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Catalog Number: (BOSSBS-13581R-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 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-12239R-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 protein 750 is a 723 amino acid member of the Kr_ppel C2H2-type zinc finger protein family. localised to the nucleus, ZNF750 contains one conserved C2H2 zinc finger domain and is expressed in the skin, lungs, prostate, placenta and thymus. ZNF750 is also expressed in primary human keratinocytes but not in fibroblasts. Mutations in the gene encoding ZNF750 cause Seborrhea-like dermatitis with psoriasiform, a condition characterised by a chronic and diffuse rash on the face and hyperkeratosis of skin over the elbows, soles, knees and palms.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13580R-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 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-11753R-HRP)
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: (ABCAAB154680-100)
Supplier: Abcam
Description: Anti-Zinc finger antiviral protein Rabbit Polyclonal Antibody
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9230R-CY5.5)
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. SH3RF2 (SH3 domain containing ring finger 2), also known as RNF158, is a 729 amino acid protein with one RING-type zinc finger domain and three SH3 domains. Via its RING-type zinc finger domain, SH3RF2 binds an E2 ubiquitin-conjugating enzyme. This suggests that SH3RF2 functions as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and immediately transfers that residue to a protein that is targeted for degradation. Due to alternative splicing events, SH3RF2 is expressed as two different isoforms.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9230R-A488)
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. SH3RF2 (SH3 domain containing ring finger 2), also known as RNF158, is a 729 amino acid protein with one RING-type zinc finger domain and three SH3 domains. Via its RING-type zinc finger domain, SH3RF2 binds an E2 ubiquitin-conjugating enzyme. This suggests that SH3RF2 functions as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and immediately transfers that residue to a protein that is targeted for degradation. Due to alternative splicing events, SH3RF2 is expressed as two different isoforms.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9432R-A488)
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. TRIM8 (tripartite motif containing 8), also known as GERP (glioblastoma-expressed RING finger protein) or RNF27 (RING finger protein 27), is a 551 amino acid protein that is thought to function as an E3 ubiquitin-protein ligase that promotes SOCS-1 proteasomal degradation. As a widely expressed homodimer, TRIM8 localizes to nuclear bodies and contains two B box-type zinc fingers and one RING-type zinc finger. TRIM8 is expressed in lung, heart, brain and skeletal muscle, with low levels detected in intestine, placenta, leukocytes and liver. The gene encoding TRIM8 maps to human chromosome 10q24.32.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9432R-A350)
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. TRIM8 (tripartite motif containing 8), also known as GERP (glioblastoma-expressed RING finger protein) or RNF27 (RING finger protein 27), is a 551 amino acid protein that is thought to function as an E3 ubiquitin-protein ligase that promotes SOCS-1 proteasomal degradation. As a widely expressed homodimer, TRIM8 localizes to nuclear bodies and contains two B box-type zinc fingers and one RING-type zinc finger. TRIM8 is expressed in lung, heart, brain and skeletal muscle, with low levels detected in intestine, placenta, leukocytes and liver. The gene encoding TRIM8 maps to human chromosome 10q24.32.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9230R-HRP)
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. SH3RF2 (SH3 domain containing ring finger 2), also known as RNF158, is a 729 amino acid protein with one RING-type zinc finger domain and three SH3 domains. Via its RING-type zinc finger domain, SH3RF2 binds an E2 ubiquitin-conjugating enzyme. This suggests that SH3RF2 functions as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and immediately transfers that residue to a protein that is targeted for degradation. Due to alternative splicing events, SH3RF2 is expressed as two different isoforms.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9379R-A680)
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-9379R-A488)
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-9432R-HRP)
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. TRIM8 (tripartite motif containing 8), also known as GERP (glioblastoma-expressed RING finger protein) or RNF27 (RING finger protein 27), is a 551 amino acid protein that is thought to function as an E3 ubiquitin-protein ligase that promotes SOCS-1 proteasomal degradation. As a widely expressed homodimer, TRIM8 localizes to nuclear bodies and contains two B box-type zinc fingers and one RING-type zinc finger. TRIM8 is expressed in lung, heart, brain and skeletal muscle, with low levels detected in intestine, placenta, leukocytes and liver. The gene encoding TRIM8 maps to human chromosome 10q24.32.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9432R-CY3)
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. TRIM8 (tripartite motif containing 8), also known as GERP (glioblastoma-expressed RING finger protein) or RNF27 (RING finger protein 27), is a 551 amino acid protein that is thought to function as an E3 ubiquitin-protein ligase that promotes SOCS-1 proteasomal degradation. As a widely expressed homodimer, TRIM8 localizes to nuclear bodies and contains two B box-type zinc fingers and one RING-type zinc finger. TRIM8 is expressed in lung, heart, brain and skeletal muscle, with low levels detected in intestine, placenta, leukocytes and liver. The gene encoding TRIM8 maps to human chromosome 10q24.32.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12215R-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. ZNF266 is a 549 amino acid nuclear protein belonging to the Krüppel 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-12215R)
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. ZNF266 is a 549 amino acid nuclear protein belonging to the Krüppel 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


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at eurega_services@eu.vwr.com
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