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Nickel(II)+p-toluenesulfonate


18,822  results were found

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Supplier:  Bioss
Description:   APMAP is a 416 amino acid single-pass type II membrane protein that belongs to the strictosidine synthase family and is thought to play a role in adipocyte differentiation. The gene encoding C20orf3 maps to human chromosome 20, which houses over 600 genes some of which are associated with Creutzfeldt-Jakob disease, amyotrophic lateral sclerosis, spinal muscular atrophy, ring chromosome 20 epilepsy syndrome and Alagille syndrome. Additionally, chromosome 20 contains a region with numerous genes which are thought important for seminal production and may be potential targets for male contraception.

Supplier:  Bioss
Description:   MP21 is a member of the EMP24/GP25L/p24 cargo family of proteins that regulates vesicular trafficking in the early secretory pathway. TMP21 is a ubiquitously expressed single-pass type I membrane protein localizing to the Golgi cisternae and the plasma membrane. It contains one GOLD (Golgi dynamics) domain and participates in protein transport and quality control between the endoplasmic reticulum (ER) and the Golgi complex. In addition, TMP21 is a component of the heteromeric secretase complex (or Presenilin complex) and functions to regulate the ?secretase activity. Two isoforms, namely TMP21-I and TMP21-II, exist for this protein.
Supplier:  Adipogen
Description:   Most commonly-used phorbol ester. Binds to and activates protein kinase C (PKC) at nM concentrations. Induces cell growth arrest through a variety of pathways including the mitogen-activated protein kinases (MAPKs), p38 and c-Jun N-terminal kinase (JNK) pathways mediated by cyclin dependent kinase (CDK) inhibitors such as p21WAF1/CIP1, p27KIP1, p15 and p16. Potent mouse skin tumor promoter. Promoter of inducible NOS (iNOS; NOS II). Apoptosis inducer. Potential effective cancer therapeutic agent. Inhibitor of anti-lipolytic activity of insulin.
Small Business Enterprise
Supplier:  Bioss
Description:   Substrate-recognition component of the CSA complex, a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, involved in transcription-coupled nucleotide excision repair. The CSA complex (DCX(ERCC8) complex) promotes the ubiquitination and subsequent proteasomal degradation of ERCC6 in a UV-dependent manner; ERCC6 degradation is essential for the recovery of RNA synthesis after transcription-coupled repair. It is required for the recruitment of XAB2, HMGN1 and TCEA1/TFIIS to a transcription-coupled repair complex which removes RNA polymerase II-blocking lesions from the transcribed strand of active genes.
Supplier:  Bioss
Description:   Substrate-recognition component of the CSA complex, a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, involved in transcription-coupled nucleotide excision repair. The CSA complex (DCX(ERCC8) complex) promotes the ubiquitination and subsequent proteasomal degradation of ERCC6 in a UV-dependent manner; ERCC6 degradation is essential for the recovery of RNA synthesis after transcription-coupled repair. It is required for the recruitment of XAB2, HMGN1 and TCEA1/TFIIS to a transcription-coupled repair complex which removes RNA polymerase II-blocking lesions from the transcribed strand of active genes.
Supplier:  Biotium
Description:   This antibody recognizes an oncofetal glycoprotein with a single chain of 70 kDa, which is identified as alpha fetoprotein (AFP). This MAb is highly specific to AFP and shows no cross-reaction with other oncofetal antigens or serum albumin. The yolk sac and the liver produce AFP during fetal life. AFP expression in adults is often associated with hepatoma or teratoma. However, hereditary persistence of alpha-fetoprotein may also be found in individuals with no obvious pathology. The protein is thought to be the fetal counterpart of serum albumin, and the AFP and albumin genes are present in tandem in the same transcriptional orientation on chromosome 4. AFP is found in monomeric as well as dimeric and trimeric forms, and binds copper, nickel, fatty acids and bilirubin. The level of AFP in amniotic fluid is used to measure renal loss of protein to screen for spinal bifida and anencephaly.

CF® dyes are Biotium's next-generation fluorescent dyes. CF®405S is a blue fluorescent dye (Ex/Em 404/431 nm) with superior brightness compared to other blue dyes; it is also compatible with super-resolution imaging by SIM. Note: Conjugates of blue fluorescent dyes are not recommended for detecting low abundance targets, because blue dyes have lower fluorescence and can give higher non-specific background than other dye colors.

Supplier:  Genetex
Description:   Topoisomerases are nuclear enzymes involved in a variety of cellular activities such as chromosome condensation, DNA replication, transcription, recombination and segregation at mitosis. Human topoisomerase I is a 100kD protein capable of relaxing positively and negatively supercoiled DNA by performing a transient single-stranded nick which is then re-ligated at the end of the reaction. It has been shown that the enzyme is located in regions of the genome that are undergoing active RNA synthesis, where it probably reduces superhelical stresses in the DNA, enabling RNA polymerase to function properly. In normal eukaryotic cells, DNA topoisomerase I does not show relevant fluctuations across the cell cycle, unlike DNA topoisomerase II alpha. Both DNA topoisomerases I and II have been found to be targets of autoantibodies in the sera of patients with certain autoimmune diseases such as systemic lupus erythematosus and also of some anti-tumor drugs and antibiotics. Elevated levels of DNA topoisomerase I, detected by <sup>32</sup>P transfer assays, have been demonstrated in colorectal tumors compared with normal colon mucosa as a result of increased transcription or mRNA stability. Renal tumors were found not to show any differential levels compared with normal kidney. Topo I may be useful for the evaluation of DNA topoisomerase I expression in normal tissues, solid tumors and in further studies of ovarian, colorectal, cervical and prostatic tumors.
Catalog Number: (10398-598)

Supplier:  Bioss
Description:   Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. Along with the family of proteins known as defensins, cathelicidins participate in the first line of defense by preventing local infection and systemic invasion of microbes. FALL-39 precursor (FALL-39 peptide antibiotic, cationic anti-microbial protein, CAMP, CAP-18, HSD26) is a cathelicidin anti-microbial protein that contains the antibacterial peptide LL-37 (amino acids 134-170). In contrast to the defensins, which are cysteine-rich peptides that fold in ∫-pleated sheets, LL-37 is a cysteine-free peptide that can adopt an amphipathic Ã¥-helical conformation. LL-37 binds to bacterial lipopolysaccharides (LPS) and is a potent chemotactic factor for recruiting mast cells to sites of inflammation. LL-37 is present in inflammatory skin diseases that include psoriasis, sub-acute lupus erthematosus, dermatitis and nickel contact hypersensitivity. It is not found in normal skin epidermis. The secreted protein is expressed primarily in bone marrow, testis and neutrophils. The mouse and rat ortholog, CRAMP (cathelin-related antimicrobial peptide), is also part of the cathelicidin family of host defense peptides. These include precursors of potent antimicrobial peptides that direct antimicrobial activity against various microbial pathogens and also activate mesenchymal cells during wound repair. CRAMP is expressed in testis, spleen, stomach and intestine.
Catalog Number: (77440-656)

Supplier:  Bioss
Description:   This gene is a member of the DEAH-box family of RNA-dependent NTPases which are named after the conserved amino acid sequence Asp-Glu-Ala-His in motif II. The protein encoded by this gene has been shown to enhance the deadenylation and decay of mRNAs with 3'-UTR AU-rich elements (ARE-mRNA). The protein has also been shown to resolve into single strands the highly stable tetramolecular DNA configuration (G4) that can form spontaneously in guanine-rich regions of DNA. Alternative splicing results in multiple transcript variants encoding different isoforms. (provided by RefSeq, Jul 2008).

Supplier:  Bioss
Description:   Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. Along with the family of proteins known as defensins, cathelicidins participate in the first line of defense by preventing local infection and systemic invasion of microbes. FALL-39 precursor (FALL-39 peptide antibiotic, cationic anti-microbial protein, CAMP, CAP-18, HSD26) is a cathelicidin anti-microbial protein that contains the antibacterial peptide LL-37 (amino acids 134-170). In contrast to the defensins, which are cysteine-rich peptides that fold in ∫-pleated sheets, LL-37 is a cysteine-free peptide that can adopt an amphipathic Ã¥-helical conformation. LL-37 binds to bacterial lipopolysaccharides (LPS) and is a potent chemotactic factor for recruiting mast cells to sites of inflammation. LL-37 is present in inflammatory skin diseases that include psoriasis, sub-acute lupus erthematosus, dermatitis and nickel contact hypersensitivity. It is not found in normal skin epidermis. The secreted protein is expressed primarily in bone marrow, testis and neutrophils. The mouse and rat ortholog, CRAMP (cathelin-related antimicrobial peptide), is also part of the cathelicidin family of host defense peptides. These include precursors of potent antimicrobial peptides that direct antimicrobial activity against various microbial pathogens and also activate mesenchymal cells during wound repair. CRAMP is expressed in testis, spleen, stomach and intestine.

Supplier:  Bioss
Description:   Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. Along with the family of proteins known as defensins, cathelicidins participate in the first line of defense by preventing local infection and systemic invasion of microbes. FALL-39 precursor (FALL-39 peptide antibiotic, cationic anti-microbial protein, CAMP, CAP-18, HSD26) is a cathelicidin anti-microbial protein that contains the antibacterial peptide LL-37 (amino acids 134-170). In contrast to the defensins, which are cysteine-rich peptides that fold in ∫-pleated sheets, LL-37 is a cysteine-free peptide that can adopt an amphipathic Ã¥-helical conformation. LL-37 binds to bacterial lipopolysaccharides (LPS) and is a potent chemotactic factor for recruiting mast cells to sites of inflammation. LL-37 is present in inflammatory skin diseases that include psoriasis, sub-acute lupus erthematosus, dermatitis and nickel contact hypersensitivity. It is not found in normal skin epidermis. The secreted protein is expressed primarily in bone marrow, testis and neutrophils. The mouse and rat ortholog, CRAMP (cathelin-related antimicrobial peptide), is also part of the cathelicidin family of host defense peptides. These include precursors of potent antimicrobial peptides that direct antimicrobial activity against various microbial pathogens and also activate mesenchymal cells during wound repair. CRAMP is expressed in testis, spleen, stomach and intestine.

Supplier:  Bioss
Description:   ETFA participates in catalyzing the initial step of the mitochondrial fatty acid beta-oxidation. It shuttles electrons between primary flavoprotein dehydrogenases and the membrane-bound electron transfer flavoprotein ubiquinone oxidoreductase. Defects in electron-transfer-flavoprotein have been implicated in type II glutaricaciduria in which multiple acyl-CoA dehydrogenase deficiencies result in large excretion of glutaric, lactic, ethylmalonic, butyric, isobutyric, 2-methyl-butyric, and isovaleric acids. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier:  Bioss
Description:   ETFA participates in catalyzing the initial step of the mitochondrial fatty acid beta-oxidation. It shuttles electrons between primary flavoprotein dehydrogenases and the membrane-bound electron transfer flavoprotein ubiquinone oxidoreductase. Defects in electron-transfer-flavoprotein have been implicated in type II glutaricaciduria in which multiple acyl-CoA dehydrogenase deficiencies result in large excretion of glutaric, lactic, ethylmalonic, butyric, isobutyric, 2-methyl-butyric, and isovaleric acids. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008].

Supplier:  Bioss
Description:   Substrate-recognition component of the CSA complex, a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, involved in transcription-coupled nucleotide excision repair. The CSA complex (DCX(ERCC8) complex) promotes the ubiquitination and subsequent proteasomal degradation of ERCC6 in a UV-dependent manner; ERCC6 degradation is essential for the recovery of RNA synthesis after transcription-coupled repair. It is required for the recruitment of XAB2, HMGN1 and TCEA1/TFIIS to a transcription-coupled repair complex which removes RNA polymerase II-blocking lesions from the transcribed strand of active genes.
Supplier:  Southern Biotechnology
Description:   CD105, also known as endoglin, is a disulfide-linked type II transmembrane homodimer that is predominantly expressed on vascular endothelial cells. It is also found on pre-erythroblasts, macrophages, and lymphoid and myeloid leukemic cells. Both mouse and human CD105 exhibit >70% sequence homology in their cytoplasmic domains with type III transforming growth factor β (TGFβ) receptor. CD105 has been shown to be one of several receptors for the various isoforms of TGFβ which in turn is one of a family of proteins involved in regulation of cell differentiation, migration of cells, and control of the immune response.

Supplier:  Bioss
Description:   Cytochrome c oxidase subunit I (COI or MTCO1) is one of three mitochondrial DNA (mtDNA) encoded subunits (MTCO1, MTCO2, MTCO3) of respiratory Complex IV. Complex IV is located within the mitochondrial inner membrane and is the third and final enzyme of the electron transport chain of mitochondrial oxidative phosphorylation. Complex IV is composed of 13 polypeptides. Subunits I, II, and III (MTCO1, MTCO2, MTCO3) are encoded by mtDNA while subunits IV, Va, Vb, VIa, VIb, VIc, VIIa, VIIb, VIIc, and VIII are nuclear encoded. Mammalian MTCO1 has 12 membrane-spanning alpha-helices (I to XII).
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