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6-Fluorobenzo[b]thiophene-2-carboxylic+acid
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6-Fluorobenzo[b]thiophene-2-carboxylic+acid
Catalog Number:
(75791-924)
Supplier:
Prosci
Description:
Mannose-binding Lectin (MBL) is an acute phase protein bearing to the family of collectins produced by the liver as a monomer that forms a triple helix. Once released in serum, it further polymerizes forming dimers to octamers. The degree of serum polymerization is critical for the biological activity of MBL. MBL has higher affinity to microbial polysaccharides or their glycoconjugates. MBL was shown earlier to bind cell surfaces of bacteria, fungi, protozoa and viruses and acts as an acute-phase plasma protein (APP) during infection and inflammation. MBL activates the lectin-complement pathway, promotes opsonophagocytosis and modulates inflammation.
Catalog Number:
(10106-970)
Supplier:
Prosci
Description:
Transcription factors containing a basic helix-loop-helix (bHLH) motif regulate expression of tissue-specific genes in a number of mammalian and insect systems. DNA-binding activity of the bHLH proteins is dependent on formation of homo- and/or heterodimers. Dominant-negative HLH proteins encoded by Id-related genes, such as ID4, also contain the HLH-dimerization domain but lack the DNA-binding basic domain. Consequently, Id proteins inhibit binding to DNA and transcriptional transactivation by heterodimerization with bHLH proteins (Pagliuca et al., 1995).
Catalog Number:
(76100-034)
Supplier:
Bioss
Description:
Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome. Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilize XPC. May protect XPC from proteasomal degradation. 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:
(76100-036)
Supplier:
Bioss
Description:
Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome. Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilize XPC. May protect XPC from proteasomal degradation. 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:
(102981-458)
Supplier:
Adipogen
Description:
CD27 (TNFRSF7) is a member of the TNF-receptor superfamily limited to cells of the lymphoid lineage and exists as both a dimeric glycoprotein on the cell surface and as a soluble protein in serum. As a T and B cell co-stimulatory molecule, the activity of CD27 is governed by its TNF-like ligand CD70 on lymphocytes and dendritic cells. The CD27-CD70 interaction is required for Th1 generation responses to differentiation signals and long-term maintenance of T cell immunity, and meanwhile, plays a key role in regulating B cell differentiation, activation and immunoglobulin synthesis. The CD27 receptor transduces signals and subsequently leads to the activation of NF-kappaB and MAPK8/JNK, mediated by the adaptor proteins TRAF2 and TRAF5. In addition, the proapoptotic protein SIVA is capable of binding the cytoplasmic tail of CD27 and exerts action in the process of apoptosis.
Catalog Number:
(10258-596)
Supplier:
Bioss
Description:
This gene encodes a telomere specific protein which is a component of the telomere nucleoprotein complex. This protein is present at telomeres throughout the cell cycle and functions as an inhibitor of telomerase, acting in cis to limit the elongation of individual chromosome ends. The protein structure contains a C-terminal Myb motif, a dimerization domain near its N-terminus and an acidic N-terminus. Two transcripts of this gene are alternatively spliced products. [provided by RefSeq].
Catalog Number:
(10792-760)
Supplier:
Genetex
Description:
Rabbit Polyclonal antibody to PCBD1
Supplier:
PeproTech, Inc.
Description:
β-NGF is a neurotrophic factor structurally related to BDNF, NT-3 and NT-4. These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. β-NGF is a potent neurotrophic factor that signals through its receptor β-NGFR, and plays a crucial role in the development and preservation of the sensory and sympathetic nervous systems. β-NGF also acts as a growth and differentiation factor for B lymphocytes, and enhances B-cell survival. The functional form of Recombinant Human β-NGF is a non-covalently-linked homodimer of two 13.5 kDa, polypeptide monomers that each contain 120 amino acids and three disulfide bonds, which are required for biological activity.
Catalog Number:
(10813-814)
Supplier:
Prosci
Description:
E2A is a transcription factor that plays major roles in determining tissue-specific cell fate during embryogenesis, like muscle or early B-cell differentiation. Heterodimers between E2A and tissue-specific basic helix-loop-helix (bHLH) Dimers bind DNA on E-box motifs: 5'- CANNTG-3'. Binds to the kappa-E2 site in the kappa immunoglobulin gene enhancer. Deletions in E2A have been observed in a subset of pre-B-cell acute lymphoblastic leukemia (B-ALL) cases. Two alternatively spliced human isoforms have been described.
Catalog Number:
(10459-178)
Supplier:
Bioss
Description:
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.Sequence similarities: Belongs to the RuBisCO large chain family. Type I subfamily.Post-translational modifications: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bonds reported in 1RBO may be the result of oxidation during crystallization.
Catalog Number:
(10459-180)
Supplier:
Bioss
Description:
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.Sequence similarities: Belongs to the RuBisCO large chain family. Type I subfamily.Post-translational modifications: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bonds reported in 1RBO may be the result of oxidation during crystallization.
Catalog Number:
(10451-044)
Supplier:
Bioss
Description:
This gene encodes a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. These proteins are synthesized as prepropeptides, cleaved, and then processed into dimeric proteins. This protein may act as an important signaling molecule within the trabecular meshwork and optic nerve head, and may play a potential role in glaucoma pathogenesis. This gene is differentially regulated during the formation of various tumors. [provided by RefSeq, Jul 2008].
Catalog Number:
(10485-820)
Supplier:
Bioss
Description:
RENBP is a 427 amino acid protein that is a proteinaceous renin inhibitor. In inhibiting renin, RENBP forms a complex with it; a high molecular weight renin. RENBP contains a leucine zipper domain, which is essential for its dimerization with renin. RENBP can catalyze the interconversion of N-acetylglucosamine to N-acetylmannosamine, indicating that it is a GlcNAc 2-epimerase. Sequences of porcine, human and rat renin-binding proteins are highly homologous. The RENBP gene is conserved in dog, mouse, rat and zebrafish, and maps to human chromosome Xq28 between DXS52 and G6PD. Rat Renbp is located on chromosome X at Xq37 close to marker DXWox3 and falls outside the BP QTL regions on chromosome X.
Catalog Number:
(10104-746)
Supplier:
Prosci
Description:
NFYA is one subunit of a trimeric complex, forming a highly conserved transcription factor that binds to CCAAT motifs in the promoter regions in a variety of genes. Subunit A associates with a tight dimer composed of the B and C subunits, resulting in a trimer that binds to DNA with high specificity and affinity. The sequence specific interactions of the complex are made by the A subunit, suggesting a role as the regulatory subunit. In addition, there is evidence of post-transcriptional regulation in this gene product, either by protein degradation or control of translation. Further regulation is represented by alternative splicing in the glutamine-rich activation domain, with clear tissue-specific preferences for the two isoforms.
Catalog Number:
(10415-444)
Supplier:
Bioss
Description:
MAX protein is a member of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. It is able to form homodimers and heterodimers with other family members, which include Mad, Mxi1 and Myc. Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E box) and rearrangement among these dimer forms provides a complex system of transcriptional regulation. Mutations of this gene have been reported to be associated with hereditary pheochromocytoma. A pseudogene of this gene is located on the long arm of chromosome 7. Alternative splicing results in multiple transcript variants.
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