in response to stress signals, thereby influencing programmed cell death, cell differentiation, and cell cycle control mechanisms. p53 localizes to the nucleus, yet can be chaperoned to the cytoplasm by the negative regulator, MDM2. MDM2 is an E3 ubiquitin ligase that is upregulated in the presence of active p53, where it poly-ubiquitinates p53 for proteasome targeting. p53 fluctuates between latent and active DNA-binding conformations and is differentially activated through posttranslational modifications, including phosphorylation and acetylation. Mutations in the DNA-binding domain (DBD) of p53, amino acids 110-286, can compromise energetically-favorable association with cis elements and are implicated in several human cancers.
Catalog Number:
(10107-204)
Supplier:
Prosci
Description:
NR1D2 can interact with NCOA5 coactivator, leading to a strong increase of transcription of target genes. NR1D2 also binds to the sequences 5'-AATGTAGGTCA-3' and 5'-ATAACTAGGTCA-3' and acts as a potent competitive transcriptional silencer and negative regulator of RORalpha mediated trans-activation. NR1D2 may play different roles in metabolism, inflammation, and circadian cycling in the organ-specific manner in homeostasis.
Catalog Number:
(ABCA_AB308444-100U)
Supplier:
ABCAM INC.
Description:
Anti-Serotonin transporter Rabbit Monoclonal Antibody [clone: EPR26259-61]
Catalog Number:
(AAA17328-06)
Catalog Number:
(100504-908)
Supplier:
Electron Microscopy Sciences
Description:
Kit consists of: 450 mL Glycol methacrylate, GMA, 225 mL n-Butyl methacrylate, 50 mL Ethylene glycol dimethacrylate, 15g Benzoyl Peroxide Paste, and 20 mL Polyethylene Glycol 400.
Catalog Number:
(10270-140)
Supplier:
Bioss
Description:
P2Y purinoceptor 11 (P2Y11) is a 374 amino acid protein belonging to the G-protein coupled receptor one family. P2Y11 is a multi-pass cell membrane protein that acts as a receptor for both ATP and ATD coupled to G proteins. Due to these interactions, P2Y11 is involved in phosphatidylinositol-calcium and adenylyl cyclase pathways. Induced by DMSO and retinoic acid, P2Y11 is highly expressed in spleen tissue. A putative trans-splicing event involving the gene that encodes P2Y11 and an upstream gene encoding PPAN has been found to result in a fusion protein, designated PPAN-P2RY11.
Supplier:
MP Biomedicals
Description:
Coomassie Brilliant Blue G-250 is a protein stain in electrophoresis. Brilliant Blue G has been used in the Bradford dye-binding protein assay.
Catalog Number:
(10351-990)
Supplier:
Bioss
Description:
Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (By similarity). Interacts with MCMBP.
Catalog Number:
(10255-034)
Supplier:
Bioss
Description:
DD3 is a unique enzyme that can specifically catalyze the dehydrogenation of trans-benzenedihydrodiol and trans-naphthalenedihydrodiol.Human liver contains isoforms of dihydrodiol dehydrogenase (DD1, DD2, DD3 and DD4), which belong to the aldo-oxo reductase/aldo-keto reductase (AKR) superfamily, have 20Alpha- or 3Alpha-hydroxysteroid dehydrogenase (HSD) activity. DD1 is also designated AKR1C1, DDH or DDH1 while DD2 also can be designated AKR1C2, dDD, BABP or DDH2. AKR1C3 and 3Alpha-HSD are alternate designations for DD3, while DD4 also can be called AKR1C4, CD or CHDR. DD1 and DD2 are 20Alpha-HSDs, whereas DD3 and DD4 are the 3Alpha-HSDs. The multiple human cytosolic dihydrodiol dehydrogenases are involved in the metabolism of xenobiotics, such as polycyclic aromatic hydrocarbons, pesticides and steroid hormones, and are responsible for the reduction of ketone-containing drugs by using NADH or NADPH as a cofactor. The 20Alpha-HSD catalyzes the reaction of progesterone to the inactive form 20Alpha-hydroxyprogesterone. The 3Alpha-HSD is a cytosolic, monomeric, NADPH-dependent oxidoreductase that reduces 3-keto-5-dihydrosteroids to their tetrahydro products. DD1 and DD2 are ubiquitously expressed, whereas DD4 mRNA is restricted to the liver.
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