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Catalog Number: (BOSSBS-13192R-CY3)
Supplier: Bioss
Description: Fibronectins are multi-domain glycoproteins that bind to a variety of substances including collagen, actin, heparin, DNA, fibrin and fibronectin receptors. They are involved in a diverse array of important functions such as blood coagulation, wound healing, cell adhesion, cell differentiation and migration. FNDC4 (Fibronectin type III domain-containing protein 4), also known as FRCP1 (Fibronectin type III repeat-containing protein 1), is a 234 amino acid membrane protein that contains one fibronectin type-III domain, which serves as a binding site for DNA, heparin or the cell surface. The gene encoding FNDC4 is localized to human chromosome two, which houses over 1,400 genes and comprises nearly 8% of the human genome.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13192R)
Supplier: Bioss
Description: Fibronectins are multi-domain glycoproteins that bind to a variety of substances including collagen, actin, heparin, DNA, fibrin and fibronectin receptors. They are involved in a diverse array of important functions such as blood coagulation, wound healing, cell adhesion, cell differentiation and migration. FNDC4 (Fibronectin type III domain-containing protein 4), also known as FRCP1 (Fibronectin type III repeat-containing protein 1), is a 234 amino acid membrane protein that contains one fibronectin type-III domain, which serves as a binding site for DNA, heparin or the cell surface. The gene encoding FNDC4 is localized to human chromosome two, which houses over 1,400 genes and comprises nearly 8% of the human genome.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13581R-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. 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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12228R-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 protein 568 (ZNF568) is a 644 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZNF568 contains fifteen C2H2-type zinc fingers and one KRAB domain through which it is thought to be involved in DNA-binding and transcriptional regulation. Two isoforms of ZNF568 exist as a result of alternative splicing events.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12228R-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 protein 568 (ZNF568) is a 644 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZNF568 contains fifteen C2H2-type zinc fingers and one KRAB domain through which it is thought to be involved in DNA-binding and transcriptional regulation. Two isoforms of ZNF568 exist as a result of alternative splicing events.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12908R)
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 protein. ZBTB44 is a 570 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZBTB44 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 ZBTB44 functions as a transcription regulator. Four isoforms of ZBTB44 have been identified.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12908R-A350)
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 protein. ZBTB44 is a 570 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZBTB44 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 ZBTB44 functions as a transcription regulator. Four isoforms of ZBTB44 have been identified.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13581R-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. 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-13581R-A350)
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-12908R-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 Krüppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying protein. ZBTB44 is a 570 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZBTB44 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 ZBTB44 functions as a transcription regulator. Four isoforms of ZBTB44 have been identified.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13205R-CY7)
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-13205R-A555)
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-3737R-CY3)
Supplier: Bioss
Description: Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated proinflammatory responses.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-3737R-CY7)
Supplier: Bioss
Description: Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated proinflammatory responses.
UOM: 1 * 100 µl


Catalog Number: (ENZOALX210879R100)
Supplier: ENZO LIFE SCIENCES
Description: MDA (Malondialdehyde) is a highly reactive three carbon dialdehyde produced as a byproduct of polyunsaturated fatty acid peroxidation and arachidonic acid metabolism. MDA readily combines with several functional groups on molecules including proteins, lipoproteins, and DNA. MDA modified proteins may show altered physico-chemical behavior and antigenicity. Antibodies to MDA will help to visualize the MDA-adducts.
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


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