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Omschrijving: 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. RNF130 (ring finger protein 130), also known as GP, G1RZFP (G1-related zinc finger protein) or GOLIATH, is a 419 amino acid single-pass type I membrane protein that shares similarity with a Drosophila zinc-finger protein found in mesoderm known as g1. RNF130 contains one PA (protease associated) domain and a single RING-type zinc finger. Implicated in the regulation of growth factor withdrawal-induced apoptosis of myeloid precursor cells, RNF130 is encoded by a gene located on human chromosome 5q35.3 and mouse chromosome 11 B1.3.
Catalogus nummer: BOSSBS-9252R-CY5.5
UOM: 1 * 100 µl
Leverancier: Bioss


Omschrijving: 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. RNF130 (ring finger protein 130), also known as GP, G1RZFP (G1-related zinc finger protein) or GOLIATH, is a 419 amino acid single-pass type I membrane protein that shares similarity with a Drosophila zinc-finger protein found in mesoderm known as g1. RNF130 contains one PA (protease associated) domain and a single RING-type zinc finger. Implicated in the regulation of growth factor withdrawal-induced apoptosis of myeloid precursor cells, RNF130 is encoded by a gene located on human chromosome 5q35.3 and mouse chromosome 11 B1.3.
Catalogus nummer: BOSSBS-9252R
UOM: 1 * 100 µl
Leverancier: Bioss


Omschrijving: 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. ANKZF1 (ankyrin repeat and zinc finger domain containing 1), also known as ZNF744, is 726 amino acids in length and lacks a KRAB domain but contains one C2H2-type zinc finger and two ANK repeats. The gene encoding ANKZF1 localizes to chromosome 2.
Catalogus nummer: BOSSBS-12476R-A647
UOM: 1 * 100 µl
Leverancier: Bioss


Omschrijving: 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. Zinc finger and BTB domain-containing protein 5 (ZBTB5) is a 677 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZBTB5 contains a BTB domain, also known as a POZ domain, which inhibits DNA binding and mediates homotypic and heterotypic dimerization. Characteristics of the BTB domain suggest that ZBTB5 functions as a transcription regulator.
Catalogus nummer: BOSSBS-13581R-A647
UOM: 1 * 100 µl
Leverancier: Bioss


Omschrijving: 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. Zinc finger and BTB domain-containing protein 5 (ZBTB5) is a 677 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZBTB5 contains a BTB domain, also known as a POZ domain, which inhibits DNA binding and mediates homotypic and heterotypic dimerization. Characteristics of the BTB domain suggest that ZBTB5 functions as a transcription regulator.
Catalogus nummer: BOSSBS-13581R-A350
UOM: 1 * 100 µl
Leverancier: Bioss


Omschrijving: 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.
Catalogus nummer: BOSSBS-12241R-CY5
UOM: 1 * 100 µl
Leverancier: Bioss


Omschrijving: 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, ZNF449 is a 518 amino acid protein that contains one SCAN box domain and seven C2H2-type zinc fingers. ZNF449 is ubiquitously expressed and localizes to the nucleus. There are three isoforms of ZNF449 that are produced as a result of alternative splicing events.
Catalogus nummer: BOSSBS-12236R-A350
UOM: 1 * 100 µl
Leverancier: Bioss


Omschrijving: 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, ZNF449 is a 518 amino acid protein that contains one SCAN box domain and seven C2H2-type zinc fingers. ZNF449 is ubiquitously expressed and localizes to the nucleus. There are three isoforms of ZNF449 that are produced as a result of alternative splicing events.
Catalogus nummer: BOSSBS-12236R-CY3
UOM: 1 * 100 µl
Leverancier: Bioss


Omschrijving: 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, ZNF449 is a 518 amino acid protein that contains one SCAN box domain and seven C2H2-type zinc fingers. ZNF449 is ubiquitously expressed and localizes to the nucleus. There are three isoforms of ZNF449 that are produced as a result of alternative splicing events.
Catalogus nummer: BOSSBS-12236R-A647
UOM: 1 * 100 µl
Leverancier: Bioss


Omschrijving: This fine dosing tap is made of zinc injection moulding.
Catalogus nummer: MSGA2796
UOM: 1 * 1 ST
Leverancier: asecos


Omschrijving: 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. TRIM7 (tripartite motif-containing 7), also known as RNF90 or GNIP, is a 511 amino acid protein that belongs to the TRIM family and contains one RING-type zinc finger, one B box-type zinc finger and one SPRY domain. Expressed in placenta and skeletal muscle and present at lower levels in brain, heart and pancreas, TRIM7 localizes to both the cytoplasm and the nucleus where it exists as dimers and is thought to participate in the initiation of glycogen synthesis. Multiple isoforms of TRIM7 exist due to alternative splicing events.
Catalogus nummer: BOSSBS-9164R-CY5
UOM: 1 * 100 µl
Leverancier: Bioss


Omschrijving: 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. TRIM7 (tripartite motif-containing 7), also known as RNF90 or GNIP, is a 511 amino acid protein that belongs to the TRIM family and contains one RING-type zinc finger, one B box-type zinc finger and one SPRY domain. Expressed in placenta and skeletal muscle and present at lower levels in brain, heart and pancreas, TRIM7 localizes to both the cytoplasm and the nucleus where it exists as dimers and is thought to participate in the initiation of glycogen synthesis. Multiple isoforms of TRIM7 exist due to alternative splicing events.
Catalogus nummer: BOSSBS-9164R-FITC
UOM: 1 * 100 µl
Leverancier: Bioss


Omschrijving: 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. TRIM7 (tripartite motif-containing 7), also known as RNF90 or GNIP, is a 511 amino acid protein that belongs to the TRIM family and contains one RING-type zinc finger, one B box-type zinc finger and one SPRY domain. Expressed in placenta and skeletal muscle and present at lower levels in brain, heart and pancreas, TRIM7 localizes to both the cytoplasm and the nucleus where it exists as dimers and is thought to participate in the initiation of glycogen synthesis. Multiple isoforms of TRIM7 exist due to alternative splicing events.
Catalogus nummer: BOSSBS-9164R-A350
UOM: 1 * 100 µl
Leverancier: Bioss


Omschrijving: 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. TRIM7 (tripartite motif-containing 7), also known as RNF90 or GNIP, is a 511 amino acid protein that belongs to the TRIM family and contains one RING-type zinc finger, one B box-type zinc finger and one SPRY domain. Expressed in placenta and skeletal muscle and present at lower levels in brain, heart and pancreas, TRIM7 localizes to both the cytoplasm and the nucleus where it exists as dimers and is thought to participate in the initiation of glycogen synthesis. Multiple isoforms of TRIM7 exist due to alternative splicing events.
Catalogus nummer: BOSSBS-9164R-A488
UOM: 1 * 100 µl
Leverancier: Bioss


Omschrijving: 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. Zinc finger and BTB domain-containing protein 5 (ZBTB5) is a 677 amino acid member of the Kr_ppel C2H2-type zinc-finger protein family. localised to the nucleus, ZBTB5 contains a BTB domain, also known as a POZ domain, which inhibits DNA binding and mediates homotypic and heterotypic dimerization. Characteristics of the BTB domain suggest that ZBTB5 functions as a transcription regulator.
Catalogus nummer: BOSSBS-13581R-A750
UOM: 1 * 100 µl
Leverancier: Bioss


Omschrijving: RNF113A is a novel gene whose function cannot directly be inferred from it's sequence analysis. Ring finger proteins have a role in signalling the destruction of a range of heterologous protein substrates. They are small zinc binding domains present within arrays of larger, functionally distinct proteins, often close to the amino or carboxyl termini. RNF113A is a ubiquitously expressed protein that contains a RING type zinc finger and a C3H1 type zinc finger.
Catalogus nummer: BOSSBS-9248R-A680
UOM: 1 * 100 µl
Leverancier: Bioss


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