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Supplier: Whatman products (Cytiva)
Description: These borosilicate glass filters are ideal for measuring landfill leachate composition with a TCLP test. They can also be used for DNA binding and purification, filtering finely precipitated proteins and filtering biochemical solutions, fluids, and nucleic acids.

Catalog Number: (BOSSBS-12476R-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. 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-12476R-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. 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-12212R-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 Kr_ppel C2H2-type zinc-finger protein family, ZNF342 (zinc finger protein 342), also known as Zinc finger protein 296, is a 475 amino acid nuclear protein that contains six C2H2-type zinc fingers through which it is thought to be involved in DNA-binding and transcriptional regulation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12235R-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. ZNF346 (Zinc finger protein 346), also known as JAZ (Just another zinc finger protein), is a 294 amino acid protein that contains four matrin-type zinc fingers. The matrin-type zinc finger, which is very similar in structure to the classical DNA-binding C2H2 zinc finger, was first identified in the protein matrin-3. The matrin-type zinc finger has also been identified in several spliceosome RNA-binding proteins. Two isoforms exists due to alternate splicing events.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12212R-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 proteins. As a member of the Krüppel C2H2-type zinc-finger protein family, ZNF342 (zinc finger protein 342), also known as Zinc finger protein 296, is a 475 amino acid nuclear protein that contains six C2H2-type zinc fingers through which it is thought to be involved in DNA-binding and transcriptional regulation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12212R-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. As a member of the Krüppel C2H2-type zinc-finger protein family, ZNF342 (zinc finger protein 342), also known as Zinc finger protein 296, is a 475 amino acid nuclear protein that contains six C2H2-type zinc fingers through which it is thought to be involved in DNA-binding and transcriptional regulation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12212R-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. As a member of the Krüppel C2H2-type zinc-finger protein family, ZNF342 (zinc finger protein 342), also known as Zinc finger protein 296, is a 475 amino acid nuclear protein that contains six C2H2-type zinc fingers through which it is thought to be involved in DNA-binding and transcriptional regulation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12228R-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 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-13581R-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. 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. 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-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 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-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 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-13192R-A680)
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-12908R-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 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-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-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


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