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Zinc+dimethyldithiocarbamate


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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 Krüppel-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, ZNF704 is a 412 amino acid nuclear protein that contains one C2H2-type zinc finger. The gene encoding ZNF704 maps to human chromosome 8, which is made up of nearly 146 million bases and encodes about 800 genes. Chromosome 8 is also associated with Pfeiffer syndrome, congenital hypothyroidism and Waardenburg syndrome.
Catalog Number: (103288-668)

Supplier:  Novus Biologicals
Description:   The ZNF850 Antibody from Novus Biologicals is a rabbit polyclonal antibody to ZNF850. This antibody reacts with human. The ZNF850 Antibody has been validated for the following applications: Immunohistochemistry, Immunocytochemistry / Immunofluorescence, Immunohistochemistry-Paraffin.
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. ZDHHC1 (zinc finger, DHHC-type containing 1), also known as ZNF377 (zinc finger protein 377) or C16orf1, is a 485 amino acid multi-pass membrane protein that contains one DHHC-type zinc finger. Expressed in fetal heart, lung and kidney and also present in adult lung and pancreas, ZDHHC1 functions as a palmitoyltransferase that catalyzes the conversion of palmitoyl-CoA and protein-cysteine to S-palmitoyl protein and CoA. Like ZDHHC1, ZDHHC5, ZDHHC6, ZDHHC7 and ZDHHC18 each contain one DHHC-type zinc finger through which they convey palmitoyltransferase activity against a broad range of substrates, including H-Ras, SNAP 25 and GABAA R proteins.
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. As a member of the Krüppel C2H2-type zinc-finger protein family, ZNF323 (zinc finger protein 323) is a 406 amino acid protein containing six C2H2-type zinc fingers and one SCAN box domain. Specifically, C2H2-type zinc fingers function to bind DNA, while SCAN box domains are thought to participate in protein-protein interactions. Therefore, it is probable that ZNF323 functions as a transcription factor. With highest expression in kidney, liver and lung and weaker expression in brain, heart, intestine, muscle, cholecyst and pancreas, ZNF323 is localized to the nucleus. It is also suggested that ZNF323 may play a role in the development of multiple embryonic organs.

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 protein-protein interactions and protein-DNA interactions. Specifically, they are thought to be involved in the ubiquitination pathway of protein degradation. RNF165 (RING finger protein 165) is a 346 amino acid protein that contains one RING-type zinc finger. Via its RING-type zinc finger, RNF165 may play a role in transcriptional regulation and protein degradation events. The gene encoding RNF165 maps to human chromosome 18, which houses over 300 genes, including Trisomy 18, or Edwards syndrome, the second most common trisomy after Downs syndrome. Translocation between chromosome 18 and 14 is the most common translocation in cancers, and occurs in follicular lymphomas. Niemann-Pick disease, hereditary hemorrhagic telangiectasia and erythropoietic protoporphyria are also associated with chromosome 18.
Supplier:  Bioss
Description:   The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM50 (tripartite motif containing 50), also known as TRIM50A or E3 ubiquitin-protein ligase TRIM50, is a 487 amino acid cytoplasmic protein that functions as an E3 ubiquitin-protein ligase. Containing one RING-type zinc finger, a B30.2/SPRY domain and a single B box-type zinc finger, TRIM50 belongs to the TRIM/RBCC family and undergoes post-translational auto-ubiquitination. TRIM50 exists as two alternatively spliced isoforms, designated TRIM50 alpha and TRIM50 beta, and has the ability to form dimers and trimers. The gene encoding TRIM50 maps to human chromosome 7, which houses over 1,000 genes, comprises nearly 5% of the human genome and has been linked to Osteogenesis imperfecta, Pendred syndrome, Lissencephaly, Citrullinemia and Shwachman-Diamond syndrome.

Supplier:  Bioss
Description:   The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM50 (tripartite motif containing 50), also known as TRIM50A or E3 ubiquitin-protein ligase TRIM50, is a 487 amino acid cytoplasmic protein that functions as an E3 ubiquitin-protein ligase. Containing one RING-type zinc finger, a B30.2/SPRY domain and a single B box-type zinc finger, TRIM50 belongs to the TRIM/RBCC family and undergoes post-translational auto-ubiquitination. TRIM50 exists as two alternatively spliced isoforms, designated TRIM50 alpha and TRIM50 beta, and has the ability to form dimers and trimers. The gene encoding TRIM50 maps to human chromosome 7, which houses over 1,000 genes, comprises nearly 5% of the human genome and has been linked to Osteogenesis imperfecta, Pendred syndrome, Lissencephaly, Citrullinemia and Shwachman-Diamond syndrome.
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 protein-protein interactions and protein-DNA interactions. Specifically, they are thought to be involved in the ubiquitination pathway of protein degradation. RNF165 (RING finger protein 165) is a 346 amino acid protein that contains one RING-type zinc finger. Via its RING-type zinc finger, RNF165 may play a role in transcriptional regulation and protein degradation events. The gene encoding RNF165 maps to human chromosome 18, which houses over 300 genes, including Trisomy 18, or Edwards syndrome, the second most common trisomy after Downs syndrome. Translocation between chromosome 18 and 14 is the most common translocation in cancers, and occurs in follicular lymphomas. Niemann-Pick disease, hereditary hemorrhagic telangiectasia and erythropoietic protoporphyria are also associated with chromosome 18.

Supplier:  Bioss
Description:   SMAD regulates gene expression by interacting with different classes of transcription factors including DNA-binding multi-zinc finger proteins. SIP1, for SMAD interacting protein 1, is a member of the delta-EF1/Zfh1 family of 2-handed zinc finger/homeodomain proteins. SIP1 contains a SMAD-binding domain, a homeodomain and two clusters of zinc fingers on the N- and C-termini. SIP1, also known as SMADIP1, ZFHX1B and ZEB2 (zinc finger E-box-binding protein 2), can be induced by TGF∫ treatment. SIP1 plays a crucial role in normal embryonic development of neural structures and the neural crest. The human SIP1 gene maps to chromosome 2q22. Mutations in the SIP1 gene cause a form of Hirschsprung disease (HSCR). Patients with SIP1 mutations show mental retardation, delayed motor development, epilepsy, microcephaly, distinct facial features and/or congenital heart disease—all symptoms of HSCR.

Supplier:  Bioss
Description:   SMAD regulates gene expression by interacting with different classes of transcription factors including DNA-binding multi-zinc finger proteins. SIP1, for SMAD interacting protein 1, is a member of the delta-EF1/Zfh1 family of 2-handed zinc finger/homeodomain proteins. SIP1 contains a SMAD-binding domain, a homeodomain and two clusters of zinc fingers on the N- and C-termini. SIP1, also known as SMADIP1, ZFHX1B and ZEB2 (zinc finger E-box-binding protein 2), can be induced by TGF∫ treatment. SIP1 plays a crucial role in normal embryonic development of neural structures and the neural crest. The human SIP1 gene maps to chromosome 2q22. Mutations in the SIP1 gene cause a form of Hirschsprung disease (HSCR). Patients with SIP1 mutations show mental retardation, delayed motor development, epilepsy, microcephaly, distinct facial features and/or congenital heart disease—all symptoms of HSCR.

Supplier:  Bioss
Description:   SMAD regulates gene expression by interacting with different classes of transcription factors including DNA-binding multi-zinc finger proteins. SIP1, for SMAD interacting protein 1, is a member of the delta-EF1/Zfh1 family of 2-handed zinc finger/homeodomain proteins. SIP1 contains a SMAD-binding domain, a homeodomain and two clusters of zinc fingers on the N- and C-termini. SIP1, also known as SMADIP1, ZFHX1B and ZEB2 (zinc finger E-box-binding protein 2), can be induced by TGF∫ treatment. SIP1 plays a crucial role in normal embryonic development of neural structures and the neural crest. The human SIP1 gene maps to chromosome 2q22. Mutations in the SIP1 gene cause a form of Hirschsprung disease (HSCR). Patients with SIP1 mutations show mental retardation, delayed motor development, epilepsy, microcephaly, distinct facial features and/or congenital heart disease—all symptoms of HSCR.
Catalog Number: (89316-390)

Supplier:  Genetex
Description:   Rabbit Polyclonal antibody to DPF2 (D4, zinc and double PHD fingers family 2)
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 Krüppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. ZNF266 is a 549 amino acid nuclear protein belonging to the Krüppel C2H2-type zinc finger protein family. ZNF266 has one KRAB domain and fourteen C2H2 zinc fingers. Due to the presence of these domains, ZNF266 is thought to be involved in transcriptional regulation. Repression of ZNF266 results in the blocking of erythroid differentiation and partial blocking of megakaryocytic differentiation, possibly indicating a role in the differentiation of erythroids and megakaryocytes.
Catalog Number: (10276-244)

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. A member of the Krüppel C2H2-type zinc-finger protein family, ZNF274, also known as Zinc finger protein with KRAB and SCAN domains 19, is a 653 amino acid protein containing five C2H2-type zinc fingers, two KRAB A domains and one SCAN box domain. Predominantly localized to the nucleolus, ZNF274 exhibits transcriptional repressing activity. There are four isoforms of ZNF274 that are produced as a result of alternative splicing events. Although total ZNF274 expression seems to be ubiquitous, the two main isoforms, ZNF274a and ZNF274b, differ slightly in tissue distribution with higher expression of ZNF274a in testis and higher expression of ZNF274b in spleen, ovary, skeletal muscle and thymus.

Supplier:  Bioss
Description:   Midline-2 is a 715 amino acid protein encoded by the human gene MID2. Midline-2 belongs to the TRIM/RBCC family and contains two B box-type zinc fingers, one B30.2/SPRY domain, one COS domain, one fibronectin type-III domain and one RING-type zinc finger. Midline-2 is a cytoplasmic protein found as a homodimer or heterodimer with Midline-1. It also interacts with IGBP1 (Lymphocyte signaling protein A4). Dimerization is mediated by the tripartite motif (RBCC; RING- and B box-type zinc fingers and coiled coil domains) and microtubule association is dependent on the C-terminal B30.2 domain. Midline-2 is expressed at low levels in fetal kidney and lung, and in adult prostate, ovary and small intestine.
Catalog Number: (10111-698)

Supplier:  Prosci
Description:   ZNF77 belongs to the krueppel C2H2-type zinc-finger protein family. It contains 12 C2H2-type zinc fingers and 1 KRAB domain. ZNF77 may be involved in transcriptional regulation.
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