25957 Results for: "2,5-Dichloro-4-pyridineboronic acid"

Supplier: TCI America

CAS Number: 51857-17-1
MDL Number: MFCD00671489
Molecular Formula: C11H24N2O2
Molecular Weight: 216.33
Purity/Analysis Method: >97.0% (GC,T)
Form: Clear Liquid
Flash Point (°C): 125
Specific Gravity (20/20): 0.96

Supplier: TCI America

CAS Number: 10465-81-3
MDL Number: MFCD00010111
Molecular Formula: C12H20N4O2
Molecular Weight: 252.32
Purity/Analysis Method: >98.0% (N)
Form: Crystal
Melting point (°C): 136

Supplier: TCI America

CAS Number: 431-47-0
MDL Number: MFCD00000417
Molecular Formula: C3H3F3O2
Molecular Weight: 128.05
Purity/Analysis Method: >98.0% (GC)
Form: Clear Liquid
Color: Colorless
Boiling point (°C): 43
Melting point (°C): -78
Flash Point (°C): -20
Specific Gravity (20/20): 1.29

Supplier: Labconco

Specifically designed to rapidly concentrate multiple small heat-sensitive samples using centrifugal force, vacuum, and controlled temperature

Supplier: ANTIBODIES.COM LLC

Human SLC25A20 ELISA kit is a sandwich Enzyme-Linked Immunosorbent Assay (sELISA) designed for the in vitro quantitative determination of human SLC25A20 in serum, plasma, tissue homogenates, and other biological fluids.

Supplier: ANTIBODIES.COM LLC

Human TPPP ELISA kit is a sandwich Enzyme-Linked Immunosorbent Assay (sELISA) designed for the in vitro quantitative determination of human TPPP in serum, plasma, tissue homogenates, and other biological fluids.

Supplier: Bioss

GEFT is a 580 amino acid cytoplasmic protein that is highly expressed in excitable tissues such as brain, heart and muscle, and weakly expressed in small intestine, colon, liver, placenta and lung. GEFT may play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. GEFT works as a guanine nucleotide exchange factor for the Rho family of small GTPases and links specifically to G alpha q/11-coupled receptors in Rho A activation. GEFT is an important regulator of processes involved in axon and dendrite formation. Involved in skeletal myogenesis, GEFT seems to be an exchange factor primarily for Rac 1 in neurons. Existing as two alternatively spliced variants, GEFT contains a DH (DBL-homology) domain and a PH domain.

Supplier: Bioss

The claudin superfamily consists of structurally related proteins that are important structural and functional components of tight junctions. Claudin-23, also known as CLDN23 or CLDNL, is a 292 amino acid multi-pass membrane protein that localizes to cell junctions and belongs to the claudin family. Expressed in stomach and placenta, as well as in germinal center B-cells, claudin-23 is thought to exhibit calcium-dependent cell-adhesion activity through which it plays an essential role in tight junction-specific obliteration of the intercellular space. Human claudin-23 shares 80% sequence similarity with its mouse counterpart, suggesting a conserved role between species. Overexpression of claudin-23 is associated with colon tumors, implicating claudin-23 as a possible metastasis factor.

Supplier: Peprotech

LIF is a pleiotrophic factor produced by multiple cell types, including T cells, myelomonocytic lineages, fibroblasts, liver, heart and melanoma. LIF promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Other activities include the stimulation of acute phase protein synthesis by hepatocytes, stimulation of differentiation of cholinergic nerves, and suppression of adipogenesis by inhibiting the lipoprotein lipase in adipocytes. While human LIF is active on mouse cells and is widely used in the maintenance of murine ESC to prevent spontaneous differentiation, mouse LIF is not active on human cells due to its inability to bind to the human LIF receptor. Recombinant Murine LIF is a 19.9 kDa protein containing 180 amino acids residues, including three disulfide bonds.

Supplier: Enzo Life Sciences

The small ubiquitin-related modifier SUMO-1 belongs to the growing family of ubiquitin-related proteins involved in post-translational protein modification. It is present in all eukaryotic kingdoms and is highly conserved from yeast to humans. Whereas invertebrates have only one SUMO gene, three members of the SUMO family have been described in vertebrates, SUMO-1 and the close homologues SUMO-2 and SUMO-3 with some 50% homology between SUMO-1 and SUMO-2/3. The SUMO family members have a short N-terminal extension that is absent in ubiquitin, and the function of which is unknown and the sequence of which varies between the three family members.  Unlike ubiquitin, SUMO-1 does not appear to target proteins for degradation but seems to be involved in the modulation of protein-protein interactions. Although having only 18% amino acid sequence identity with ubiquitin, the overall structure closely resembles that of ubiquitin. Whereas the two C-terminal glycine residues required for isopeptide bond formation are conserved between the two molecules, Lys48 found in ubiquitin, and required to generate ubiquitin polymers, is substituted by Gln69in SUMO-1 thereby providing an explanation of why SUMO-1 has not been observed to form polymers.  An increasing number of SUMO-1 substrates are being described but three major substrates for SUMO-1 modification are RanGAP1, PML and IκBα proteins. 

Supplier: MP Biomedicals

Diethyl Pyrocarbonate (DEPC) is a chemical used to inactivate RNase enzymes and is sensitive to moisture and pH. DEPC is also sensitive to ammonia, which causes decomposition to urethane, a possible carcinogen.
DEPC is effective as a nuclease inhibitor. Modification reagent for His and Tyr residues in proteins. Robust probe for structural disruptions in dsDNA, reacting with fully or partially unstacked bases. Diethyl Pyrocarbonate is used to modify proteins and nucleic acids.
Modification reagent for His and Tyr residues in proteins. Robust probe for structural disruptions in dsDNA, reacting with fully or partially unstacked bases. Diethyl pyrocarbonate has been used in PCR reaction for treating deionized water, which reduces the risk of RNA being degraded by RNases. It is also used for Dot blot hybridization, to dilute total RNA isolated from different micro-organisms.
Inactivates RNase in solution at about 0.1% (v/v), thus protecting RNA against degradation. It inhibits the ryanodine binding to ryanodine/Ca2+ receptor channels in skeletal muscle in a dose and time dependent manner and increases the Ca2+ permeability of SR vesicles.

Supplier: Genetex

Nucleolin, which is identical to human DNA helicase IV, is a major nucleolar phosphoprotein which is associated with preribosomal RNA and is implicated in the early stage of preribosomal RNP assembly and processing. This 100 kDa protein has three major domains: a N-terminal domain comprised of long acidic stretches interspersed with basic repeats, similar to the structure of a high mobility group-type protein (this domain is responsible for the ablility of nucleolin to modulate chromatin condensation), a central domain that contains four RNA binding elements, a C-terminal domain approximately 85 amino acids long that is rich in glycine, arginine, and phenylalanine residues. Nucleolin fluctuates in parallel to DNA synthesis; intact 100 kDa protein is the major species in actively dividing cells, whereas the degraded forms are relativley abundant in nondividing cells. Nucleolin can unwind RNA-RNA duplexes, as well as DNA-DNA and DNA-RNA duplexes. Nucleolin also interacts directly with DNA topoisomerase I. It is located mainly in dense fibrillar regions of the nucleolus. Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and preribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. It interacts with APTX and contains 4 RNA recognition motif (RRM) domains.

Supplier: Prosci

Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. The ribosomal protein is a component of the 60S subunit. The protein, which is the functional equivalent of the E. coli L10 ribosomal protein, belongs to the L10P family of ribosomal proteins. It is a neutral phosphoprotein with a C-terminal end that is nearly identical to the C-terminal ends of the acidic ribosomal phosphoproteins P1 and P2. The P0 protein can interact with P1 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 60S subunit. The protein, which is the functional equivalent of the E. coli L10 ribosomal protein, belongs to the L10P family of ribosomal proteins. It is a neutral phosphoprotein with a C-terminal end that is nearly identical to the C-terminal ends of the acidic ribosomal phosphoproteins P1 and P2. The P0 protein can interact with P1 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. Transcript variants derived from alternative splicing exist; they encode the same protein. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.

Supplier: Peprotech

KLF4 is a member of the Kruppel-like factor (KLF) family of zinc finger transcription factors. Members of this family share 3 contiguous C2H2-type zinc fingers at the carboxyl terminus that comprise the DNA-binding domain. KLF4 is highly expressed in skin and gut epithelial tissues, but is also found in various other cells and tissues, including vascular endothelial cells, lymphocytes, lung, and testis. It is an important regulator of the cell cycle, transcription, and cell differentiation. Together with Sox2, Oct4, and cMyc, KLF4 can induce the reprogramming of primary human fibroblasts to a pluripotent state. KLF4 and other transcription factors can be introduced into cells by DNA transfection, viral infection, or microinjection. Protein transduction using TAT fusion proteins represents an alternative methodology for introducing transcription factors into primary, as well as transformed, cells. Recombinant Human KLF4-TAT is a 483 amino acid protein, including a 13-residue C-terminal TAT peptide, with a calculated molecular weight of 51.7 kDa. PeproTech’s Recombinant Human KLF4-TAT is a mixture of the expected sequence beginning at Met1 and a truncated isoform beginning at Tyr54. Due to post-translational modifications, SDS-PAGE gel shows bands at approximately 72 and 66kDa, under reduced conditions.

Supplier: Prosci

FBXO25 is a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein belongs to the Fbxs class. Three alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class. Three alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

Supplier: Quantabio

Faster, better, tougher next generation cDNA SuperMix for cDNA synthesis.

Supplier: Enzo Life Sciences

P62, also known as Sequestosome I, is a 62kDa, 440 amino acid protein, initially identified as a ligand of the SH2 domain of p56lck, now known to be expressed in many tissues. In addition to TRAF6, PEST and zinc finger motifs, p62 has a C-terminal ubiquitin binding association (UBA) domain with an affinity for multi-ubiquitin chains, and it is considered to serve as a scaffold protein, capable of binding to multiple signalling molecules and uniting receptor-mediated signalling events with ubiquitinylation. Elevated levels of p62 have been reported in breast tumours and in alcoholic liver disease where p62 has been shown to be involved in the formation of Mallory bodies. Several mutations in the p62 UBA domain have been identified and the etiology of Paget’s disease of bone has been linked to one such mutation. Kuusisto and colleagues have demonstrated that p62 is also present in elevated levels in the hallmark inclusions found in various neurodegenerative conditions, including tauopathies (Alzheimer’s disease, Picks disease, and frontotemporal dementia) and synucleinopathies (Parkinson’s disease, dementia with Lewy body disease and multiple system atrophy). In recent years ubiquitin immunostaining has been used to provide adjunct information for neuropathological diagnosis, but it is becoming evident that p62 may be an even more reliable marker of neurodegenerative disease inclusion detection than tau, alpha-synuclein or ubiquitin immunostaining.

Supplier: Labconco

Self-contained ductless enclosures allow safe handling of organic, formaldehyde, acid gas, sulfur compounds, or ammonia chemical fumes and vapors.

Supplier: Genetex

Tau proteins are microtubule-associated proteins that are abundant in neurons in the central nervous system and are less common elsewhere. They were discovered in 1975 in Marc Kirschner's laboratory at Princeton University. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene. Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization. Hyperphosphorylation of the tau protein (tau inclusions), however, can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies. Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are mostly found in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is not present in dendrites and is active primarily in the distal portions of axons where it provides microtubule stabilization but also flexibility as needed. This contrasts with STOP proteins in the proximal portions of axons which essentially lock down the microtubules and MAP2 that stabilizes microtubules in dendrites. The tau gene locates on chromosome 17q21, containing 16 exons. The major tau protein in the human brain is encoded by 11 exons. Exon 2, 3 and 10 are alternative spliced, allowing six combinations (2-3-10-; 2+3-10-; 2+3+10-; 2-3-10+; 2+3-10+; 2+3+10+). Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They differ in either no, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-regions at the C-terminal part exon 10 missing. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments from Alzheimer's Disease brain. In other neurodegenerative diseases, the deposition of aggregates enriched in certain tau isoforms has been reported. When misfolded this otherwise very soluble protein can form extremely insoluble aggregates that contribute to a number of neurodegenerative diseases.

Supplier: FUJIFILM IRVINE SCIENTIFIC, INC

Interleukin 17F (IL-17F), a member of the IL-17 cytokine family, is secreted by activated CD4+ T cells and monocytes. IL-17F binds the IL-17 receptor related molecule, IL17RC, to promote the production of the interleukin 6 (IL-6), interleukin 8 (IL-8), and granulocyte macrophage colony-stimulating factor (GM-CSF) cytokines. IL-17F also functions to regulate matrix turnover rates, inhibit endothelial cell angiogenesis, and induce the endothelial cell expression of interleukin 2 (IL-2), monocyte chemoattractant protein-1 (MCP-1), and transforming growth factor beta 1 (TGF-β1).

Supplier: MP Biomedicals

Chlortetracycline hydrochloride has antimicrobial action similar to tetracycline hydrochloride, but it is somewhat less active against many Gram-negative organisms. It was first isolated from the culture of Streptomyces aureofacien.

Supplier: MP Biomedicals

Cesium chloride, an inorganic compound, is an important source of cesium ions in a variety of applications. Its crystal structure forms a major structural type where each cesium ion is coordinated by 8 chlorine ions. Cesium chloride occurs naturally in mineral waters and as an impurity in carnallite (up to 0.002%), sylvite and kainite. Less than 20 tonnes of CsCl is produced annually worldwide, mostly from a cesium-bearing mineral pollucite.

Supplier: Genetex

Tau proteins are microtubule-associated proteins that are abundant in neurons in the central nervous system and are less common elsewhere. They were discovered in 1975 in Marc Kirschner's laboratory at Princeton University. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene. Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization. Hyperphosphorylation of the tau protein (tau inclusions), however, can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies. Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are mostly found in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is not present in dendrites and is active primarily in the distal portions of axons where it provides microtubule stabilization but also flexibility as needed. This contrasts with STOP proteins in the proximal portions of axons which essentially lock down the microtubules and MAP2 that stabilizes microtubules in dendrites. The tau gene locates on chromosome 17q21, containing 16 exons. The major tau protein in the human brain is encoded by 11 exons. Exon 2, 3 and 10 are alternative spliced, allowing six combinations (2-3-10-; 2+3-10-; 2+3+10-; 2-3-10+; 2+3-10+; 2+3+10+). Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They differ in either no, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-regions at the C-terminal part exon 10 missing. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments from Alzheimer's Disease brain. In other neurodegenerative diseases, the deposition of aggregates enriched in certain tau isoforms has been reported. When misfolded this otherwise very soluble protein can form extremely insoluble aggregates that contribute to a number of neurodegenerative diseases.

Supplier: TCI America

CAS Number: 333338-18-4
MDL Number: MFCD00066288
Molecular Formula: C6H6NO6P
Molecular Weight: 263.05
Purity/Analysis Method: >98.0% (HPLC,T)
Form: Crystal
Storage Temperature: 0-10°C

Supplier: Genetex

Tau proteins are microtubule-associated proteins that are abundant in neurons in the central nervous system and are less common elsewhere. They were discovered in 1975 in Marc Kirschner's laboratory at Princeton University. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene. Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization. Hyperphosphorylation of the tau protein (tau inclusions), however, can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies. Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are mostly found in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is not present in dendrites and is active primarily in the distal portions of axons where it provides microtubule stabilization but also flexibility as needed. This contrasts with STOP proteins in the proximal portions of axons which essentially lock down the microtubules and MAP2 that stabilizes microtubules in dendrites. The tau gene locates on chromosome 17q21, containing 16 exons. The major tau protein in the human brain is encoded by 11 exons. Exon 2, 3 and 10 are alternative spliced, allowing six combinations (2-3-10-; 2+3-10-; 2+3+10-; 2-3-10+; 2+3-10+; 2+3+10+). Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They differ in either no, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-regions at the C-terminal part exon 10 missing. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments from Alzheimer's Disease brain. In other neurodegenerative diseases, the deposition of aggregates enriched in certain tau isoforms has been reported. When misfolded this otherwise very soluble protein can form extremely insoluble aggregates that contribute to a number of neurodegenerative diseases.

Supplier: Invitrogen

Thermo Scientific RBS Solid is a low-foaming, surface-active powdered detergent formulated for use in automatic laboratory dishwashing machines.

Supplier: BioVendor

CRF serves as a potential neurochemical marker of early dementia and possible early AD.

Supplier: CLOUD-CLONE CORP MS

This assay has high sensitivity and excellent specificity for detecting Mouse FSTL3 (Follistatin Like Protein 3). The assay range is from 15.6 to 1000 pg/ml (Sandwich kit) with a sensitivity of 6.4 pg/ml. There is no detectable cross-reactivity with other relevant proteins. Activity loss rate and accelerated stability test ect have been conducted to guarantee the best performance of the products after long storage and delivery.

Supplier: Peprotech

TIGAR is a p53-inducible enzyme that catalyzes the hydrolysis of fructose-2-6 bisphosphate (F-2-6-BP) to fructose-6-phosphate and inorganic phosphate. F-2-6-BP is a powerful activator of 6-phosphofructose-1 kinase, the rate limiting enzyme of glycolysis. By lowering the intracellular level of F-2-6-BP, TIGAR expression leads to increased glucose processing via the pentose phosphate pathway, the major cellular source for NADPH. Protein transduction using TAT fusion proteins represents an alternative methodology for introducing transcription factors and other intracellular proteins into primary, as well as transformed, cells. Recombinant Human TIGAR-TAT expressed in

Supplier: TCI America

CAS Number: 113-98-4
MDL Number: MFCD00036193
Molecular Formula: C16H18N2O4S
Molecular Weight: 372.48
Purity/Analysis Method: >98.0% (HPLC,N)
Form: Crystal
Color: White
Melting point (°C): 217
Specific rotation [a]20/D: 294 deg (C=1, H2O)