You Searched For: Zinc

Catalog Number: (BOSSBS-15486R-FITC)

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 Kr_ppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. HIC-2 (hypermethylated in cancer 2) possesses Zinc finger motifs that are thought to be important for DNA-binding and also has a BTB/POZ domain at the N-terminus, which is thought to be important for protein-protein binding, as well as for the binding of transcription factors. HIC-2 is also known as Hic-3, HIC1-related gene on chromosome 22 or Zinc finger and BTB domain-containing protein 30, and is a 615 amino acid protein that is expressed as two isoforms produced by alternative splicing. HIC-2 is highly expressed in cerebellum and is localised to the nucleus in cells. HIC-2 contains a short amino acid sequence that is thought to interact with CtBP, a transcriptional repressor. The gene sequence associated with HIC-2 is thought to be a target for miRNAs (microRNAs) which are expressed in many cancers, suggesting that HIC-2 could possess tumor suppressor capabilities.

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Catalog Number: (BOSSBS-9245R-A680)

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. MARCH10 (membrane-associated ring finger (C3HC4) 10), also known as RNF190 (ring finger protein 190) or MARCH-X, is an 808 amino acid protein with one RING-CH-type zinc finger domain. MARCH10 may function as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and immediately transfers that residue to a protein that is targeted for degradation.

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Catalog Number: (BOSSBS-9258R-CY5)

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.

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Catalog Number: (BOSSBS-9264R-CY3)

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. RNF215 (ring finger protein 215), is a 377 amino acid multi-pass membrane protein containing one RING-type zinc finger. The gene encoding RNF215 maps to human chromosome 22, which houses over 500 genes and is the second smallest human chromosome. Mutations in several of the genes that map to chromosome 22 are involved in the development of Phelan-McDermid syndrome, Neurofibromatosis type 2, autism and schizophrenia.

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Catalog Number: (BOSSBS-12330R-A647)

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. Staf-50 (50 kDa-stimulated trans-acting factor), also known as TRIM22 (tripartite motif-containing 22), RNF94 or GPSTAF50, is a 498 amino acid cytoplasmic protein that belongs to the TRIM family and, characteristic of TRIM family members, contains one RING-type zinc finger, one B box-type zinc finger and one SPRY domain. Induced by IFN-å and IFN-∫, Staf-50 is strongly expressed in ovary, spleen, thymus and peripheral blood leukocytes where it is thought to mediate the antiviral effects of IFN proteins. Additionally, Staf-50 is present in leukemic cells, suggesting a role in cancer formation and metastasis. Staf-50 exists as two alternatively spliced isoforms which are encoded by a gene that maps to human chromosome 11.

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Catalog Number: (BOSSBS-9258R-A750)

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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-9258R-A680)

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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-9258R-CY7)

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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-9152R-A488)

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.

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Catalog Number: (BOSSBS-9152R-CY5.5)

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.

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Catalog Number: (BOSSBS-9238R-CY5)

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.

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Catalog Number: (BOSSBS-9265R-CY7)

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. RNF32 (RING finger protein 32), also known as HSD15 or FKSG33, is a 362 amino acid cytoplasmic protein that contains one IQ domain and two RING-type zinc fingers. Highly expressed in testis with lower expression levels in ovary tissue, RNF32 is thought to play a role in spermatogenesis, specifically contributing to the growth and maturation of round spermatids. Six isoforms of RNF32 exist due to alternative splicing events.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-9245R-FITC)

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. MARCH10 (membrane-associated ring finger (C3HC4) 10), also known as RNF190 (ring finger protein 190) or MARCH-X, is an 808 amino acid protein with one RING-CH-type zinc finger domain. MARCH10 may function as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and immediately transfers that residue to a protein that is targeted for degradation.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13562R-CY5)

Supplier: Bioss

Description: ZADH2 belongs to the zinc containing alcohol dehydrogenase family.

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Catalog Number: (BOSSBS-6440R-CY5.5)

Supplier: Bioss

Description: May be involved in zinc transport out of the cell.

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Catalog Number: (BOSSBS-12215R-HRP)

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.

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