You Searched For: 3-Bromo-2,5,6-trifluorobenzamide

Catalog Number: (BOSSBS-13581R-A488)

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. 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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13582R-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. 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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9164R-A555)

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. 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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9164R-A680)

Supplier: Bioss

Description: The tripartite motif (TRIM) family of proteins are characterised 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 localises 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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12241R-A750)

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. 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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11753R-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. RNF135 (RING finger protein 135), also known as L13, is a 432 amino acid protein that contains one RING-type zinc finger and one SPRY domain. Via its RING-type zinc finger, RNF135 may play a role in transcriptional regulation and protein degradation events. Defects in the gene encoding RNF135 are the cause of RNF135-related overgrowth syndrome which is characterized by learning disabilities, facial dysmorphism and increased weight and height. Multiple isoforms of RNF135 exist due to alternative splicing events.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11669R-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. RNF146 (RING finger protein 146), also known as Dactylidin, is a 359 amino acid protein that contains one RING-type zinc finger and one WWE domain. Via its RING-type zinc finger, RNF146 may play a role in transcriptional regulation and protein degradation events. Defects in the gene encoding RNF146 are associated with Alzheimer's disease (AD) and may lead to a higher risk of breast cancer. Two isoforms of RNF146 exist due to alternative splicing events.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12219R-CY5)

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. ZNF426 (Zinc finger protein 426), also known as MGC2663, is a 554 amino acid protein that is thought to be involved in transcriptional regulation. Localized to the nucleus, ZNF426 contains one KRAB domain and 12 C2H2-type zinc fingers through which it may convey DNA, RNA and protein binding capabilities. Specifically, ZNF426 may interact with the viral protein KSHV ORF 50 and, through this interaction, may activate viral gene transcription.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12215R-A680)

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. ZNF266 is a 549 amino acid nuclear protein belonging to the Kr_ppel 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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12476R-A647)

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. 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.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11669R-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. RNF146 (RING finger protein 146), also known as Dactylidin, is a 359 amino acid protein that contains one RING-type zinc finger and one WWE domain. Via its RING-type zinc finger, RNF146 may play a role in transcriptional regulation and protein degradation events. Defects in the gene encoding RNF146 are associated with Alzheimer's disease (AD) and may lead to a higher risk of breast cancer. Two isoforms of RNF146 exist due to alternative splicing events.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9379R-CY5.5)

Supplier: Bioss

Description: The Makorins are a family of putative ribonucleoproteins containing two to four C3H zinc fingers that may confer RNA-binding. In addition, they contain a C3HC4 RING zinc finger that allows them to function as E3 ubiquitin ligases. Makorin-2, also known as RNF62, HSPC070 or MKRN2, is a widely expressed, evolutionarily conserved protein with four C3H-type zinc fingers (three at the N-terminus and one at the C-terminus), one RING-type zinc finger and a cysteine and histidine motif similar to that found in Makorin-1. In Xenopus, Makorin-2 functions, via PI 3-kinase/Akt signaling, as a negative regulator of neurogenesis. In humans, Makorin-2 is overexpressed in various cancer cell lines, suggesting a possible role of Makorin-2 in tumor progression. In addition, Makorin-2 is co-expressed with Raf-1 in the same tissues and cell lines.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11753R-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. RNF135 (RING finger protein 135), also known as L13, is a 432 amino acid protein that contains one RING-type zinc finger and one SPRY domain. Via its RING-type zinc finger, RNF135 may play a role in transcriptional regulation and protein degradation events. Defects in the gene encoding RNF135 are the cause of RNF135-related overgrowth syndrome which is characterized by learning disabilities, facial dysmorphism and increased weight and height. Multiple isoforms of RNF135 exist due to alternative splicing events.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13373R)

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 krueppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. GLI-4, also known as HKR4, is a 376 amino acid protein that localizes to the nucleus and contains seven C2H2-type zinc fingers. Belonging to the krueppel C2H2-type zinc-finger protein family, GLI-4 may function as a transcriptional regulator, effectively activating or repressing the transcription of target genes. The gene encoding GLI-4 maps to human chromosome 8, which consists of nearly 146 million base pairs, houses more than 800 genes and is associated with a variety of diseases and malignancies.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13578R-CY7)

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. Zinc finger and BTB domain-containing protein 43 (ZBTB43), also known as ZNF297B or ZBTB22B, is a 467 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZBTB43 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 and the interaction of ZBTB43 with BDP1 suggest that ZBTB43 functions as a transcription regulator.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11753R-A350)

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. RNF135 (RING finger protein 135), also known as L13, is a 432 amino acid protein that contains one RING-type zinc finger and one SPRY domain. Via its RING-type zinc finger, RNF135 may play a role in transcriptional regulation and protein degradation events. Defects in the gene encoding RNF135 are the cause of RNF135-related overgrowth syndrome which is characterized by learning disabilities, facial dysmorphism and increased weight and height. Multiple isoforms of RNF135 exist due to alternative splicing events.

UOM: 1 * 100 µl