| Description | Casein sodium salt from bovine milk is suitable for use in: ·the preparation of casein-based diets to investigate nutritional effect of vitamin E in diets for Litopenaeus vannamei postlarve ·in an assay to determine the activity of a three-enzyme solution containing trypsin, chymotrypsin Casein sodium salt from bovine milk is suitable for use in: ·the preparation of casein-based diets to investigate nutritional effect of vitamin E in diets for Litopenaeus vannamei postlarve ·in an assay to determine the activity of a three-enzyme solution containing trypsin, chymotrypsin and peptidase ·a study to investigate the effects of bovine somatotropin (bST) administration and abomasal casein infusion on nitrogen metabolism in Holstein steers ·as constituent of blocking solution in immunoblotting. 生化机理英文：Biochem/physiol Actions α-Casein can be an immunogen in young children, and anti-α-casein antibodies have strong cross-reactivity with insulin. This effect can explain the uncommon insulin autoimmunity, but it does not appear to progress to Type I diabetes. Casein sodium salt from bovine milk is a phosphoprotein. There are four main types of Casein which make up approximately 80% of the total protein in bovine milk: α-s1 Casein, α-s2 Casein, β-Casein, and κ-Casein. Casein is proposed to be the main protective constituent in milk... Read More | Inquire | TEV Protease is the 241 amino acid (aa), 27 kDa catalytic domain of the nuclear inclusion a (NIa) protein encoded by the potyvirus, tobacco etch virus (TEV). It may be used in biotechnology to cleave affinity tags from recombinant proteins, either co-translationally orin vitrofollowing purification.TEV Protease is the 241 amino acid (aa), 27 kDa catalytic domain of the nuclear inclusion a (NIa) protein encoded by the potyvirus, tobacco etch virus (TEV). It may be used in biotechnology to cleave affinity tags from recombinant proteins, either co-translationally orin vitrofollowing purification. Its high specificity and activity at a wide range of pH and ionic strength make TEV Protease more versatile than many other proteases used for the same purpose. Unlike factor Xa, enteropeptidase or thrombin, TEV Protease has not been found to cleave at unintended sites, even when present at a high concentration. TEV Protease is a 3C-type protease that cleaves substrates with a consensus sequence of ENLYFQG. Cleavage occurs between Q and G. Since the final aa remains on the cleaved protein where it could potentially affect structure or function, substitution of a variety of aa have been tested. In order of efficiency, S, A, M, Y, D, N, E, K or L may be effectively used in place of G. Several of the remaining aa may also vary, giving a final consensus sequence of ExxYF(M)Q(E)/G(S, A or others) where aa in parenthesis are alternatives and x is any aa. The autocatalytic site of NIa at S2256 has been mutated to an N for improved stability of the protease.Tobacco Etch Virus Protease is a highly site-specific cysteine protease that is found in the tags from fusion proteins. The optimal temperature for cleavage is 30°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of recombinant viral TEV protease, reaction time, or incubation temperature. It can be removed by Ni2+ affinity resin... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:MCP-2 and CCL7 are two monocyte chemotactic proteins produced by human MG-63 osteosarcoma cells. Both MCP-2 and CCL7 are members of the C-C family of chemokines and share 62% and 71% amino acid sequence identity, Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:MCP-2 and CCL7 are two monocyte chemotactic proteins produced by human MG-63 osteosarcoma cells. Both MCP-2 and CCL7 are members of the C-C family of chemokines and share 62% and 71% amino acid sequence identity, respectively, with MCP-1. CCL7 also shares 58% amino acid identity with MCP-2. CCL7 cDNA encodes a 99 amino acid residue precursor protein from which the N-terminal 23 amino acid residues are cleaved to generate the 76 amino acid residue mature CCL7. Mature CCL7 contains a potential N-linked and several possible O-linked glycosylation sites. Similarly to other C-C chemokines, all three MCP proteins are monocyte chemoattractants. In addition, the three MCPs can chemoattract activated NK cells as well as CD4+ and CD8+ T lymphocytes. All three cytokines have also been shown to attract eosinophils and induce histamine secretion from basophils... 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 |