Text Search >
Dioctyltin+oxide
Print…
You Searched For:
142,006 results were found
Dioctyltin+oxide
Catalog Number:
(RL617-100-130)
Supplier:
Rockland Immunochemical
Description:
Secondary Goat Anti-IgG IgA IgM Reacts with Monkey
Catalog Number:
(76073-046)
Supplier:
Prosci
Description:
For WB starting dilution is: 1:1000 For IHC-P starting dilution is: 1:50~100 For FACS starting dilution is: 1:10~50
Catalog Number:
(77322-352)
Supplier:
GeminiBio
Description:
GeminiBio’s Cell and Molecular Grade Water is manufactured specifically for your most stringent research applications. GemPure™ Cell and Molecular Grade Water is sterile and low endotoxin for your cell culture processes. Protease and nuclease free, it is perfect for any of your molecular biology needs as well saving valuable lab space and simplifying your purchasing process.
Catalog Number:
(PI26181)
Supplier:
Invitrogen
Description:
26181 is supplied as 2 ml of antibody on crosslinked 4% beaded agarose supplied as a 50% slurry in 0. 1M phosphate, 0. 15M NaCl, pH 7. 2 with 0. 05% sodium azide. Specific for the HA peptide YPYDVPDYA. The anti-HA agarose has been used successfully in immunoprecipitation applications. The anti-HA agarose has 3. 5mg mouse anti-HA IgG1 monoclonal antibody conjugated per mL of settled agarose resin. HA Synthetic Peptide is available for use in neutralization and control experiments and to competitively elute HA-tagged fusion proteins from immobilized anti-HA affinity resin. An HA tag is frequently incorporated into recombinant proteins for a variety of purposes. An anti-HA antibody can then be used to detect the protein when doing studies with transfected cells.
Catalog Number:
(76118-502)
Supplier:
Bioss
Description:
Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. <i>in vitro</i>, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.
Catalog Number:
(10451-498)
Supplier:
Bioss
Description:
Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.
Catalog Number:
(10294-992)
Supplier:
Bioss
Description:
Glucose-6-phosphatase (G6Pase), is a multicomponent enzyme system that hydrolyzes glucose-6-phosphate (G6P) in the final step of gluconeogenesis and gluconeolysis. G6Pase localizes to the endoplasmic reticulum, and while liver, kidney, and intestine are the only tissues that express the first identified isoform, G6Pase-Alpha, a second form, designated G6Pase-Beta, contributes to blood glucose homeostasis in a wider range of tissues. G6Pase-Beta, also known as SCN4, UGRP or G6PC3 (glucose 6 phosphatase, catalytic, 3), is a 346 amino acid endoplasmic reticulum multi-pass membrane protein that is involved in carbohydrate biosynthesis and the gluconeogenesis pathway. Inhibited by vanadate, G6Pase-Beta hydrolyzes GP6 to glucose in the endoplasmic reticulum. Due to its necessary involvement in normal glucose metabolism, G6Pase-Beta may play an integral role in diabetes and glycogen storage diseases (GSDs).
Catalog Number:
(10297-240)
Supplier:
Bioss
Description:
The glycine cleavage system is comprised of AMT (known as Protein T), GCSH (known as Protein H), DLD (known as Protein L) and GLDC (known as Protein P), all of which work together to catalyze the cleavage and degradation of glycine. GLDC (glycine dehydrogenase ), also known as GCE, GCSP (glycine cleavage system P protein) or HYGN1, is a 1,020 amino acid protein that localizes to the mitochondria and belongs to the gcvP family. GLDC binds to glycine and enables the methylamine group from glycine to be transferred to the Protein T. GLDC exists as a homodimer and utilizes pyridoxal phosphate as a cofactor. Mutations in the gene encoding GLDC leads to nonketotic hyperglycinemia (NKH), also known as glycine encephalopathy (GCE), an autosomal recessive disease characterized by accumulation of a large amount of glycine in body fluid and by severe neurological symptoms.
Catalog Number:
(10268-690)
Supplier:
Bioss
Description:
Binds to DNA, at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcription factor controlling nuclear gene expression, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin-loop remodeling. Acts as a docking site for several chromatin remodeling enzymes and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Required for the initiation of the upper-layer neurons (UL1) specific genetic program and for the inactivation of deep-layer neurons (DL) and UL2 specific genes, probably by modulating BCL11B expression. Repressor of Ctip2 and regulatory determinant of corticocortical connections in the developing cerebral cortex. May play an important role in palate formation. Acts as a molecular node in a transcriptional network regulating skeletal development and osteoblast differentiation.
Catalog Number:
(10464-952)
Supplier:
Bioss
Description:
Involved in translation as a component of the 40S small ribosomal subunit (PubMed:8706699). Has endonuclease activity and plays a role in repair of damaged DNA (PubMed:7775413). Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA (PubMed:15707971). Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS) (PubMed:14706345). Has also been shown to bind with similar affinity to intact and damaged DNA (PubMed:18610840). Stimulates the N-glycosylase activity of the base excision protein OGG1 (PubMed:15518571). Enhances the uracil excision activity of UNG1 (PubMed:18973764). Also stimulates the cleavage of the phosphodiester backbone by APEX1 (PubMed:18973764). When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage (PubMed:23911537). Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide (PubMed:17049931). Plays a role in regulating transcription as part of the NF-kappa-B p65-p50 complex where it binds to the RELA/p65 subunit, enhances binding of the complex to DNA and promotes transcription of target genes (PubMed:18045535). Represses its own translation by binding to its cognate mRNA (PubMed:20217897). Binds to and protects TP53/p53 from MDM2-mediated ubiquitination (PubMed:19656744). Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization (PubMed:23131551). Involved in induction of apoptosis through its role in activation of CASP8 (PubMed:14988002). Induces neuronal apoptosis by interacting with the E2F1 transcription factor and acting synergistically with it to up-regulate pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5 (PubMed:20605787). Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation (PubMed:22510408).
Catalog Number:
(10302-240)
Supplier:
Bioss
Description:
Protein kinases comprise a large group of encoded factors that regulate cellular processes by catalyzing the transfer of a phosphate group to a hydroxyl acceptor in serine, threonine or tyrosine residues (1,2). Kinases are capable of influencing the oncogenic potential of cell sytems at the level of oncoprotein or tumor suppressor protein phosphorylation states (1,2). STAP-2 is a protein that contains a pleckstrin homology (PH) domain and an SH2 domain, and associates with BRK (3). BRK (breast tumor kinase, Sik) is a 451 amino acid, nonreceptor protein-tyrosine kinase that is overexpressed in breast tumors and metastatic melanoma cell lines (4). Similar to the Src family of intracellular kinses, BRK is comprised of an SH3 domain, an SH2 domain, and a catalytic domain (5). STAP-2 is susceptiple to tyrosine phosphorylation and may be invovled in tyrosine kinase-mediated signaling cascades, whose aberrant function may lead to metastis (3).
Catalog Number:
(10748-768)
Supplier:
Prosci
Description:
S1P1 Antibody: Movement of lymphocytes through lymphoid organs is required for generating immunity. Their migration into lymph nodes follows a series of events including integrin activation through chemokine signaling, adhesion and diapedis. The release of lymphocytes from lymph nodes is regulated by the phospholipid sphingosine-1-phosphate (S1P). One of its receptors S1P1 binds S1P with high specificity and affinity; agonism of this receptor by the immunosuppressive agent FTY720 inhibits the entry of tissue T cells into afferent lymphatics in homeostatic and inflammatory conditions. Recent experiments have indicated that CCR7-deficient T cells left lymph nodes more rapidly than wild-type cells did and these cells where also less effectively retained after treatment with FTY720, and that egress competence could be restored by inactivating G alpha i-protein-coupled receptor signaling. These results suggest that S1P1 acts in the lymphocyte to promote lymph node egress by overcoming retention signals mediated by CCR7 and G alpha i-protein-coupled receptor signaling.
Catalog Number:
(76119-588)
Supplier:
Bioss
Description:
Deoxyribonuclease I gene is approximately 3.2 kb long with 9 exons separated by 8 introns. In the form of a bovine pancreatic enzyme preparation, it occupies an important place in the history of protein chemistry and enzymology: it was the first enzyme to be recognized as specific for DNA; it was the first DNase to be crystallized; and it was the first DNase for which a specific protein inhibitor was characterized. DNase I is a Ca2+ and Mg2+ dependant endonuclease. DNase I is synthesized in the pancreas and stored in zymogen granules. It has been used to reduce the viscosity of cystic fibrosis sputum. A DNase I-like enzyme appears to catalyze the degradation of chromatin to oligo- and mononucleosomes during apoptosis. A recent study has demonstrated an endonuclease with activity and antigenicity indistinguishable from DNase I in thymocytes, cells susceptible to apoptosis. DNase I is an endonuclease that hydrolyzes double-stranded or single stranded DNA preferentially at sites adjacent to pyrimidine nucleotides. The product of hydrolysis is a complex mixture of 5'-phosphate mononucleotides and oligonucleotides. In the presence of Mg ion, DNase I attacks each strand of DNA independently and the cleavage sites are random.
Catalog Number:
(10466-602)
Supplier:
Bioss
Description:
Deoxyribonuclease I gene is approximately 3.2 kb long with 9 exons separated by 8 introns. In the form of a bovine pancreatic enzyme preparation, it occupies an important place in the history of protein chemistry and enzymology: it was the first enzyme to be recognized as specific for DNA; it was the first DNase to be crystallized; and it was the first DNase for which a specific protein inhibitor was characterized. DNase I is a Ca2+ and Mg2+ dependant endonuclease. DNase I is synthesized in the pancreas and stored in zymogen granules. It has been used to reduce the viscosity of cystic fibrosis sputum. A DNase I-like enzyme appears to catalyze the degradation of chromatin to oligo- and mononucleosomes during apoptosis. A recent study has demonstrated an endonuclease with activity and antigenicity indistinguishable from DNase I in thymocytes, cells susceptible to apoptosis. DNase I is an endonuclease that hydrolyzes double-stranded or single stranded DNA preferentially at sites adjacent to pyrimidine nucleotides. The product of hydrolysis is a complex mixture of 5'-phosphate mononucleotides and oligonucleotides. In the presence of Mg ion, DNase I attacks each strand of DNA independently and the cleavage sites are random.
Catalog Number:
(10771-688)
Supplier:
PeproTech, Inc.
Description:
The IGFs are mitogenic, polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone, and cartilage tissue in vitro . IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar to insulin by structure and function, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant Human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids, respectively, and 3 intra-molecular disulfide bonds. The calculated molecular weight of Recombinant Human IGF-I is 7.6 kDa.
Supplier:
PeproTech, Inc.
Description:
The IGFs are mitogenic, polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone, and cartilage tissue in vitro . IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar to insulin by structure and function, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant Murine IGF-I is a 7.6 kDa globular protein containing amino acids including 3 intra-molecular disulfide bonds.
Inquire for Price
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
 is still displayed and you need assistance, please call us at 1-800-932-5000.
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
is still displayed and you need assistance, please call us at 1-800-932-5000.
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 Regulatory_Affairs@vwr.com
-Additional Documentation May be needed to purchase this item. A VWR representative will contact you if needed.
This product has been blocked by your organization. Please contact your purchasing department for more information.
The original product is no longer available. The replacement shown is available.
This product is no longer available. Alternatives may be available by searching with the VWR Catalog Number listed above. If you need further assistance, please call VWR Customer Service at 1-800-932-5000.
|
|||||||||
List View
