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Catalog Number: (BOSSBS-15486R-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 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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-15486R-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. 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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-15486R-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. 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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-8687R-A555)
Supplier: Bioss
Description: p53, a DNA-binding, oligomerization domain- and transcription activation domain-containing tumor suppressor, upregulates growth arrest and apoptosis-related genes in response to stress signals, thereby influencing programmed cell death, cell differentiation, and cell cycle control mechanisms. p53 localizes to the nucleus, yet can be chaperoned to the cytoplasm by the negative regulator, MDM2. MDM2 is an E3 ubiquitin ligase that is upregulated in the presence of active p53, where it poly-ubiquitinates p53 for proteasome targeting. p53 fluctuates between latent and active DNA-binding conformations and is differentially activated through posttranslational modifications, including phosphorylation and acetylation. Mutations in the DNA-binding domain (DBD) of p53, amino acids 110-286, can compromise energetically-favorable association with cis elements and are implicated in several human cancers.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13578R-A555)
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-12219R-A555)
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-12236R-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. 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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12236R)
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, 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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12223R)
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. ZNF786 (zinc finger protein 786) is a 782 amino acid protein that belongs to the Krüppel C2H2-type zinc-finger protein family and is thought to function in transcriptional regulation. Localizing to nucleus, ZNF786 contains sixteen C2H2-type zinc fingers, a single KRAB domain and is encoded by a gene that maps to human chromosome 7q36.1.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11293R)
Supplier: Bioss
Description: The Hox homeobox genes encode proteins that are transcriptional regulators with an established role in embryonic development. HoxA4 (homeobox A4), also known as HOX1D or HOX1, is a 320 amino acid protein that localizes to the nucleus and contains one homeobox DNA-binding domain. Expressed in the embryonic nervous system, HoxA4 functions as a sequence-specific DNA-binding transcription factor that is part of a regulatory mechanism that provides cells with positional identities during development. Via its ability to bind DNA, HoxA4 plays an important role in the regulation of gene expression, as well as morphogenesis and differentiation. The gene encoding HoxA4 maps to human chromosome 7, which houses over 1,000 genes and comprises nearly 5% of the human genome. Defects in some of the genes localized to chromosome 7 have been linked to Osteogenesis imperfecta, Williams-Beuren syndrome, Pendred syndrome, Lissencephaly, Citrullinemia and Shwachman-Diamond syndrome.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13580R-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 48 (ZBTB48), also known as Kruppel-related zinc finger protein 3 or HKR3, is a 688 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZBTB48 is expressed in the adrenal gland and neuroblastoma cell lines. ZBTB48 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 ZBTB48 functions as a transcription regulator.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13205R-A488)
Supplier: Bioss
Description: The forkhead domain-containing gene family (Fox) comprises over 20 members in mammals and is defined by a conserved 110 amino-acid motif containing a winged helix structure DNA-binding domain. The members of this gene family have been implicated as key regulators of embryogenesis, cell cycling, cell lineage restriction and cancer. As such, FOXN2 contains a domain with homology to the forkhead DNA binding domain. FOXN2, or Human T-cell leukemia virus enhancer factor, is a 341 amino acid protein mapping to human gene FOXN2, which has been localized to human chromosome 2p16-p22. This protein, encoded by a 1239-bp cDNA isolated from the Jurkat cDNA library, is capable of binding to a region of the human T-cell leukemia virus long terminal repeat (HTLV-I LTR) located between amino acids 155 and 117. This purine-rich region is important in the regulation of gene expression by the Ets family of transcription factors. FOXN2 is a unique cellular gene that may function in the transcriptional regulation of HTLV-I LTR.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13026R-CY7)
Supplier: Bioss
Description: Methylation at the 5'-position of cytosine is the only known naturally occurring covalent modification of the mammalian genome. DNA methylation requires the enzymatic activity of DNA 5-cytosine methyltransferase (Dnmt) proteins, which catalyze the transfer of a methyl group from S-adenosyl methionine to the 5'-position of cytosines, thereby repressing expression of the target gene. Dnmt3L (DNA (cytosine-5)-methyltransferase 3-like) is a 387 amino acid protein that contains one ADD-type zinc finger and is a member of the Dnmt family. Localized to the nucleus and expressed at lows levels in thymus, testis and ovary, Dnmt3L does not exhibit DNA methyltransferase activity, but is able to stimulate de novo methylation by Dnmt3 and is thought to play a key role in the establishment of genomic imprints. Additionally, Dnmt3L interacts with histone deacetylase 1 (HDAC1) and, through this interaction, mediates transcriptional repression. Multiple isoforms of Dnmt3L exist due to alternative splicing events.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-15486R-CY3)
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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13026R-CY5)
Supplier: Bioss
Description: Methylation at the 5'-position of cytosine is the only known naturally occurring covalent modification of the mammalian genome. DNA methylation requires the enzymatic activity of DNA 5-cytosine methyltransferase (Dnmt) proteins, which catalyze the transfer of a methyl group from S-adenosyl methionine to the 5'-position of cytosines, thereby repressing expression of the target gene. Dnmt3L (DNA (cytosine-5)-methyltransferase 3-like) is a 387 amino acid protein that contains one ADD-type zinc finger and is a member of the Dnmt family. Localized to the nucleus and expressed at lows levels in thymus, testis and ovary, Dnmt3L does not exhibit DNA methyltransferase activity, but is able to stimulate de novo methylation by Dnmt3 and is thought to play a key role in the establishment of genomic imprints. Additionally, Dnmt3L interacts with histone deacetylase 1 (HDAC1) and, through this interaction, mediates transcriptional repression. Multiple isoforms of Dnmt3L exist due to alternative splicing events.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13026R)
Supplier: Bioss
Description: Methylation at the 5'-position of cytosine is the only known naturally occurring covalent modification of the mammalian genome. DNA methylation requires the enzymatic activity of DNA 5-cytosine methyltransferase (Dnmt) proteins, which catalyze the transfer of a methyl group from S-adenosyl methionine to the 5'-position of cytosines, thereby repressing expression of the target gene. Dnmt3L (DNA (cytosine-5)-methyltransferase 3-like) is a 387 amino acid protein that contains one ADD-type zinc finger and is a member of the Dnmt family. Localized to the nucleus and expressed at lows levels in thymus, testis and ovary, Dnmt3L does not exhibit DNA methyltransferase activity, but is able to stimulate de novo methylation by Dnmt3 and is thought to play a key role in the establishment of genomic imprints. Additionally, Dnmt3L interacts with histone deacetylase 1 (HDAC1) and, through this interaction, mediates transcriptional repression. Multiple isoforms of Dnmt3L exist due to alternative splicing events.
UOM: 1 * 100 µl


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