| Description | An acute-phase plasma protein found in human plasma at 100-300 mg per 100 ml. Binds hemoglobin, thus preventing loss of iron through the kidneys. Humans are polymorphic for haptoglobin, with three major phenotypes: Hp 1-1, Hp 2-1, and Hp 2-2. While the phenotypic distribution can vary greatly An acute-phase plasma protein found in human plasma at 100-300 mg per 100 ml. Binds hemoglobin, thus preventing loss of iron through the kidneys. Humans are polymorphic for haptoglobin, with three major phenotypes: Hp 1-1, Hp 2-1, and Hp 2-2. While the phenotypic distribution can vary greatly between ethnicities and geographic location, the Hp 2-1 phenotype is the most prevalent phenotype in humans. Plasma concentrations of haptoglobin are highest in individuals with Hp 1-1, intermediate in Hp 2-1 individuals, and lowest in Hp 2-2 individuals. Hp 1-1 is the most effective at binding hemoglobin, and Hp 2-2 is the least effective. This functional difference may be associated with the frequency and severity of epilepsy attacks, as researchers have found a correlation between recurring seizures and the Hp 2-2 phenotype... Read More | Purity>95% (SDS-PAGE&HPLC) Endotoxin level<1.0 EU/µgFunctionBifunctional growth-modulating glycoprotein. Inhibits growth of several human carcinoma cells in culture and stimulates proliferation of human fibroblasts and certain other tumor cells | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:GAPDH (Glyceraldehyde-3-Phosphate Dehydrogenase) is a Protein Coding gene. Diseases associated with GAPDH include Microcephaly 21, Primary, Autosomal Recessive and Schistosomiasis. Among its related pathways are Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:GAPDH (Glyceraldehyde-3-Phosphate Dehydrogenase) is a Protein Coding gene. Diseases associated with GAPDH include Microcephaly 21, Primary, Autosomal Recessive and Schistosomiasis. Among its related pathways are glycolysis (BioCyc) and gluconeogenesis III. Gene Ontology (GO) annotations related to this gene include identical protein binding and NAD binding. An important paralog of this gene is GAPDHS... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Histones are a complex family of highly conserved basic proteins responsible for packaging chromosomal DNA into nucleosomes. Histone proteins exhibit two levels of diversity: 1. evolutionary diversity Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Histones are a complex family of highly conserved basic proteins responsible for packaging chromosomal DNA into nucleosomes. Histone proteins exhibit two levels of diversity: 1. evolutionary diversity between species and 2. subtype diversity in a class(H1, H2A, H2B, H3 or H4) within a species. It has become more and more evident that histone modifications are key players in the regulation of chromatin states and dynamics as well as in gene expression. Therefore, histone modifications and the enzymatic machinery that set them are crucial regulators that can control cellular proliferation, differentiation, plasticity, and malignancy processes. However, extracellular histones are a double-edged sword because they also damage host tissue and may cause death. Histones bound to platelets, induced calcium influx, and recruited plasma adhesion proteins such as fibrinogen to induce platelet aggregation. Histone H2B proteins have been studied in a variety of species and are easily detected in most species. The reversible ubiquitylation of histone H2B has long been implicated in transcriptional activation and gene silencing. Phosphorylation of H2B serine 32 occurs in normal cycling and mitogen-stimulated cells. Notably, this phosphorylation is elevated in skin cancer cell lines and tissues compared with normal counterparts. HIST2H2BE is a member of the histone H2B family and generates two transcripts through the use of the conserved stem-loop termination motif, and the polyA addition motif... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hingePurity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hinge region with a hydrophobic cleft that is exposed upon Ca2+ binding. S100B is a 91 amino acid (aa) protein, after removal of the initial methionine, and is found as homodimers of 10.4 kDa monomers. Human S100B shares 99%, 98%, 100%, 99% and 97% aa sequence identity with mouse, rat, rabbit, equine and bovine S100B, respectively. Within the S100 family, human S100B shows the highest aa identity (59%) with S100A1. S100B is expressed primarily by astrocytes and oligodendrocytes in the central nervous system, and by Schwann cells in the peripheral nervous system. Ca2+-bound S100B interacts in vitro with at least 20 cytoplasmic proteins, including several structural molecules such as tubulin and GFAP. It can inhibit the phosphorylation of these kinase substrates and others such as tau and neuromodulin. Astrocytes can secrete S100B, which then acts in a cytokine-like manner. Nanomolar concentrations of S100B are secreted constitutively, promote proliferation, and are neurotrophic and anti-apoptotic. Blood levels of S100B reflect extracellular concentrations within the nervous system, and are elevated in Down’s syndrome, Alzheimer’s disease and Tourette’s syndrome, metabolic stress, acute brain injury and brain tumors. Micromolar concentrations of S100B can be destructive and pro-apoptotic; they induce the expression of iNOS, COX-2, IL-1, IL‑6 and TNF-alpha by microglia, astrocytes or neurons. Most extracellular actions of S100B can be mediated by RAGE (receptor for advanced glycation end products), which is also a receptor for other S100 proteins... Read More |