Katalognummer: 223 - 91-673
Produktkategori: Företag och industri > Vetenskap och laboratorium
Storlek: 0.05 mg
91-975
14-3-3 Protein Epsilon acts as an adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. 14-3-3 protein epsilon binds to a large number of partners, usually by recognition of a phophoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.
91-660
Galectin-3(LGALS3) is also known as Galactose-specific lectin 3, Mac-2 antigen, Carbohydrate-binding protein 35, Laminin-binding protein and Galactoside-binding protein. LGALS3 is highly expressed in early stages of papillary carcinoma, and lowly during tumor progression. LGALS3 is probably forms homo- or heterodimers and secreted by a non-classical secretory pathway and associates with the cell surface. LGALS3 plays an important role during the acquisition of vasculogenic mimicry and angiogenic properties. LGLAS3 takes part in an immune regulator to inhibit T-cell immune responses and promote tumor growth, as a result providing a new mechanism for tumor immune tolerance.
91-718
Ribonuclease 3 (RNASE3) is a basic protein that is localized to the eosinophil primary matrix and belongs to the pancreatic ribonuclease family. RNASE3 is released during degranulation of eosinophils. RNASE3 possesses a wide variety of biological activities. RNASE3 interacts with bacterial lipopolysaccharide (LPS) and lipoteichoic acid (LTA). RNASE3 exhibits antibacterial activity, including cytoplasmic membrane depolarization of preferentially Gram-negative, but also Gram-positive strains. It promotes E. coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content.
91-752
Reticulocalbin-3 is a member of the CREC family that is involved in the secretory pathway. Members of the CREC family consist of a number of multiple EF-hand domains. Reticulocalbin-3 localizes to the endoplasmic reticulum lumen. The bioinformaticanalysis of Reticulocalbin-3 reveal that it is a putative Ca2+-binding protein. In addition, it has been shown that autoactivation and secretion of PACE4 was increased upon co-expression with Reticulocalbin-3. The proPACE4-RCN-3 complex is plays an important role in the biosynthesis of PACE4.