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Catalog Number: (10480-126)
Supplier: Bioss
Description: Carbonic anhydrases (CAs) are members of a large family of zinc metalloenzymes responsible for catalyzing the reversible hydration of carbon dioxide. CAs show extensive diversity in their distribution and subcellular localization. They are involved in a variety of biological processes, including calcification, bone resorption, respiration, acid-base balance and the formation of aqueous humor, saliva, gastric juice and cerebrospinal fluid. CA XI, also referred to as carbonic anhydrase-related protein 11 precursor (CA-RP XI) or carbonic anhydrase-related protein 2 (CA-RP II), is a member of the carbonic anhydrase family that lacks two of the three Zn-binding motifs essential for carbonic anhydrase activity. For this reason, CA XI does not exhibit catalytic activity. It is expressed primarily in brain but is also found in spinal cord and thyroid. CA XI may play a role in brain development.Tissue specificity:Expressed abundantly in the brain with moderate expression also present in spinal cord and thyroid.


Catalog Number: (76107-366)
Supplier: Bioss
Description: Carbonic anhydrases (CAs) are members of a large family of zinc metalloenzymes responsible for catalyzing the reversible hydration of carbon dioxide. CAs show extensive diversity in their distribution and subcellular localization. They are involved in a variety of biological processes, including calcification, bone resorption, respiration, acid-base balance and the formation of aqueous humor, saliva, gastric juice and cerebrospinal fluid. CA XI, also referred to as carbonic anhydrase-related protein 11 precursor (CA-RP XI) or carbonic anhydrase-related protein 2 (CA-RP II), is a member of the carbonic anhydrase family that lacks two of the three Zn-binding motifs essential for carbonic anhydrase activity. For this reason, CA XI does not exhibit catalytic activity. It is expressed primarily in brain but is also found in spinal cord and thyroid. CA XI may play a role in brain development.Tissue specificity:Expressed abundantly in the brain with moderate expression also present in spinal cord and thyroid.


Catalog Number: (76110-050)
Supplier: Bioss
Description: Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.


Catalog Number: (10484-054)
Supplier: Bioss
Description: The hydroxyacylglutathione hydrolase-like protein (HAGHL) is a 290 amino acid protein that belongs to the glyoxalase II family. HAGHL binds two zinc ions per subunit and acts as a hydrolase on ester bonds. The gene encoding HAGHL maps to human chromosome 16, which encodes over 900 genes in approximately 90 million base pairs, makes up nearly 3% of human cellular DNA and is associated with a variety of genetic disorders. The rare disorder Rubinstein-Taybi syndrome is associated with chromosome 16, as is Crohn's disease, a gastrointestinal inflammatory condition that may involve the NOD2 gene. An association with systemic lupus erythematosis and a number of other autoimmune disorders with the pericentromeric region of chromosome 16 has led to the identification of SLC5A11 as a potential autoimmune modifier.


Catalog Number: (10797-728)
Supplier: Prosci
Description: Cluster of differentiation 10 (CD10) is also known as membrane metallo-endopeptidase, neutral endopeptidase (NEP), Neprilysin, and common acute lymphoblastic leukemia antigen (CALLA), is a 90-110-kDa type II transmembrane glycoprotein normally expressed by a variety of tissues, including epithelial cells of the prostate, kidney, intestine, endometrium, adrenal glands, and lung. This zinc-dependent metalloprotease enzyme cleaves peptide bonds on the amino side of hydrophobic residues and inactivates a variety of physiologically active secreted peptides. CD20 is thought to be the rate-limiting degrading enzyme of amyloid ? peptide (A?) whose abnormal misfolding and aggregation in neural tissue has been implicated in the development of Alzheimer's disease (AD). CD10 is also identified as the common acute lymphoblastic leukemia antigen (CALLA) present on leukemic cells of pre-B phenotype, and thus serves as the most important biomarker in the diagnosis of human acute lymphocytic leukemia (ALL).


Catalog Number: (10097-250)
Supplier: Proteintech
Description: ZBTB7B belongs to a large family of transcription factors, generally acting as repressors, characterized by a carboxy-terminal DNA binding domain made of multiple zinc fingers (four in Thpok) and an amino-terminal BTB-POZ domain that mediates homo- (and possibly hetero-) dimerization . Zbtb7b is up-regulated by MHC-II-restricted thymocytes during their CD4 differentiation and is a major determinant of CD4 lineage choice. Two properties of ZBTB7B deserve attention. First, although Thpok is expressed in a wide variety of cells, its expression in the thymus is highly lineage-specific : CD4 SP thymocytes (and all CD4 T cells) express Thpok, whereas DP and CD8 SP thymocytes do notSecond, both loss- and gain-of-function experiments indicate that Thpok affects lineage choice but not positive selection .


Catalog Number: (10797-730)
Supplier: Prosci
Description: Cluster of differentiation 10 (CD10) is also known as membrane metallo-endopeptidase, neutral endopeptidase (NEP), Neprilysin, and common acute lymphoblastic leukemia antigen (CALLA), is a 90-110-kDa type II transmembrane glycoprotein normally expressed by a variety of tissues, including epithelial cells of the prostate, kidney, intestine, endometrium, adrenal glands, and lung. This zinc-dependent metalloprotease enzyme cleaves peptide bonds on the amino side of hydrophobic residues and inactivates a variety of physiologically active secreted peptides. CD20 is thought to be the rate-limiting degrading enzyme of amyloid ? peptide (A?) whose abnormal misfolding and aggregation in neural tissue has been implicated in the development of Alzheimer's disease (AD). CD10 is also identified as the common acute lymphoblastic leukemia antigen (CALLA) present on leukemic cells of pre-B phenotype, and thus serves as the most important biomarker in the diagnosis of human acute lymphocytic leukemia (ALL).


Catalog Number: (10667-942)
Supplier: Bioss
Description: Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.


Catalog Number: (10671-956)
Supplier: Bioss
Description: Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.


Catalog Number: (10671-958)
Supplier: Bioss
Description: Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.


Catalog Number: (10671-942)
Supplier: Bioss
Description: Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.


Catalog Number: (10667-940)
Supplier: Bioss
Description: Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.


Catalog Number: (10671-960)
Supplier: Bioss
Description: Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.


Catalog Number: (76110-052)
Supplier: Bioss
Description: Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). Ubr2 (Ubiquitin-protein ligase E3-alpha-2), also known as N-recognin-2, is a 1755 amino acid protein that contains one UBR-type zinc finger and one RING-type zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr2 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation. Mice lacking Ubr2 are infertile due to defects in male meiosis.


Catalog Number: (10782-366)
Supplier: Biosensis
Description: FUNCTION: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1/Tip60 and inhibit Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. May be involved in copper homeostasis/oxidative stress through copper ion reduction. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. FUNCTION: Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. Rat and mouse beta-amyloid peptides bind only weakly transient metals and have little reducing activity due to substitutions of transient metal chelating residues. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation (By similarity). FUNCTION: The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. SUBUNIT: Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1, Numb and Dab1. Binding to Dab1 inhibits its serine phosphorylation. Also interacts with GPCR-like protein BPP, FPRL1, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains. Associates with microtubules in the presence of ATP and in a kinesin-dependent manner. Interacts, through a C-terminal domain, with GNAO1. Amyloid beta-42 binds CHRNA7 in hippocampal neurons. Beta-amyloid associates with HADH2. TISSUE SPECIFICITY: different isoforms in different tissues: kidney. brain. liver. hippocampus, substania nigra pars compacta and cerebellum. In the cerebellum, all the isoforms are abundantly expressed in Purkinje cells.


Catalog Number: (10782-368)
Supplier: Biosensis
Description: FUNCTION: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1/Tip60 and inhibit Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. May be involved in copper homeostasis/oxidative stress through copper ion reduction. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. FUNCTION: Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. Rat and mouse beta-amyloid peptides bind only weakly transient metals and have little reducing activity due to substitutions of transient metal chelating residues. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation (By similarity). FUNCTION: The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. SUBUNIT: Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1, Numb and Dab1. Binding to Dab1 inhibits its serine phosphorylation. Also interacts with GPCR-like protein BPP, FPRL1, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains. Associates with microtubules in the presence of ATP and in a kinesin-dependent manner. Interacts, through a C-terminal domain, with GNAO1. Amyloid beta-42 binds CHRNA7 in hippocampal neurons. Beta-amyloid associates with HADH2. TISSUE SPECIFICITY: different isoforms in different tissues: kidney. brain. liver. hippocampus, substania nigra pars compacta and cerebellum. In the cerebellum, all the isoforms are abundantly expressed in Purkinje cells.


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