5787 Results for: "extraction"

Supplier: Rockland Immunochemical

SIRT1 antibody detects human SIRT1 protein. SIRT1 is a member of the sirtuin family of protein-modifying enzymes. SIRT1 is a NAD+-dependent deacetylase that plays an important role in many cellular processes. SIRT1 protein is known to regulate epigenetic gene silencing and suppress recombination of rDNA. SIRT1 deacetylates a wide range of substrates, including p53, NF-kB, FOXO transcription factors, and PGC-1 alpha, with roles in cellular processes such as muscle differentiation, adipogenesis, protection from axonal degeneration, and life span extension. SIRT1 is downregulated in cells that have high insulin resistance and inducing its expression increases insulin sensitivity, suggesting the molecule is associated with improving insulin sensitivity. Furthermore, SIRT1 de-acetylates and affects the activity of both members of the PGC1-alpha/ERR-alpha complex, which are essential metabolic regulatory transcription factors. Anti-SIRT1 Antibody is significant for researchers involved in research areas including cancer, diabetes, aging, neurodegenerative, metabolic and cardiovascular diseases.

Supplier: Rockland Immunochemical

UCHL1 antibody recognizes Ubiquitin C-terminal hydrolase 1 (UCHL1) which is also known as ubiquitin carboxyl esterase L1, ubiquitin thiolesterase, neuron-specific protein PGP9.5 and Park5. It was originally identified as a major component of the neuronal cytoplasm from 2-dimensional gel analysis of brain tissues, and was given the name PGP9.5. It was later found that ubiquitin C-terminal hydrolase enzyme activity was associated with the PGP9.5 protein. The ubiquitin C-terminal hydrolases cleave ubiquitin from other molecules. Regulation of the ubiquitin pathway is very important and many disease states are associated with defects in this pathway. Genetic knockout of UCHL1 in mice results in a motor neuron degeneration similar to the spontaneous gracile axonal dystrophy (gad) mutant mice. Point mutations in the UCHL1 gene are associated with some forms of human Parkinson's disease. Since UCHL1 is heavily expressed in neurons, it is released in large amounts following injury or degeneration, so the detection of UCHL1 in CSF and other bodily fluids can be used as a biomarker.
Therefore, UCHL1 monoclonal antibody is ideal for investigators involved in Neuroscience.

Supplier: Rockland Immunochemical

NLRP3(NLR FAMILY, PYRIN DOMAIN-CONTAINING 3),also known as CIAS1, CRYOPYRIN, NALP3 or PYPAF1, is a protein that in humans is encoded by the NLRP3 (NOD-like receptor family, pryin domain containing 3) gene. The NLRP3 gene encodes a pyrin-like protein expressed predominantly in peripheral blood leukocytes. And the NLRP3 gene is mapped on 1q44. NLRP3 interacts with apoptosis-associated speck-like protein containing a CARD (ASC). The encoded protein may play a role in the regulation of inflammation and apoptosis. Mutation of the NALP3 nucleotide-binding domain reduced ATP binding, CASP1 activation, IL1B production, cell death, macromolecular complex formation, self-association, and association with ASC. Consistent with an essential role for Nlrp3 inflammasomes in antifungal immunity, Gross et al.showed that Nlrp3-deficient mice are hypersusceptible to C. albicans infection. Activation of the NLRP3 inflammasome in response to virus or to RNA was dependent upon lysosomal maturation and reactive oxygen species production in human cells. The NLRP3 inflammasome senses obesity-associated danger signals and contributes to obesity-induced inflammation and insulin resistance. This antibody is suitable for researchers interested in cancer research.

Supplier: Rockland Immunochemical

TP53 (tumor suppressor gene p53) is one of the most well-studied genes that suppresses tumor formation and renders protection against DNA damage by inducing cell cycle arrest, DNA repair, or apoptosis. TP53 signaling is triggered through numerous cellular events ranging from DNA damage to hypoxia, stress and a plethora of other causes. Upon activation, p53 acts as zinc-containing transcriptional regulator and initiates a cascade of events that determines the cellular outcome including cell cycle arrest, apoptosis, senescence, DNA repair, development, differentiation and tissue homeostasis. Cell cycle arrest is induced by p53 via trans-activating genes such as p21 (CDK-inhibitor 1, cyclin dependent kinase) and others. Interestingly, p53 itself is capable of triggering cellular responses (survival or induced cell death) as well. Mutations or deletions in the TP53 gene are present in nearly 50% of human cancers, and primarily results in impaired tumor suppressor function. Anti-p53 (ac Lys305) antibody is ideal for researchers interested in developmental biology, cell growth and cancer research.

Supplier: Rockland Immunochemical

SIRT1 antibody detects human SIRT1 protein. SIRT1 is a member of the sirtuin family of protein-modifying enzymes. SIRT1 is a NAD+-dependent deacetylase that plays an important role in many cellular processes. SIRT1 protein is known to regulate epigenetic gene silencing and suppress recombination of rDNA. SIRT1 deacetylates a wide range of substrates, including p53, NF-kB, FOXO transcription factors, and PGC-1 alpha, with roles in cellular processes such as muscle differentiation, adipogenesis, protection from axonal degeneration, and life span extension. SIRT1 is downregulated in cells that have high insulin resistance and inducing its expression increases insulin sensitivity, suggesting the molecule is associated with improving insulin sensitivity. Furthermore, SIRT1 de-acetylates and affects the activity of both members of the PGC1-alpha/ERR-alpha complex, which are essential metabolic regulatory transcription factors. Anti-SIRT1 Antibody is useful for researcher involved in research areas including cancer, diabetes, aging, neurodegenerative, metabolic or cardiovascular diseases.

Supplier: Rockland Immunochemical

Histone H2A.X (phospho S139) antibody is ideal for western blotting and ELISA. Histones play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA is wrapped around histone-groups, consisting of the core histones H2A, H2B, H3 and H4. As a reaction on DNA Double-strand breaks (DSB) H2AX becomes phosphorylated on serine 139, called gamma-H2AX. ATM, ATR and PRKDCs, kinases of the PI3-family, are responsible for this phosphorylation. The modification can happen accidentally during replication fork collapse, exogenous genotoxic agents, may also occur during meiotic recombination events and immunoglobulin class switching in lymphocytes, in the response to ionizing radiation but also during controlled physiological processes such as V(D)J recombination. Mutagenesis experiments have shown that the modification is necessary for the proper formation of ionizing radiation induced foci in response to double strand breaks, but is not required for the recruitment of proteins to the site of DSBs. Gamma-H2AX is a sensitive target for looking at DSBs in cells. Dephosphorylation of Ser-140 by PP2A is required for DNA DSB repair. The role of the phosphorylated form of the histone in DNA repair is under. Anti-H2AX pS139 is ideal for researched interested in Histones, DNA Damage and Repair, and Epigenetics.

Supplier: Rockland Immunochemical

Anti-Nuclear receptor ROR gamma pS203 was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). Nuclear receptor ROR gamma pS203 antibody detects mouse receptor ROR gamma phosphorylated at the serine 203 position. RAR-related orphan receptor gamma is a member of the nuclear receptor family of transcription factors. (ROR-gamma) is a key regulator of cellular differentiation, immunity, peripheral circadian rhythm as well as lipid, steroid, xenobiotics and glucose metabolism. ROR-gamma regulates the circadian expression of clock genes such as CRY1, ARNTL/BMAL1 and NR1D1 in peripheral tissues and in a tissue-selective manner. It is also involved in the regulation of the rhythmic expression of genes involved in glucose and lipid metabolism and is a negative regulator of adipocyte differentiation. It controls adipogenesis as well as adipocyte size and modulates insulin sensitivity in obesity. Isoform 2, ROR-gamma is essential for lymphoid organogenesis, in particular lymph nodes and Peyer's patches. ROR-gamma also plays an important regulatory role in thymopoiesis, and in inhibiting apoptosis of undifferentiated T cells. Anti-nuclear receptor ROR gamma pS203 is ideal for researcher's interested in autoimmune diseases such as psoriasis and rheumatoid arthritis, circadian rhythms, and immune system disorders.

Supplier: Genetex

The INK4a/ARF locus encodes two unrelated tumor suppressor proteins, p16INK4a and p19ARF that restrain cell growth by modifying the functions of the retinoblastoma protein and p53, respectively. It is among the most frequently mutated tumor suppressor loci in human cancer. Both p16INK4a and p19ARF act as cell proliferation inhibitors. The ARF gene, p19ARF in mouse and p14ARF in human, has become an important player in cell cycle regulation. In mice, tumor suppressor effects appear to be mediated by interactions between p19ARF and the p53 tumor-suppressor protein. p19ARF counters uncontrolled proliferation and oncogenic signals in p53-dependent pathways. Proteins encoded by the INK4a/ARF locus also play a role in Abelson virus transformation. Both p16INK4a and p19ARF are expressed in many cells as they emerge from the apoptotic crisis that characterizes the transformation process. Expression of p19ARF but not p16INK4a induces apoptosis in Ab-MLV-transformed pre-B cells. INK4a/ARF expression correlates with or precedes the emergence of cells expressing mutant p53. p19ARF is an important part in cellular defense against transforming signals from the Abl oncoprotein, providing direct evidence that the p19ARF-p53 regulatory loop plays an important role in lymphoma induction.

Supplier: Rockland Immunochemical

The Anti-Glut2 antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). The glucose transporter GLUT2 is a transmembrane carrier protein that allows protein facilitated glucose movement across cell membranes. GLUT2 is expressed in the plasma membranes of the liver, intestine, renal tubular cells, pancreatic islet beta cells, as well as in the portal and hypothalamic areas. Due to its low affinity and high capacity, GLUT2 transports dietary sugars, glucose, galactose and fructose in high concentrations, displaying large bidirectional fluxes in and out of cells. In pancreatic beta cells, GLUT2 is essential for glucose-stimulated insulin secretion. GLUT2 expression is necessary for the physiological control of glucose-sensitive genes, and its inactivation in the liver leads to impaired glucose-stimulated insulin secretion. In the nervous system, GLUT2-dependent glucose sensing regulates feeding, thermoregulation and pancreatic islet cell mass and function, as well as sympathetic and parasympathetic activities. In humans, inactivating mutations in GLUT2 cause Fanconi–Bickel syndrome, which is characterized by hepatomegaly and kidney disease. Anti-Glut2 is ideal for researchers interested in studying glucose transport mediated by Glut2 protein in the fields of diabetes, obesity, metabolism, and neuroscience research.

Supplier: Biosensis

The Biosensis Mature BDNF/proBDNF Combo RapidTM enzyme-linked immunosorbent assay (ELISA) Kit combines individual, but complementary ELISA kits for the two most important BDNF isoforms: Mature BDNF (BEK-2211) and full-length proBDNF (BEK-2237).

Supplier: Rockland Immunochemical

The Anti-Glut2 antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). The glucose transporter GLUT2 is a transmembrane carrier protein that allows protein facilitated glucose movement across cell membranes. GLUT2 is expressed in the plasma membranes of the liver, intestine, renal tubular cells, pancreatic islet beta cells, as well as in the portal and hypothalamic areas. Due to its low affinity and high capacity, GLUT2 transports dietary sugars, glucose, galactose and fructose in high concentrations, displaying large bidirectional fluxes in and out of cells. In pancreatic beta cells, GLUT2 is essential for glucose-stimulated insulin secretion. GLUT2 expression is necessary for the physiological control of glucose-sensitive genes, and its inactivation in the liver leads to impaired glucose-stimulated insulin secretion. In the nervous system, GLUT2-dependent glucose sensing regulates feeding, thermoregulation and pancreatic islet cell mass and function, as well as sympathetic and parasympathetic activities. In humans, inactivating mutations in GLUT2 cause Fanconi–Bickel syndrome, which is characterized by hepatomegaly and kidney disease. Anti-Glut2 is ideal for researchers interested in studying glucose transport mediated by Glut2 protein in the fields of diabetes, obesity, metabolism, and neuroscience research.

Supplier: Rockland Immunochemical

Anti-Cyclin D3 antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). Cyclin D3 belongs to a highly conserved cyclin family, whose members are the ultimate recipients of oncogenic signals. Cyclin D3 is a key component of the cell cycle progression machinery and induces progression through the G1 phase of the cell cycle. Cyclin D3 is expressed in nearly all proliferating cells, and shows the most broad expression pattern of all three D-type (D1-D3) cyclins. Cyclin D3 is encoded from the 6p21 chromosome region and the protein is predominantly localized in the nucleus. Once induced, cyclin D3 binds and activates its associated cyclin-dependent kinases CDK4 and CDK6. Amplification of the cyclin D3 gene and overexpression of cyclin D3 protein is seen in several human cancers. A large number of human malignancies contain lesions in pathways impacting on cyclin D3. Abnormal expression of Cyclin D3 is believed to be a driving force in several human cancers. A possible role for cyclin D3 in the malignancies of the lymphoid system is suggested by the observations that cyclin D3 gene is rearranged in several neoplastic diseases such as diffuse large B cell lymphomas or multiple myelomas. Anti-Cyclin D3 is ideal for researchers interested in Cancer Research and Immunology research.

Supplier: Rockland Immunochemical

The Anti-Glut2 antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). The glucose transporter GLUT2 is a transmembrane carrier protein that allows protein facilitated glucose movement across cell membranes. GLUT2 is expressed in the plasma membranes of the liver, intestine, renal tubular cells, pancreatic islet beta cells, as well as in the portal and hypothalamic areas. Due to its low affinity and high capacity, GLUT2 transports dietary sugars, glucose, galactose and fructose in high concentrations, displaying large bidirectional fluxes in and out of cells. In pancreatic beta cells, GLUT2 is essential for glucose-stimulated insulin secretion. GLUT2 expression is necessary for the physiological control of glucose-sensitive genes, and its inactivation in the liver leads to impaired glucose-stimulated insulin secretion. In the nervous system, GLUT2-dependent glucose sensing regulates feeding, thermoregulation and pancreatic islet cell mass and function, as well as sympathetic and parasympathetic activities. In humans, inactivating mutations in GLUT2 cause Fanconi–Bickel syndrome, which is characterized by hepatomegaly and kidney disease. Anti-Glut2 is ideal for researchers interested in studying glucose transport mediated by Glut2 protein in the fields of diabetes, obesity, metabolism, and neuroscience research.

Supplier: Rockland Immunochemical

Nitric Oxide Synthase 1(NOS1,neuronal NOS,nNOS1) is a messenger molecule, mediating the effect of endothelium-derived relaxing factor in blood vessels and the cytotoxic actions of macrophages, and playing a part in neuronal communication in the brain. It may be involved in neuronal cell death and damage in neurological illness. nNOS1 localized to the 12q24.2 region of human chromosome 12. It splice variant, expressed in testis, that encodes an NH2-terminal truncated protein of 1098 amino acids. nNOS cDNA clones were shown to contain different 5' terminal exons spliced to a common exon 2. Genomic cloning and sequence analysis demonstrate that the unique exons are positioned within 300 bp of each other but separated from exon 2 by an intron that is at least 20 kb in length. The neuronal isoform of nitric oxide synthase is highly expressed in mammalian skeletal muscle, it suggested a specific role for NOS1 in the local metabolic inhibition of alpha-adrenergic vasoconstriction in active skeletal muscle. The novel gaseous neuromediator nitric oxide is thought to play an important role in development and plasticity. Despite this, gene-knockout mice lacking neuronal (Type I) nitric oxide synthase exhibit relatively normal brain development and behavior. This antibody is suitable for researchers interested in apoptosis research, cell death, and TNF pathways.

Supplier: Rockland Immunochemical

TAF10 (TATA-Box Binding Protein Associated Factor 10) is the protein that coordinates activities for the initiation of transcription by RNA polymerase II required for activities of more than 70 polypeptides. TFIID binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as co-activators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes one of the small subunits of TFIID that is associated with a subset of TFIID complexes. Studies with human and mammalian cells have shown that this subunit is required for transcriptional activation by the estrogen receptor, for progression through the cell cycle, and may also be required for certain cellular differentiation programs. Anti-TAF10 Antibody is useful for researchers interested in Chromatin research, transcription factor activity research, and DNA binding and transcription co-activator activity research.

Supplier: Biosensis

The heat shock proteins were discovered, as the name suggests, since they are heavily upregulated when cells are stressed by temperatures above the normal physiological range. They are expressed in unstressed cells also and have a normal function as chaperones, helping other proteins to fold correctly, and are required in much greater amounts if the cell or tissue is stressed by heat. The increased levels are generated transcriptionally under the influence of a powerful transcription factor, the heat shock factor 1 (HSF1). The different heat shock proteins were originally named based on their SDS-PAGE mobility, so HSP27 has an apparent molecular weight of 27kDa. It is an abundant protein even under non-stress conditions and frequently shows up as a major spot on 2 dimensional gels of cells or tissues. It is known to associate with a variety of other proteins such as actin, intermediate filament subunits and ubiquitin and is found both in the cytoplasm and the nucleus of cells. HSP27 can become heavily phosphorylated under the influence of multiple protein kinases particularly as a result of activation of the p38/SAPK pathway. Upregulation of this protein is protective against neurodegenerative diseases at least in certain mouse models (1). Point mutations in the HSP27 gene are associated with two neurological diseases, Charcot-Marie-Tooth disease type 2F and distal hereditary motor neuropathy IIB (2). These diseases are associated with axonal loss apparently following defects in the transport of neurofilaments.

Supplier: Rockland Immunochemical

Anti-Cyclin D3 antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). Cyclin D3 belongs to a highly conserved cyclin family, whose members are the ultimate recipients of oncogenic signals. Cyclin D3 is a key component of the cell cycle progression machinery and induces progression through the G1 phase of the cell cycle. Cyclin D3 is expressed in nearly all proliferating cells, and shows the most broad expression pattern of all three D-type (D1-D3) cyclins. Cyclin D3 is encoded from the 6p21 chromosome region and the protein is predominantly localized in the nucleus. Once induced, cyclin D3 binds and activates its associated cyclin-dependent kinases CDK4 and CDK6. Amplification of the cyclin D3 gene and overexpression of cyclin D3 protein is seen in several human cancers. A large number of human malignancies contain lesions in pathways impacting on cyclin D3. Abnormal expression of Cyclin D3 is believed to be a driving force in several human cancers. A possible role for cyclin D3 in the malignancies of the lymphoid system is suggested by the observations that cyclin D3 gene is rearranged in several neoplastic diseases such as diffuse large B cell lymphomas or multiple myelomas. Anti-Cyclin D3 is ideal for researchers interested in Cancer Research and Immunology research.

Supplier: Rockland Immunochemical

The Anti-Glut2 antibody was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). The glucose transporter GLUT2 is a transmembrane carrier protein that allows protein facilitated glucose movement across cell membranes. GLUT2 is expressed in the plasma membranes of the liver, intestine, renal tubular cells, pancreatic islet beta cells, as well as in the portal and hypothalamic areas. Due to its low affinity and high capacity, GLUT2 transports dietary sugars, glucose, galactose and fructose in high concentrations, displaying large bidirectional fluxes in and out of cells. In pancreatic beta cells, GLUT2 is essential for glucose-stimulated insulin secretion. GLUT2 expression is necessary for the physiological control of glucose-sensitive genes, and its inactivation in the liver leads to impaired glucose-stimulated insulin secretion. In the nervous system, GLUT2-dependent glucose sensing regulates feeding, thermoregulation and pancreatic islet cell mass and function, as well as sympathetic and parasympathetic activities. In humans, inactivating mutations in GLUT2 cause Fanconi–Bickel syndrome, which is characterized by hepatomegaly and kidney disease. Anti-Glut2 is ideal for researchers interested in studying glucose transport mediated by Glut2 protein in the fields of diabetes, obesity, metabolism, and neuroscience research.

Supplier: Rockland Immunochemical

TAF10 (TATA-Box Binding Protein Associated Factor 10) is the protein that coordinates activities for the initiation of transcription by RNA polymerase II required for activities of more than 70 polypeptides. TFIID binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as co-activators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes one of the small subunits of TFIID that is associated with a subset of TFIID complexes. Studies with human and mammalian cells have shown that this subunit is required for transcriptional activation by the estrogen receptor, for progression through the cell cycle, and may also be required for certain cellular differentiation programs. Anti-TAF10 Antibody is useful for researchers interested in Chromatin research, transcription factor activity research, and DNA binding and transcription co-activator activity research.

Supplier: Rockland Immunochemical

Anti-Nuclear receptor ROR gamma pS203 was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). Nuclear receptor ROR gamma pS203 antibody detects mouse receptor ROR gamma phosphorylated at the serine 203 position. RAR-related orphan receptor gamma is a member of the nuclear receptor family of transcription factors. (ROR-gamma) is a key regulator of cellular differentiation, immunity, peripheral circadian rhythm as well as lipid, steroid, xenobiotics and glucose metabolism. ROR-gamma regulates the circadian expression of clock genes such as CRY1, ARNTL/BMAL1 and NR1D1 in peripheral tissues and in a tissue-selective manner. It is also involved in the regulation of the rhythmic expression of genes involved in glucose and lipid metabolism and is a negative regulator of adipocyte differentiation. It controls adipogenesis as well as adipocyte size and modulates insulin sensitivity in obesity. Isoform 2, ROR-gamma is essential for lymphoid organogenesis, in particular lymph nodes and Peyer's patches. ROR-gamma also plays an important regulatory role in thymopoiesis, and in inhibiting apoptosis of undifferentiated T cells. Anti-nuclear receptor ROR gamma pS203 is ideal for researcher's interested in autoimmune diseases such as psoriasis and rheumatoid arthritis, circadian rhythms, and immune system disorders.

Supplier: Genetex

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fibre is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. Covalent modifications of the canonical core histones, including acetylation, phosphorylation, methylation, and monoubiquitination, are used to mark nucleosomes to create chromatin domains with a range of functions. The information encoded by the modifications can contribute to the formation and/or maintenance of transcriptionally active and inactive chromatin in response to various signalling pathways. 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. Phosphorylation of histone H3, referred to as the nucleosomal response, is localized to a small fraction of highly acetylated H3 and occurs primarily in response to mitogenic and stress stimuli.2, 3, 9-12 Phosphorylation of histone H3 on S10 is tightly correlated with chromosome condensation during both mitosis and meiosis. Phosphorylation at this site is also directly correlated with the induction of immediate-early genes such as c-jun, c-fos, and c-myc.

Supplier: Biosensis

The Biosensis Mature BDNF/proBDNF Combo RapidTM enzyme-linked immunosorbent assay (ELISA) Kit combines individual, but complementary ELISA kits for the two most important BDNF isoforms: Mature BDNF (BEK-2211) and full-length proBDNF (BEK-2217).

Supplier: Biosensis

The Lamin proteins are members of the intermediate filament protein family but are located inside the nucleus rather than in the cytoplasm (1). The lamins function as skeletal components tightly associated with the inner nuclear membrane. Originally the proteins of the nuclear cytoskeleton were named Lamin A, B and C, from top to bottom as visualized on SDS-PAGE gels. Subsequently it was found that Lamins A and C were coded for by a single gene (2), while the Lamin B band may contain two proteins encoded by two genes now called Lamin B1 and Lamin B2. Lamin A has a mass of about 74kDa while Lamin C is 65kDa. The Lamin A protein includes 98 amino acids missing from Lamin C, while Lamin C has a C-terminal 6 amino acid peptide not present in Lamin A. Apart from these regions Lamin A and C are identical so that antibodies raised against either protein are likely to cross react with the other, as is the case with this monoclonal. Lamin polymerization and depolymerization is regulated by phosphorylation by cyclin dependent protein kinase 1 (CDK1), the key component of "maturation promoting factor", the central regulator of cell division. Activity of this kinase increases during cell division and is responsible for the breakdown of the nuclear lamina. Mutations in the LMNA gene are associated with several serious human diseases, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease type 2B1, and Hutchinson-Gilford progeria syndrome. This family of diseases belong to a larger group which are often referred to as Laminopathies, though some laminopathies are associated in defects in Lamin B1, B2 or one or other of the numerous nuclear lamina binding proteins. A truncated version of lamin A, commonly known as progerin, causes Hutchinson-Gilford progeria syndrome, a form of premature aging (3).

Supplier: Biosensis

The Lamin proteins are members of the intermediate filament protein family but are located inside the nucleus rather than in the cytoplasm (1). The lamins function as skeletal components tightly associated with the inner nuclear membrane. Originally the proteins of the nuclear cytoskeleton were named Lamin A, B and C, from top to bottom as visualized on SDS-PAGE gels. Subsequently it was found that Lamins A and C were coded for by a single gene (2), while the Lamin B band may contain two proteins encoded by two genes now called Lamin B1 and Lamin B2. Lamin A has a mass of about 74kDa while Lamin C is 65kDa. The Lamin A protein includes 98 amino acids missing from Lamin C, while Lamin C has a C-terminal 6 amino acid peptide not present in Lamin A. Apart from these regions Lamin A and C are identical so that antibodies raised against either protein are likely to cross react with the other, as is the case with this monoclonal. Lamin polymerization and depolymerization is regulated by phosphorylation by cyclin dependent protein kinase 1 (CDK1), the key component of "maturation promoting factor", the central regulator of cell division. Activity of this kinase increases during cell division and is responsible for the breakdown of the nuclear lamina. Mutations in the LMNA gene are associated with several serious human diseases, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease type 2B1, and Hutchinson-Gilford progeria syndrome. This family of diseases belong to a larger group which are often referred to as Laminopathies, though some laminopathies are associated in defects in Lamin B1, B2 or one or other of the numerous nuclear lamina binding proteins. A truncated version of lamin A, commonly known as progerin, causes Hutchinson-Gilford progeria syndrome, a form of premature aging (3).

Supplier: Biosensis

High-mobility group proteins were named originally since they are abundand relatively low molecular weight proteins which run quickly on SDS-PAGE gels. High-mobility group protein box 1 (HMGB1, Amphoterin) is one of these. The "bx" in the name refers to the so-called high mobility group (HMG) box, a compact domain involved in DNA binding and protein-protein interactions. the HMGB1 molecule has two of these HMG domains. The protein is alslo called amphoterin, this name being derived from the presence of two highly charged regions in the molecule, a relatively neutrally charged N-terminus and a very negatively charged C-terminus. In fact the molecule is very unusually charged throughout, the human sequence consisting of 16.7% Glutamic acid, 9.3% Aspartic acid, 20% lysine and 9.3% Arginine. HMGB1 can bind Toll like receptor 4 (TLR4) and the Receptor for Advanced Glycation End products (RAGE). TLRs are components of the innate immune system, first recognized as a family of receptors which recognize "Pathogen Associated Molecular Pattern molecules (PAMPs). PAMPs are common components of bacteria and when TLRs bind these a strong inflammatory response is activated. More recently it has been recognized that TLRs can also be activated by Damage Associated Molecular Pattern molecules (DAMPs), which are endogenous substances released from damaged and diseased cells which also bind to TLR family receptors and also activate inflammation. HMGB1 is such a DAMP, binding to TLR4, and much evidence suggests that HMGB1 is a strong activator of inflammation. Interestingly, HMGB1 is released by necrotic cells but not by apoptotic cells (1).

Supplier: BioVendor

Glycosaminoglycans (GAGs) are large complex carbohydrate molecules that interact with a wide variety of proteins involved in physiological and pathological processes. GAGs are also known as mucopolysaccharides due to their viscous, lubricating properties, as found in mucous secretions. GAGs are found on all animal cell surfaces in the extracellular matrix (ECM), and some are known to bind and regulate certain proteins, including chemokines, cytokines, growth factors, morphogens, enzymes and adhesion molecules.

GAGs are linear, sulphated, negatively charged polysaccharides that have molecular weights of approximately 10–100 kDa. GAGs can be divided into two main types. Non‐sulphated GAGs include hyaluronic acid (HA), whereas sulphated GAGs include chondroitin sulphate (CS), dermatan sulphate (DS), keratan sulphate (KS), heparin and heparan sulphate (HS).

GAGs play an important role in cell signaling and development, angiogenesis, axonal growth, tumour progression, metastasis and anti‐coagulation. Uncontrolled progenitor cell proliferation leads to malignant tissue transformation and cancer. GAGs and proteoglycans (PGs) are believed to play a critical role in cell proliferation, acting as co‐receptors for growth factors of the fibroblast growth factor (FGF) family.

PGs are composed of a core protein to which one or more GAG chains are covalently attached. Examples of large PGs are aggrecan, the major PG in cartilage, and versican, which is present in numerous adult tissues such as blood vessels and skin. PGs are known to have a variety of functions, dependent on type and in vivo location, and have important roles in invertebrate and vertebrate development, maintenance, and tissue repair. Many biologically potent small proteins can bind GAG chains as a major part of their function in the ECM, at the cell surface, and also in some intracellular locations. Thus, PGs have become a major focus in research on many diseases.

Supplier: Genevac

miVac Centrifugal Evaporation Systems provide a compact, high performing solution for removing water and organic solvents from a variety of sample formats. Configure a system to meet your application requirements.