13200 Results for: "Sodium-tert-pentoxide"

Supplier: Prosci

Progesterone receptors (PRs) are nuclear hormone receptors of the NR3C class, which also includes mineralocorticoid, glucocorticoid and androgen receptors. They exist as homodimers coupled to Hsp90 or HMGB proteins, which are shed upon activation. The major signaling pathway used by progesterone receptors is via direct DNA binding and transcriptional regulation of target genes. They can also signal by binding to other proteins, mainly with transcription factors such as NF-κB, AP-1 or STAT. Progesterone receptors are found in the female reproductive tract, mammary glands, brain and pituitary gland and receptor expression is induced by estrogen. Well established functions of progesterone receptors include ovulation, implantation, mammary gland development and maintenance of pregnancy. In addition, progesterone, signaling through the progesterone receptor, increases the ventilatory response of the respiratory centers to carbon dioxide and decreases arterial and alveolar PCO2 in the luteal phase of the menstrual cycle and during pregnancy. The human gene encoding the progesterone receptor has been localized to 11q22.

Supplier: Prosci

Gli-2 (also known as Zinc Finger Protein Gli-2, GLI-Kruppel family member GLI-2 or Tax helper protein) belongs to the C2H2-type zinc finger protein subclass of the Gli family. Members of this subclass are characterized as transcription factors that bind DNA through zinc finger motifs. These motifs contain conserved H-C links. Gli family zinc finger proteins are mediators of Sonic hedgehog (Shh) signaling, and they are implicated as potent oncogenes in the embryonal carcinoma cell. The protein encoded by this gene localizes to the cytoplasm and activates patched Drosophila homolog (PTCH) gene expression. Gli-2 is also thought to play a role during embryogenesis. The encoded protein is associated with several phenotypes: Greig cephalopolysyndactyly syndrome, Pallister-Hall syndrome, pre-axial polydactyly type IV, post-axial polydactyly types A1 and B. Expression has been reported for this mRNA in human testis, myometrium, kidney, lung, glioblastomas, and embryonal cell carcinomas. Multiple splice variants have been reported for this protein.

Supplier: Prosci

Rb operates in the midst of the cell cycle clock apparatus. Its main role is to act as a signal transducer connecting the cell cycle clock with the transcriptional machinery. It plays an important role in the Rb/ E2F pathway in cell proliferation, cell fate determination, and cancer. Cellular senescence is a stable form of cell cycle arrest that limits proliferation of damaged cells and act as a natural barrier to cancer progression. A distinct heterochromatic structure that accumulates in senescent human fibroblasts, designated as SAHF (Senescence-Associated Heterochromatic Foci). SAHF formation coincides with recruitment of heterochromatin proteins and the Rb protein to E2F-responsive promoters and is associated with the stable repression of E2F target genes. Both SAHF formation and the silencing of E2F target genes depended on the integrity of the Rb pathway and do not occur in reversibly arrested cells. Rb activates transcription of the c-Jun gene through the SP1-binding site within the c-Jun promoter

Supplier: SPEX CERTIPREP LLC

Contract Laboratory Program (CLP) standards allow you to Calibrate with Confidence®. The standards are to be used in conjunction with the Statement of Work for Inorganic Analysis; Multi-Media/Multi-Concentration Document Number ILM 05.3/ISM 01.2.

Supplier: Cytiva

rProtein A Sepharose™ 4 Fast Flow is a well established antibody affinity medium is designed for the purification of monoclonal and polyclonal antibodies based on Sepharose™ Fast Flow platform. The recombinant protein A is produced in E.coli and engineered for an oriented coupling to giving a matrix with enhanced binding capacity. The epoxy-based coupling ensures low ligand leakage. The specificity of the recombinant protein A for the Fc region of IgG is similar to native protein A and provides excellent purification in one step. The high capacity, low ligand leakage and a well established base matrix makes rProtein A Sepharose™ Fast Flow ideal for purification of monoclonal antibodies at both laboratory and process scale.

Supplier: Prosci

p53 is a nuclear protein which plays an essential role in the regulation of cell cycle specifically in the transition from G0 to G1. It is found in very low levels in normal cells however in a variety of transformed cell lines in high amounts and believed to contribute to transformation and malignancy. The open reading frame of p53 is 393 amino acids long, with the central region (consisting of amino acids from about 100 to 300) containing the DNA-binding domain. This proteolysis-resistant core is flanked by a C-terminal end mediating oligomerization and an N-terminal end containing a strong transcription activation signal. p53 binds as a tetramer to a PBS (p53-Binding Site) and activates the expression of downstream genes that inhibit growth and/or invasion. p53 binds as a tetramer to a p53-binding site (PBS) and to activate the expression of adjacent genes that inhibit growth and/or invasion. Deletion of one or both p53 alleles reduces the expression of tetramers, resulting in decreased expression of the growth inhibitory genes

Supplier: Prosci

Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger.

Supplier: Prosci

Pathogen-recognition receptor expressed on the surface of immature dendritic cells (DCs) and involved in initiation of primary immune response. Thought to mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. The receptor returns to the cell membrane surface and the pathogen-derived antigens are presented to resting T-cells via MHC class II proteins to initiate the adaptive immune response. Probably recognizes in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens, including HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, cytomegalovirus gB, HCV E2, dengue virus gE, Leishmania pifanoi LPG, Lewis-x antigen in Helicobacter pylori LPS, mannose in Klebsiella pneumonae LPS, di-mannose and tri-mannose in Mycobacterium tuberculosis ManLAM and Lewis-x antigen in Schistosoma mansoni SEA. On DCs it is a high affinity receptor for ICAM2 and ICAM3 by binding to mannose-like carbohydrates. May act as a DC rolling receptor that mediates transendothelial migration of DC presursors from blood to tissues by binding endothelial ICAM2. Seems to regulate DC-induced T-cell proliferation by binding to ICAM3 on T-cells in the immunological synapse formed between DC and T-cells.

Supplier: Prosci

Calcium-activated and phospholipid-dependent serine/threonine-protein kinase involved in various processes such as regulation of the B-cell receptor (BCR) signalosome, apoptosis and transcription regulation. Plays a key role in B-cell activation and function by regulating BCR-induced NF-κ-B activation and B-cell suvival. Required for recruitment and activation of the IKK kinase to lipid rafts and mediates phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652', leading to activate the NF-κ-B signaling. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. Also involved in triglyceride homeostasis. Serves as the receptor for phorbol esters, a class of tumor promoters.

Supplier: Prosci

General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI3K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase. /General protein kinase capable of phosphorylating several known proteins. /IGF-1 leads to the activation of AKT3, which may play a role in regulating cell survival. Capable of phosphorylating several known proteins. Truncated isoform 2/PKB gamma 1 without the second serine phosphorylation site could still be stimulated but to a lesser extent.

Supplier: Prosci

Essential proto-oncogenic transcriptional regulator necessary for development and differentiation of erythroid and megakaryocytic lineages. Transcriptional repressor or activator depending on both promoter and cell type context; represses promoter activity of SOCS1 and SOCS3 and thus, may regulate cytokine signaling pathways. Cooperates with GATA1 to repress target gene transcription, such as the apoptosis regulator BCL2L1; GFI1B silencing in leukemic cell lines markedly increase apoptosis rate. Inhibits down-regulation of MYC and MYB as well as the cyclin-dependent kinase inhibitor CDKN1A/P21WAF1 in IL6-treated myelomonocytic cells. Represses expression of GATA3 in T-cell lymphomas and inhibits GATA1-mediated transcription; as GATA1 also mediates erythroid GFI1B transcription, both GATA1 and GFI1B participate in a feedback regulatory pathway controlling the expression of GFI1B gene in erythroid cells. Suppresses GATA1-mediated stimulation of GFI1B promoter through protein interaction. Binds to gamma-satellite DNA and to its own promoter, auto-repressing its own expression. Alters histone methylation by recruiting histone methyltransferase to target genes promoters. Plays a role in heterochromatin formation.

Supplier: Thermo Scientific

Thermo Scientific Pierce SMCC is a hetero-bifunctional crosslinker that contain N-hydroxysuccinimide (NHS) ester and maleimide groups that allow covalent conjugation of amine- and sulfhydryl-containing molecules. NHS esters react with primary amines at pH 7–9 to form amide bonds, while maleimides react with sulfhydryl groups at pH 6.5–7.5 to form stable thioether bonds. In aqueous solutions, NHS ester hydrolytic degradation is a competing reaction whose rate increases with pH. The maleimide group is more stable than the NHS-ester group, but will slowly hydrolyze and lose its reaction specificity for sulfhydryls at pH values > 7.5. For these reasons, conjugations with these crosslinkers are usually performed at pH 7.2–7.5, with the NHS ester (amine-targeted) reacted before or simultaneous with the maleimide (sulfhydryl-targeted) reaction.

Supplier: Genetex

Histone proteins H3, H4, H2A, and H2B function as building blocks to package eukaryotic DNA into repeating nucleosome units that are folded in higher order chromatin fibers. The nucleosome is composed of an octamer containing a H3/H4 tetramer and two H2A/H2B dimers, surrounded by approximately 146 base pairs of DNA. A diverse and elaborate array of post-translational modifications including acetylation, phosphorylation, methylation, ubiquitination, and ADP-ribosylation occurs on the N-terminal tail domains of histones. Acetylation of lysine residues within these N-terminal domains by histone acetyl-transferases (HATs), including Gcn5p, P/CAF, p300/CBP, and TAFII250, is associated with transcriptional activation. This modification results in remodeling of the nucleosome structure into an open conformation more accessible to transcription complexes. Conversely, histone deacetylation by histone deacetylases (HDACs) is associated with transcription repression reversing the chromatin remodeling process. In most species, histone H3 is primarily acetylated at lysine 9, 14, 18, and 23. Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms.

Supplier: Prosci

FANCA (also called Protein FACA or Fanconi anemia group A protein) is involved in DNA repair, perhaps specifically with post-replication repair or a cell cycle checkpoint function. FANCA may also be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. The Fanconi anemia complementation group (FANC) currently includes FANCA, FANCB, FANCC, FANCD1 (also called BRCA2), FANCD2, FANCE, FANCF, FANCG, and FANCL. The previously defined group FANCH is the same as FANCA. Fanconi anemia is a genetically heterogeneous recessive disorder characterized by cytogenetic instability, hypersensitivity to DNA crosslinking agents, increased chromosomal breakage, and defective DNA repair. The members of the Fanconi anemia complementation group do not share sequence similarity; they are related by their assembly into a common nuclear protein complex. This gene encodes the protein for complementation group A. Alternative splicing results in multiple transcript variants encoding different isoforms. Variant 1 (isoform a) encodes the longest transcript. Variant 2 (isoform b) contains an alternate exon, which results in an early stop codon, compared to variant 1. Isoform b has a shorter C-terminus when compared to isoform a. Mutations in this gene are the most common cause of Fanconi anemia.

Supplier: Prosci

Tyrosine kinase that plays an essential role for the selection and maturation of developing T-cell in the thymus and in mature T-cell function. Is constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors and plays a key role in T-cell antigen receptor(TCR)-linked signal transduction pathways. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, and thereby recruits the associated LCK to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosines residues within the immunoreceptor tyrosines-based activation motifs (ITAMs) in the cytoplasmic tails of the TCRgamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. In addition, contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, and upon engagement of the CD2 molecule, LCK undergoes hyperphosphorylation and activation. Also plays a role in the IL2 receptor-linked signaling pathway that controls T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR.

Supplier: Prosci

Required for checkpoint mediated cell cycle arrest in response to DNA damage or the presence of unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. Recognizes the substrate consensus sequence [R-X-X-S/T]. Binds to and phosphorylates CDC25A, CDC25B and CDC25C. Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C. Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis of CDC25A. Inhibition of CDC25 activity leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression. Binds to and phosphorylates RAD51 at 'Thr-309', which may enhance the association of RAD51 with chromatin and promote DNA repair by homologous recombination. Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A. This may affect chromatin assembly during S phase or DNA repair. May also phosphorylate multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and enhances suppression of cellular proliferation.

Supplier: Prosci

In response to DNA damage and replication blocks, cell cycle progression is halted through the control of critical cell cycle regulators. The protein encoded by Chk2 gene is a cell cycle checkpoint regulator and putative tumor suppressor. It contains a forkhead-associated protein interaction domain essential for activation in response to DNA damage and is rapidly phosphorylated in response to replication blocks and DNA damage. When activated, the encoded protein is known to inhibit CDC25C phosphatase, preventing entry into mitosis, and has been shown to stabilize the tumor suppressor protein p53, leading to cell cycle arrest in G1. In addition, this protein interacts with and phosphorylates BRCA1, allowing BRCA1 to restore survival after DNA damage. Mutations in this gene have been linked with Li-Fraumeni syndrome, a highly penetrant familial cancer phenotype usually associated with inherited mutations in TP53. Also, mutations in this gene are thought to confer a predisposition to sarcomas, breast cancer, and brain tumors. This nuclear protein is a member of the CDS1 subfamily of serine/threonine protein kinases. Three transcript variants encoding different isoforms have been found for this gene.

Supplier: Cytiva

MabSelect SuRe™ is composed of a rigid, high-flow agarose matrix and alkali-tolerant rProtein A ligand. The ligand has been engineered to provide greater stability than conventional protein A-based media in the alkaline conditions used in CIP protocols. This enhanced alkali stability improves process economy and product quality.

Supplier: Prosci

MEK6 is a member of MAPKK protein kinase family. By using degenerate oligonucleotide primers from the conserved kinase domains of MKK3 and MKK4 two human cDNAs and 1 murine cDNA encoding closely related proteins of the MKK family were cloned. The two human clones appear to be different isoforms of the same gene generated by differential splicing: the shorter clone was designated MKK6, encodes a 278-amino acid protein, while the longer clone, designated MKK6b, encodes a 334-amino acid protein. MKK6 is about 80% identical to MKK3 and 40% identical to MKK4. 1.7-kb human MKK6 transcript is highly expressed in skeletal muscle, while an MKK6b-specific probe detected mRNA bands of 1.8, 2.4, and 4.5 kb that are enriched in heart, skeletal muscle, pancreas and liver. MKK6 plays an important role in intracellular signaling pathways leading toward activation of the p38 MAP kinase. MEK6 phosphorylates and activates p38 in response to inflammatory cytokines or environmental stress. As an essential component of p38 MAPK mediated signal transduction pathway, this gene is involved in many cellular processes such as stress induced cell cycle arrest, transcription activation and apoptosis.

Supplier: Prosci

A-Raf, B-Raf and c-Raf (Raf-1) are the main effectors recruited by GTP-bound Ras to activate the MEK-MAP kinase pathway. Activation of c-Raf is the best understood and involves phosphorylation at multiple activating sites including Ser338, Tyr341, Thr491, Ser494, Ser497 and Ser499. p21-activated protein kinase (PAK) has been shown to phosphorylate c-Raf at Ser338 and the Src family phosphorylates Tyr341 to induce c-Raf activity (3, 4). Ser338 of c-Raf corresponds to similar sites in A-Raf (Ser299) and B-Raf (Ser445), although this site is constitutively phosphorylated in B-Raf. Inhibitory 14-3-3 binding sites on c-Raf (Ser259 and Ser621) can be phosphorylated by Akt and AMPK, respectively (6, 7). While A-Raf, B-Raf and c-Raf are similar in sequence and function, differential regulation has been observed (8). Of particular interest, B-Raf contains three consensus Akt phosphorylation sites (Ser364, Ser428 and Thr439) and lacks a site equivalent to Tyr341 of c-Raf (8, 9). The B-Raf mutation V600E results in elevated kinase activity and is commonly found in malignant melanoma (10). Six residues of c-Raf (Ser29, Ser43, Ser289, Ser296, Ser301 and Ser642) become hyperphosphorylated in a manner consistent with c-Raf inactivation. The hyperphosphorylation of these six sites is dependent on downstream MEK signaling and renders c-Raf unresponsive to

Supplier: Prosci

Chek1 is a protein kinase that inhibits mitotic entry after DNA damage, required for the DNA damage checkpoint and is strongly similar to murine Chek1. Checkpoint pathways control the order and timing of cell cycle transitions and ensure that critical events, such as DNA replication and chromosome segregation, are completed with high fidelity. The mouse and human proteins share 90% sequence identity through the protein kinase domains. The sequence of the 476-amino acid human Chek1 protein is 29%, 40%, and 44% identical to those of the fission yeast Chek1, C. elegans Chek1, and Drosophila 'grapes' (Grp) proteins, respectively. Chek1 is expressed ubiquitously as an approximately 2.4-kb mRNA, with the most abundant expression in thymus, testis, small intestine, and colon. The protein has altered mobility when isolated from cells treated with ionizing radiation, indicating that Chek1 is modified in response to DNA damage. In vitro, Chek1 directly phosphorylates a regulator of CDC2 tyrosine phosphorylation, CDC25C. In response to DNA damage, Chek1 phosphorylates and inhibits CDC25C, thus preventing activation of the CDC2-Cyclin-B complex and mitotic entry

Supplier: Prosci

General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI3K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase. /General protein kinase capable of phosphorylating several known proteins. IGF-1 leads to the activation of AKT3, which may play a role in regulating cell survival. Capable of phosphorylating several known proteins. Truncated isoform 2/PKB gamma 1 without the second serine phosphorylation site could still be stimulated but to a lesser extent.

Supplier: Prosci

Myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila).Eukaryotic RNA polymerase II mediates the synthesis of mature and functional messenger RNA. This is a multistep process, called the transcription cycle,that includes five stages: preinitiation, promoter, clearance, elongation and termination. Elongation is thought to be a critical stage for the regulation of gene expression. ELL (11-19 lysine-rich leukemia protein, also designated MEN)
functions as an RNA polymerase II elongation factor that increases the rateof transcription by suppressing transient pausing by RNA polymerase II. Also, ELL is thought to regulate cellular proliferation. ELL is abundantly expressed in peripheral blood leukocytes, skeletal muscle, placenta and testis, and has lower expression in spleen, thymus, heart, brain, lung, kidney, liver and ovary.The gene encoding human ELL, which maps to chromosome 19p13.1, is one of several genes which undergo translocation with the MLL gene on chromo-some 11q23 in acute myeloid leukemia. MLL (myeloid/lymphoid leukemia,also designated ALL-1 and HRX) is a 430 kDa protein that regulates embryonal and hematopoietic development.

Supplier: Prosci

Tyrosine kinase that plays an essential role for the selection and maturation of developing T-cell in the thymus and in mature T-cell function. Is constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors and plays a key role in T-cell antigen receptor(TCR)-linked signal transduction pathways. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, and thereby recruits the associated LCK to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosines residues within the immunoreceptor tyrosines-based activation motifs (ITAMs) in the cytoplasmic tails of the TCRgamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. In addition, contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, and upon engagement of the CD2 molecule, LCK undergoes hyperphosphorylation and activation. Also plays a role in the IL2 receptor-linked signaling pathway that controls T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR.

Supplier: Prosci

Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' and activates transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-κ-B. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs.

Supplier: CUBE BIOTECH

Sulfo-DIBMA is an electroneutral modification of existing DIBMAs. It does not interfere with charge-sensitive interactions between proteins and lipids. This innovation opens up a wider range of experimental research in terms of charge-sensitive membrane protein processes like protein-protein and protein-lipid interactions. In addition, Sulfo-DIBMA belongs to a new generation of DIBMA’s which are RAFT polymerized. This achieves a reduction in both monomer size and greater monodispersity. With diisobutylene-maleic acid (DIBMA), you can directly extract membrane proteins from cells without an intermediate step of detergent solubilization, like with SDS, which would usually interfere with the protein's function. Another advantage of DIBMA is the lack of an absorbance maxima at 280 nm. SMAs, in comparison, usually interfere with protein quantification, as aromatic amino acids absorb at the same spectrum.
Another significant advantage of Sulfo polymers compared to other polymers is the wide pH range in which they remain stable. The buffer in which the polymer is supplied has a pH of 7.5, but the polymer itself remains stable between pH 4 and pH 10. The special physicochemical properties of Sulfo-DIBMAs make them ideal for cryo-TEM and other downstream applications.
Good publications to find details about Sulfo-DIBMA and Sulfo-SMA are:
Oluwole et al. (2017)
Glueck et al. (2022)
Janson et al. (2022)
Eggenreich et al. (2023)

Supplier: CUBE BIOTECH

Synthetic copolymers are capable of solubilizing and stabilizing membrane proteins without the need for detergents. They have the unique capacity to extract the membrane protein of interest while maintaining a near-native environment.

Supplier: Prosci

GABA (gamma-aminobutyric acid) is the primary inhibitory neurotransmitter in the central nervous system and interacts with three different receptors: GABA(A), GABA(B) and GABA(C) receptor. The ionotropic GABA(A) and GABA(C) receptors are ligand-gated ion channels that produce fast inhibitory synaptic transmission. In contrast, the metabotropic GABA(B) receptor is coupled to G proteins that modulate slow inhibitory synaptic transmission. Functional GABA(B) receptors form heterodimers of GABA(B)R1 and GABA(B)R2 where GABA(B)R1 binds the ligand and GABA(B)R2 is the primary G protein contact site. Two isoforms of GABA(B)R1 have been cloned: GABA(B)R1a is a 130 kD protein and GABA(B)R1b is a 95 kD protein. G proteins subsequently inhibit adenyl cylase activity and modulate inositol phospholipid hydrolysis. GABA(B) receptors have both pre- and postsynaptic inhibitions: presynaptic GABA(B) receptors inhibit neurotransmitter release through suppression of high threshold calcium channels, while postsynaptic GABA(B) receptors inhibit through coupled activation of inwardly rectifying potassium channels. In addition to synaptic inhibition, GABA(B) receptors may also be involved in hippocampal long-term potentiation, slow wave sleep and muscle relaxation.

Supplier: Prosci

NF-κ-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-κ-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-κ-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-κ-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-κ-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-κ-B complex which translocates to the nucleus. NF-κ-B heterodimeric RelB-p50 and RelB-p52 complexes are transcriptional activators. RELB neither associates with DNA nor with RELA/p65 or REL. Stimulates promoter activity in the presence of NFKB2/p49.

Supplier: Rockland Immunochemical

FGF13(Fibroblast growth factor 13), also called FHF2 is a protein that in humans is encoded by the FGF13 gene.The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. FGF13is a large gene, extending over approximately 200 kb in Xq26.3, and contains at least 7 exons. By cytogenetic, FISH, and database analysis, Gecz et al. (1999) localized the FGF13 gene within a 400-kb duplication interval on chromosome Xq26.3. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth, and invasion. Other areas of interests and use for researchers include cancer, borjeson-forssman-lehmann syndrome, regulation of actin cytoskeleton pathways, apoptosis, GPCR pathways, TGF-Beta pathways, and Rho familty GTPase pathways. This gene is located to a region associated with Borjeson-Forssman-Lehmann syndrome (BFLS), a syndromal X-linked mental retardation, which suggests it may be a candidate gene for familial cases of the BFL syndrome. The function of this gene has not yet been determined. Two alternatively spliced transcripts encoding different isoforms have been described for this gene.