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trans-2-Nitrocinnamic+acid
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trans-2-Nitrocinnamic+acid
Catalog Number:
(10266-656)
Supplier:
Bioss
Description:
Maspardin is a 308 amino acid cytoplasmic protein that is widely expressed. Belonging to the AB hydrolase superfamily, Maspardin colocalizes with CD4 on endosomal/trans-Golgi network. It is thought that Maspardin may act as a negative regulatory factor in CD4-dependent T-cell activation. Defects in the gene encoding Maspardin are the result of hereditary spastic paraplegia autosomal recessive type 21 (also designated Mast syndrome), an autosomal recessive neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. The gene encoding Maspardin is encoded by human chromosome 15, which houses over 700 genes and comprises nearly 3% of the human genome.
Catalog Number:
(10468-534)
Supplier:
Bioss
Description:
Members of the suppressor of cytokine signaling (SOCS) family of proteins contain C-terminal regions of homology called the SOCS box, which serves to couple SOCS proteins and their binding partners with the elongin B and C complex. Serveral other families of proteins also contain SOCS boxes but differ from the SOCS proteins in the type of domain they contained upstream of the SOCS box. Four members of the ankyrin repeat and SOCS box-containing (ASB) protein family are identified and termed as ASB-1, ASB-2, ASB-3 and ASB-4. ASB-1 is expressed in multiple organs, including the hematopoietic compartment. ASB-1 knock-out mice display a diminution of spermatogenesis with less complete filling of seminiferous tubules. Asb-2 is a novel retinoic-acid (RA)-induced gene in acute promyelocytic leukemia (APL) cells and its expression induces growth-inhibition and chromatin condensation recapitulating early events critical to RA-induced differentiaiton of APL cells. ASB-2 is directly induced by all-trans retinotic acid, by the binding of RARa to the RAR binding element/RXR binding element in the Asb-2 promoter.
Catalog Number:
(101189-698)
Supplier:
BioVendor
Description:
Cyclophilins belong to a group of proteins that have peptidyl-prolyl cis-trans isomerase activity; such proteins are collectively known as immunophilins and also include the FK-506-binding proteins and the parvulins. Cyclophilins are found in all cells of all organisms studied, in both prokaryotes and eukaryotes. Human have a total of 16 cyclophilin proteins. Cyclophilins also have varying degrees of affinity for the immunosuppressive drug Cyclosporine A (CsA), a cyclic 11-amino-acid peptide produced by fungus Tolypocladium infantum. Cyclophilin A, in particular, is the major intracellular receptor for CsA. Cyclophilin A (CYPA) is the first member of the cyclophilins to be identified in mammals. Human genes of CYPA, also known as Cyp18, are located on chromosome 7p11.2-p13 and encode the protein, which consists of 165 amino acid residues with a relative molecular mass approximately 18 kDa. Human CYPA has an eight-stranded antiparallel β-barrel structure, with two α-helices enclosing the barrel from either side. Seven aromatic and other hydrophobic residues form a compact hydrophobic core within the barrel, usually in the area where CsA binds. A loop from Lys118 ti His126 and four β-strands (β3-β6) make up the binding site for CsA. In mammals, the CsA-CYPA complex binds to and inhibits calcineurin, a calcium-calmodulin-activated serine/threonine-specific protein phosphatase. The inhibition of calcineurin blocks the translocation of nuclear factor of activated T cells from the cytosol to the nucleus, thus preventing the transcription of genes encoding cytokines such as interleukin-2.
Catalog Number:
(10468-544)
Supplier:
Bioss
Description:
Members of the suppressor of cytokine signaling (SOCS) family of proteins contain C-terminal regions of homology called the SOCS box, which serves to couple SOCS proteins and their binding partners with the elongin B and C complex. Serveral other families of proteins also contain SOCS boxes but differ from the SOCS proteins in the type of domain they contained upstream of the SOCS box. Four members of the ankyrin repeat and SOCS box-containing (ASB) protein family are identified and termed as ASB-1, ASB-2, ASB-3 and ASB-4. ASB-1 is expressed in multiple organs, including the hematopoietic compartment. ASB-1 knock-out mice display a diminution of spermatogenesis with less complete filling of seminiferous tubules. Asb-2 is a novel retinoic-acid (RA)-induced gene in acute promyelocytic leukemia (APL) cells and its expression induces growth-inhibition and chromatin condensation recapitulating early events critical to RA-induced differentiaiton of APL cells. ASB-2 is directly induced by all-trans retinotic acid, by the binding of RARa to the RAR binding element/RXR binding element in the Asb-2 promoter.
Catalog Number:
(75933-596)
Supplier:
Rockland Immunochemical
Description:
The sorting of acid hydrolases to lysosomes rely on mannose 6-phosphate receptors that cycle between the trans-Golgi network (TGN) and endosomes. The maintenance of this cycle requires the function of the mammalian Golgi-associated retrograde protein (GARP) complex which is composed of three subunits: VPS52, VPS53, and VPS54. Depletion of any of these three proteins, such as by RNAi, impairs the retrograde transport of multiple TGN proteins. VPS53 was identified as an HIV dependency factor (HDF) and plays a role in viral entry to the cell, suggesting that VPS53 may be an important drug target in HIV treatment. At least five isoforms of VPS53 are known to exist.
Catalog Number:
(10271-390)
Supplier:
Bioss
Description:
DDAH, a dimethylarginine dimethylaminohydrolase, hydrolyzes dimethyl arginine (ADMA) and monomethyl arginine (MMA), both inhibitors of nitric oxide synthases, and may be involved in in-vivo modulation of nitric oxide production (1,2). Impairment of DDAH causes ADMA accumulation and a reduction in cGMP generation (3). DDAH II, the predominant DDAH isoform in endothelial cells, facilitates the induction of nitric oxide synthesis by all-trans-Retinoic acid (atRA) (4). DDAH proteins are highly expressed in colon, kidney, stomach and liver tissues (1).
Catalog Number:
(10271-402)
Supplier:
Bioss
Description:
DDAH, a dimethylarginine dimethylaminohydrolase, hydrolyzes dimethyl arginine (ADMA) and monomethyl arginine (MMA), both inhibitors of nitric oxide synthases, and may be involved in in-vivo modulation of nitric oxide production (1,2). Impairment of DDAH causes ADMA accumulation and a reduction in cGMP generation (3). DDAH II, the predominant DDAH isoform in endothelial cells, facilitates the induction of nitric oxide synthesis by all-trans-Retinoic acid (atRA) (4). DDAH proteins are highly expressed in colon, kidney, stomach and liver tissues (1).
Catalog Number:
(76012-302)
Supplier:
Prosci
Description:
The protein encoded by this gene belongs to the FKBP-type peptidyl-prolyl cis/trans isomerase (PPIase) family. Members of this family exhibit PPIase activity and function as molecular chaperones. A similar protein in mouse is located in the endoplasmic reticulum and binds calcium.
Catalog Number:
(75935-502)
Supplier:
Rockland Immunochemical
Description:
The zinc transporter ZIP9, also known as SLC39A9, is a member of a family of divalent ion transporters. Zinc is an essential ion for cells and plays significant roles in the growth, development, and differentiation. The zinc transporter family is divided into four subfamilies (I, II, LIV-1 and gufA). ZIP9 is a multipass membrane protein that belongs to the ZIP transporter subfamily I. It is located at the trans-Golgi network regardless of zinc presence and is thought to be a zinc homeostasis regulator acting in the secretory pathway without significantly altering cytosolic zinc homeostasis.
Catalog Number:
(10261-648)
Supplier:
Bioss
Description:
Maspardin is a 308 amino acid cytoplasmic protein that is widely expressed. Belonging to the AB hydrolase superfamily, Maspardin colocalizes with CD4 on endosomal/trans-Golgi network. It is thought that Maspardin may act as a negative regulatory factor in CD4-dependent T-cell activation. Defects in the gene encoding Maspardin are the result of hereditary spastic paraplegia autosomal recessive type 21 (also designated Mast syndrome), an autosomal recessive neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. The gene encoding Maspardin is encoded by human chromosome 15, which houses over 700 genes and comprises nearly 3% of the human genome.
Catalog Number:
(10271-406)
Supplier:
Bioss
Description:
DDAH, a dimethylarginine dimethylaminohydrolase, hydrolyzes dimethyl arginine (ADMA) and monomethyl arginine (MMA), both inhibitors of nitric oxide synthases, and may be involved in in-vivo modulation of nitric oxide production (1,2). Impairment of DDAH causes ADMA accumulation and a reduction in cGMP generation (3). DDAH II, the predominant DDAH isoform in endothelial cells, facilitates the induction of nitric oxide synthesis by all-trans-Retinoic acid (atRA) (4). DDAH proteins are highly expressed in colon, kidney, stomach and liver tissues (1).
Catalog Number:
(10271-410)
Supplier:
Bioss
Description:
DDAH, a dimethylarginine dimethylaminohydrolase, hydrolyzes dimethyl arginine (ADMA) and monomethyl arginine (MMA), both inhibitors of nitric oxide synthases, and may be involved in in-vivo modulation of nitric oxide production (1,2). Impairment of DDAH causes ADMA accumulation and a reduction in cGMP generation (3). DDAH II, the predominant DDAH isoform in endothelial cells, facilitates the induction of nitric oxide synthesis by all-trans-Retinoic acid (atRA) (4). DDAH proteins are highly expressed in colon, kidney, stomach and liver tissues (1).
Catalog Number:
(89359-724)
Supplier:
Genetex
Description:
Lysosomes are membrane-bound vacuoles which play a critical role in cellular metabolism. These organelles participate in endocytosis, the synthesis and assembly of acid hydrolases, act as sites for digestion of foreign materials and for specialized autolytic cellular processes. Membrane-associated glycoproteins have an important role in normal lysosomal function. Prior to posttranslational modification, Lysosome Associated Membrane Protein 2 (LAMP 2) is an ~45 kDa polypeptide. Mature, functional LAMP 2 is extensively glycosylated with a variety of different N-linked and O-linked oligosaccharides with a total molecular weight of ~100-110 kDa. LAMP 2 has a structure comprised of a large amino-terminal intra-lysosomal domain, a hydrophobic trans-membrane domain, and a short carboxyl-terminal cytoplasmic tail.
Catalog Number:
(10251-974)
Supplier:
Bioss
Description:
Adaptins are heterotetrameric subunits of adaptors, which are complexes involved in the formation of Clathrin-coated pits for vesicle-mediated endocytosis. Clathrin and its associated heterotetrameric protein complexes make up the main protein components of the coat surrounding the cytoplasmic face of coated vesicles. The Adaptin family, comprising a, b, and g classes, is also responsible for the transport of ligand-receptor complexes from plasma membranes and the trans-Golgi network to lysosomes. Two main types of adaptor proteins (APs), AP-1 and AP-2, are found in Clathrin-coated structures located at the Golgi complex and the plasma membrane of mammalian cells, respectively. Adaptor protein complex 2 (AP-2) is composed of two large Adaptins (a1A/AP2A1 and b1/AP2B1), a medium Adaptin (m2/AP-2m1) and a small Adaptin (s2 long/AP2S1). AP-2m1, a 435 amino acid protein, links Clathrin to receptors in coated vesicles.
Catalog Number:
(10252-194)
Supplier:
Bioss
Description:
Adaptins are heterotetrameric subunits of adaptors, which are complexes involved in the formation of Clathrin-coated pits for vesicle-mediated endocytosis. Clathrin and its associated heterotetrameric protein complexes make up the main protein components of the coat surrounding the cytoplasmic face of coated vesicles. The Adaptin family, comprising a, b, and g classes, is also responsible for the transport of ligand-receptor complexes from plasma membranes and the trans-Golgi network to lysosomes. Two main types of adaptor proteins (APs), AP-1 and AP-2, are found in Clathrin-coated structures located at the Golgi complex and the plasma membrane of mammalian cells, respectively. Adaptor protein complex 2 (AP-2) is composed of two large Adaptins (a1A/AP2A1 and b1/AP2B1), a medium Adaptin (m2/AP-2m1) and a small Adaptin (s2 long/AP2S1). AP-2m1, a 435 amino acid protein, links Clathrin to receptors in coated vesicles.
Catalog Number:
(76009-020)
Supplier:
Prosci
Description:
The protein encoded by this gene is a peripheral membrane protein localized to the trans-Golgi network. It is sensitive to brefeldin A. This encoded protein contains a GRIP domain which is thought to be used in targeting. Alternative splicing results in multiple transcript variants.
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