| Description | Transferrin is a monomeric glycoprotein found in plasma at an average concentration of 250 mg/100ml. The specific iron-binding protein in plasma, it has a role in the transportation and distribution of iron among the body organs, in iron metabolism and in prevention of iron loss via the kidney. Transferrin is a monomeric glycoprotein found in plasma at an average concentration of 250 mg/100ml. The specific iron-binding protein in plasma, it has a role in the transportation and distribution of iron among the body organs, in iron metabolism and in prevention of iron loss via the kidney. Stored in bone marrow as TF-bound iron, it also possesses bacteriostatic and fungistatic activity. Clinically, decreases in transferrin are observed in congenital disorders, newborns, inflammatory diseases, hypo-proteinemias and nephritic syndrome; increases are found in pregnancy, iron-deficiency anemias and inoculation hepatitis. Transferrin is required by all types of cells in cultures for maximal growth. It is, therefore, an important factor used in defined culture media... 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 | Product IntroductionKGF keratinocyte growth factor (KGF), a cytokine identified by Rubin et al (1989) from the culture supernatant of embryonic lung fibroblasts, is an FGF family member, namely FGF-7.KGF is secreted by stromal cells and its receptor is distributed in epithelial cells, where it is a Product IntroductionKGF keratinocyte growth factor (KGF), a cytokine identified by Rubin et al (1989) from the culture supernatant of embryonic lung fibroblasts, is an FGF family member, namely FGF-7.KGF is secreted by stromal cells and its receptor is distributed in epithelial cells, where it is a potent epithelial cell specific growth factor, and its mitogenic activity is mainly expressed in keratinocytes, which can specifically promote epithelial cell proliferation, migration and differentiation, and is closely related to many aspects, such as organ development, wound repair, tumorigenesis and immune reconstitution.Osrhkgf was created using genetic recombination, expressed from rice endosperm cells and through a protein purification process.Specification parametersSource Oryza sativaAppearance white lyophilized powderActivity ≥1.0×105IU/mgpH 6.5-7.5Molecular weight 19.0 kDEndotoxin ≦0.1EU/ugCAS No 148348-15-6Matters needing attentionReconstitution: it is recommended to lyophilize the powder of osrhkgf to 100-200 UG/ml with sterile water to make further dilutions with other solvents.The dissolved osrhkgf could be stored for 2-7 days at 4 ◦ C and used up as soon as possible.To not use for short periods, store at - 20 ℃.Use as soon as possible after opening to avoid contamination.Limitations of useIt is suitable for research, laboratory and production use only and cannot be used directly in humans... Read More | Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：KGF (keratinocyte growth factor), also known as FGF-7 (fibroblast growth factor-7), is one of 22 known members of the mouse FGF family of secreted proteins that plays a key role in development, Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：KGF (keratinocyte growth factor), also known as FGF-7 (fibroblast growth factor-7), is one of 22 known members of the mouse FGF family of secreted proteins that plays a key role in development, morphogenesis, angiogenesis, wound healing, and tumorigenesis (1-4). KGF expression is restricted to cells of mesenchymal origin. When secreted, it acts as a paracrine growth factor for nearby epithelial cells (1). KGF speeds wound healing by being dramatically upregulated in response to damage to skin or internal structures that results in high local concentrations of inflammatory mediators such as IL-1 and TNF-alpha. (2, 5). KGF promotes cell migration and invasion, and mediates melanocyte transfer to keratinocytes upon UVB radiation (6, 7). It has been used ectopically to avoid chemotherapy-induced oral mucositis in patients with hematological malignancies (1). Deletion of KGF affects kidney development, producing abnormally small ureteric buds and fewer nephrons (8). It also impedes hair follicle differentiation (9). The 194 amino acid (aa) KGF precursor contains a 31 aa signal sequence and, like all other FGFs, an ~120 aa beta -trefoil scaffold that includes receptor- and heparin-binding sites. KGF signals only through the IIIb splice form of the tyrosine kinase receptor, FGF R2 (FGF R2-IIIb/KGF R) (10). Receptor dimerization requires an octameric or larger heparin or heparin sulfate proteoglycan (11). FGF-10, also called KGF2, shares 51% aa identity and similar function to KGF, but shows more limited expression than KGF and uses an additional receptor, FGF R2-IIIc (12). Following receptor engagement, KGF is typically degraded, while FGF-10 is recycled (12). Mature human KGF, which is active across species, shares 98% aa sequence identity with bovine, equine, ovine and canine, 96% with mouse and porcine, and 92% with rat KGF, respectively... Read More |