| Description | The Collagenase-Elastase blend is a tissue dissociation enzyme cocktail for cell isolation. The tissue dissociation process consists in the release of functional and viable cells from animal tissue, with minimal impact on the cell’s viability. The main reagent used for the tissue dissociation The Collagenase-Elastase blend is a tissue dissociation enzyme cocktail for cell isolation. The tissue dissociation process consists in the release of functional and viable cells from animal tissue, with minimal impact on the cell’s viability. The main reagent used for the tissue dissociation process is Collagenase. Collagenases are enzymes that break down the native collagen that holds animal tissues together. The second enzyme found in our blend is Elastase: a serine protease that also hydrolyzes amides and esters. It is produced in the pancreas as an inactive zymogen and activated in the duodenum by trypsin. While elastase will hydrolyze a wide variety of protein substrates, it is unique among proteases in its ability to hydrolyze native elastin, a substrate not attacked by trypsin, chymotrypsin or pepsin. Elastin, a matrix component of tissues involved in stretching processes, is found in highest concentrations in the elastic fibers of connective tissues. Elastase is frequently used to dissociate tissues which contain extensive intercellular fiber networks. For this purpose, it is usually used with other enzymes such as collagenase, trypsin, and chymotrypsin. Elastase is the enzyme of choice for the isolation of Type II cells from the lung... Read More | Inquire | Purity≥ 95% SDS-PAGE; HPLCRelevanceHuman erythropoietin is member of the EPO/TPO family and encodes a secreted, glycosylated cytokine hormone composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and Purity≥ 95% SDS-PAGE; HPLCRelevanceHuman erythropoietin is member of the EPO/TPO family and encodes a secreted, glycosylated cytokine hormone composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types. It is produced by kidney or liver of adult mammals and by liver of fetal or neonatal mammals... Read More | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：p53 is well known for its key role as a tumor suppressor protein. It is 393 amino acids (aa) in length with a predicted molecular weight of 44 kDa. It belongs to the p53 family that also includes p63 and p73Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：p53 is well known for its key role as a tumor suppressor protein. It is 393 amino acids (aa) in length with a predicted molecular weight of 44 kDa. It belongs to the p53 family that also includes p63 and p73. Structurally, p53 is characterized by an N-terminal transactivation domain, central DNA-binding and oligomerization domains, and a C-terminal regulatory domain. It is thought to exist as a homotetramer, and it exhibits approximately 72% and 76% aa identity with its mouse and rat orthologs, respectively. Mutations in the p53 gene are one of the most frequent genomic events accompanying oncogenic transformation. p53 responds to signals such as DNA damage or cell stress primarily through its actions as a transcription factor. Among its gene targets are a range factors that promote DNA repair mechanisms or apoptosis, including cell cycle regulatory proteins and members the Bcl-2 family. Because of its critical role in genomic homeostasis, p53 activities are tightly regulated by a network of protein-protein interactions, microRNAs, and a range of post-translational modifications, including phosphorylation, acetylation, methylation, and ubiquitination. A widely studied regulator is Murine Double Minute 2 (MDM2). MDM2 is known to suppress p53 activity through direct binding or through its actions as a Ubiquitin ligase (E3) that catalyzes p53 ubiquitination and proteasome-mediated degradation... Read More | Purity>98% SDS-PAGE. > 98 % by HPLC.Additional sequence informationThis product is for the mature full length protein. The signal peptide is not included.FunctionCytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including Purity>98% SDS-PAGE. > 98 % by HPLC.Additional sequence informationThis product is for the mature full length protein. The signal peptide is not included.FunctionCytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.BackgroundGM-CSF is a hematopoietic growth factor that stimulates the development of neutrophils and macrophages, and promotes the proliferation and development of early erythroid megakaryocytic and eosinophilic progenitor cells. It is produced by endothelial cells, monocytes, fibroblasts and T-lymphocytes. GM-CSF inhibits neutrophil migration and enhances the functional activity of the mature end-cells. GM-CSF has also been reported to have a functional role on non-hematopoietic cells and can induce human endothelial cells to migrate and proliferate. Additionally, it can stimulate the proliferation of a number of tumor cell lines, including osteogenic sarcoma, carcinoma and adenocarcinoma cell lines. It is reported that GM-CSF has no biological effects across species. Recombinant Rat GM-CSF is a 14.5kDa globular protein consisting of 127 amino acid residues... Read More |