You Searched For: Zinc+nitride

Catalog Number: (USBI044342-BIOTIN)

Supplier: US Biological

Description: Anti-ZNF708 Rabbit Polyclonal Antibody (Biotin)

UOM: 1 * 200 µl

Catalog Number: (BOSSBS-2510R-HRP)

Supplier: Bioss

Description: ZNF217 (Zinc-finger protein 217) is a Kruppel-like zinc-finger protein which functions as a transcriptional repressor protein and forms a complex with a number of proteins including CoREST, BHC110/LSD1, HDAC2 and CtBP1. ZNF217 has been shown to repress E-cadherin promoter activity. ZNF217 is overexpressed in a number of cancers including breast and ovarian. ZNF217 and its associated proteins have been implicated in a novel pathway that is involved in cancer progression.

UOM: 1 * 100 µl

Catalog Number: (USBI044090-BIOTIN)

Supplier: US Biological

Description: Anti-ZKSCAN1 Rabbit Polyclonal Antibody (Biotin)

UOM: 1 * 200 µl

Catalog Number: (BOSSBS-9261R-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. RNF185 (ring finger protein 185), also known as FLJ38628, is a 192 amino acid multi-pass membrane protein containing one RING-type zinc finger. Two RNF185 isoforms exist as a result of alternative splicing, and the gene encoding RNF185 maps to human chromosome 22, which houses over 500 genes and is the second smallest human chromosome. Mutations in several of the genes that map to chromosome 22 are involved in the development of Phelan-McDermid syndrome, Neurofibromatosis type 2, autism and schizophrenia.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13578R-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 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-9261R-A647)

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. RNF185 (ring finger protein 185), also known as FLJ38628, is a 192 amino acid multi-pass membrane protein containing one RING-type zinc finger. Two RNF185 isoforms exist as a result of alternative splicing, and the gene encoding RNF185 maps to human chromosome 22, which houses over 500 genes and is the second smallest human chromosome. Mutations in several of the genes that map to chromosome 22 are involved in the development of Phelan-McDermid syndrome, Neurofibromatosis type 2, autism and schizophrenia.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11277R-CY5)

Supplier: Bioss

Description: DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-11277R-CY3)

Supplier: Bioss

Description: DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9264R-A680)

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. RNF215 (ring finger protein 215), is a 377 amino acid multi-pass membrane protein containing one RING-type zinc finger. The gene encoding RNF215 maps to human chromosome 22, which houses over 500 genes and is the second smallest human chromosome. Mutations in several of the genes that map to chromosome 22 are involved in the development of Phelan-McDermid syndrome, Neurofibromatosis type 2, autism and schizophrenia.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9264R-A750)

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. RNF215 (ring finger protein 215), is a 377 amino acid multi-pass membrane protein containing one RING-type zinc finger. The gene encoding RNF215 maps to human chromosome 22, which houses over 500 genes and is the second smallest human chromosome. Mutations in several of the genes that map to chromosome 22 are involved in the development of Phelan-McDermid syndrome, Neurofibromatosis type 2, autism and schizophrenia.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9162R-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. TRIM17 (tripartite motif-containing 17), also known as RBCC, terf or RNF16, is a 477 amino acid protein that contains one RING-type zinc finger, one SPRY domain and one B box-type zinc finger. Expressed nearly exclusively in testis, TRIM17 belongs to the TRIM family and, based on its functional domains, may play a role in transcriptional regulation events. The gene encoding TRIM17 maps to human chromosome 1, which spans 260 million base pairs, contains over 3,000 genes and comprises nearly 8% of the human genome. Chromosome 1 houses a large number of disease-associated genes, including those that are involved in familial adenomatous polyposis, Stickler syndrome, Parkinson?s disease, Gaucher disease, schizophrenia and Usher syndrome. Aberrations in chromosome 1 are found in a variety of cancers, including head and neck cancer, malignant melanoma and multiple myeloma

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9162R-A647)

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. TRIM17 (tripartite motif-containing 17), also known as RBCC, terf or RNF16, is a 477 amino acid protein that contains one RING-type zinc finger, one SPRY domain and one B box-type zinc finger. Expressed nearly exclusively in testis, TRIM17 belongs to the TRIM family and, based on its functional domains, may play a role in transcriptional regulation events. The gene encoding TRIM17 maps to human chromosome 1, which spans 260 million base pairs, contains over 3,000 genes and comprises nearly 8% of the human genome. Chromosome 1 houses a large number of disease-associated genes, including those that are involved in familial adenomatous polyposis, Stickler syndrome, Parkinson’s disease, Gaucher disease, schizophrenia and Usher syndrome. Aberrations in chromosome 1 are found in a variety of cancers, including head and neck cancer, malignant melanoma and multiple myeloma

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12219R-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. 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-13578R-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 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-13373R-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 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-9186R-CY3)

Supplier: Bioss

Description: SMAD regulates gene expression by interacting with different classes of transcription factors including DNA-binding multi-zinc finger proteins. SIP1, for SMAD interacting protein 1, is a member of the delta-EF1/Zfh1 family of 2-handed zinc finger/homeodomain proteins. SIP1 contains a SMAD-binding domain, a homeodomain and two clusters of zinc fingers on the N- and C-termini. SIP1, also known as SMADIP1, ZFHX1B and ZEB2 (zinc finger E-box-binding protein 2), can be induced by TGF∫ treatment. SIP1 plays a crucial role in normal embryonic development of neural structures and the neural crest. The human SIP1 gene maps to chromosome 2q22. Mutations in the SIP1 gene cause a form of Hirschsprung disease (HSCR). Patients with SIP1 mutations show mental retardation, delayed motor development, epilepsy, microcephaly, distinct facial features and/or congenital heart disease—all symptoms of HSCR.

UOM: 1 * 100 µl