You Searched For: Zinc+nitride

Catalog Number: (BOSSBS-9265R-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. RNF32 (RING finger protein 32), also known as HSD15 or FKSG33, is a 362 amino acid cytoplasmic protein that contains one IQ domain and two RING-type zinc fingers. Highly expressed in testis with lower expression levels in ovary tissue, RNF32 is thought to play a role in spermatogenesis, specifically contributing to the growth and maturation of round spermatids. Six isoforms of RNF32 exist due to alternative splicing events.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-7418R-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. ZDHHC20 (zinc finger, DHHC-type containing 20) is a 365 amino acid multi-pass membrane protein that contains one DHHC-type zinc finger and is thought to function as a palmitoyltransferase, catalyzing the transformation of palmitoyl-CoA and a cysteine-conjugated protein to an S-palmitoyl protein and free CoA. In response to DNA damage, ZDHHC20, which exists as multiple alternatively spliced isoforms, may be phosphorylated by ATM or ATR. The gene encoding ZDHHC20 maps to human chromosome 13, which houses over 400 genes, such as BRCA2 and RB1, and comprises nearly 4% of the human genome.

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-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-11277R)

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-A680)

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 Signalling.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9261R-FITC)

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-9342R)

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. MARCH8 (membrane-associated ring finger (C3HC4) 8), also known as MIR or RNF178 (RING finger protein 178), is a 291 amino acid multi-pass membrane protein that localizes to vesicle membranes and contains one RING-CH-type zinc finger. Expressed in a variety of tissues, including immature dendritic cells, MARCH8 functions as an E3 ubiquitin ligase that is thought to regulate immune responses by promoting the ubiquitination and subsequent degradation of target proteins, such as B7-2 and CD71.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-8495R-A350)

Supplier: Bioss

Description: RFPL4B contains 1 B30.2/SPRY domain and 1 RING type zinc finger. The function of RFPL4B remains unknown.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-8495R-A488)

Supplier: Bioss

Description: RFPL4B contains 1 B30.2/SPRY domain and 1 RING type zinc finger. The function of RFPL4B remains unknown.

UOM: 1 * 100 µl

Catalog Number: (1724736.)

Supplier: USP

Description: USP Reference Standards are specified for use in conducting official USP–NF tests and assays. USP also provides Reference Standards specified in the Food Chemicals Codex as well as authentic substances—high-quality chemical samples—as a service to analytical, clinical, pharmaceutical and research laboratories. To confirm accuracy and reproducibility, USP Reference Standards are rigorously tested and evaluated by multiple independent laboratories including USP, commercial, regulatory, and academic labs. USP also provide publicly available, official documentary standards for pharmaceutical ingredients in the USP–NF that link directly with our primary reference standards.

UOM: 1 * 100 mg

Catalog Number: (BOSSBS-9635R-HRP)

Supplier: Bioss

Description: Zinc is an essential cofactor that is involved in cell growth and development, as well as in protein, nucleic acid and lipid metabolism. The transport of zinc across the cell membrane is crucial for correct enzyme and overall cell function. SLC39A11 (solute carrier family 39 (metal ion transporter), member 11), also known as ZIP11 (Zrt- and Irt-like protein 11), is a 342 amino acid multi-pass membrane protein belonging to the ZIP transporter family. Expressed as multiple alternatively spliced isoforms, SLC39A11 acts as a zinc-influx transporter and is encoded by a gene located on human chromosome 17, which comprises over 2.5% of the human genome and encodes over 1,200 genes, some of which are involved in tumor suppression and in the pathogenesis of Li-Fraumeni syndrome, early onset breast cancer and a predisposition to cancers of the ovary, colon, prostate gland and fallopian tubes.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9258R-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 protein-protein interactions and protein-DNA interactions. Specifically, they are thought to be involved in the ubiquitination pathway of protein degradation. RNF165 (RING finger protein 165) is a 346 amino acid protein that contains one RING-type zinc finger. Via its RING-type zinc finger, RNF165 may play a role in transcriptional regulation and protein degradation events. The gene encoding RNF165 maps to human chromosome 18, which houses over 300 genes, including Trisomy 18, or Edwards syndrome, the second most common trisomy after Downs syndrome. Translocation between chromosome 18 and 14 is the most common translocation in cancers, and occurs in follicular lymphomas. Niemann-Pick disease, hereditary hemorrhagic telangiectasia and erythropoietic protoporphyria are also associated with chromosome 18.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9258R-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 protein-protein interactions and protein-DNA interactions. Specifically, they are thought to be involved in the ubiquitination pathway of protein degradation. RNF165 (RING finger protein 165) is a 346 amino acid protein that contains one RING-type zinc finger. Via its RING-type zinc finger, RNF165 may play a role in transcriptional regulation and protein degradation events. The gene encoding RNF165 maps to human chromosome 18, which houses over 300 genes, including Trisomy 18, or Edwards syndrome, the second most common trisomy after Downs syndrome. Translocation between chromosome 18 and 14 is the most common translocation in cancers, and occurs in follicular lymphomas. Niemann-Pick disease, hereditary hemorrhagic telangiectasia and erythropoietic protoporphyria are also associated with chromosome 18.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9238R-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. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localizes to cytosol but shifts to mitochondria upon co-localization with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-9161R-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. 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