5798 Results for: "extraction"

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: 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.