| Description | Lactoferrin less the iron molecule. Like lactoferrin, Apolactoferrin is an iron-binding protein found in human milk. Lactoferrin along with Secretory IgA can have a bacteriostatic effect in the intestinal tract of a breast fed newborn. Lactoferrin may also function as a promoter of iron absorption Lactoferrin less the iron molecule. Like lactoferrin, Apolactoferrin is an iron-binding protein found in human milk. Lactoferrin along with Secretory IgA can have a bacteriostatic effect in the intestinal tract of a breast fed newborn. Lactoferrin may also function as a promoter of iron absorption due to the high bioavailability of iron from digested Lactoferrin.Lönnerdal, Bo. The American Journal of Clinical Nutrition 42: December 1985, pp 1299-1317 Prepared from human milk shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA-required tests... Read More | Inquire | Purity>95% SDS-PAGE.FunctionThe soluble form is chemotactic for T-cells and monocytes, but not for neutrophils. The membrane-bound form promotes adhesion of those leukocytes to endothelial cells. May play a role in regulating leukocyte adhesion and migration processes at the endothelium. Binds toPurity>95% SDS-PAGE.FunctionThe soluble form is chemotactic for T-cells and monocytes, but not for neutrophils. The membrane-bound form promotes adhesion of those leukocytes to endothelial cells. May play a role in regulating leukocyte adhesion and migration processes at the endothelium. Binds to CX3CR1.Post-translationalA soluble short 95 kDa form may be released by proteolytic cleavage from the long membrane-anchored form. O-glycosylated with core 1 or possibly core 8 glycans... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:NG2, also known as CSPG4, MCSP, and AN2, is a 400-500 kDa transmembrane chondroitin sulfate proteoglycan (CSPG) with a protein core of approximately 300 kDa. The extracellular region can be proteolytically shed fromPurity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:NG2, also known as CSPG4, MCSP, and AN2, is a 400-500 kDa transmembrane chondroitin sulfate proteoglycan (CSPG) with a protein core of approximately 300 kDa. The extracellular region can be proteolytically shed from the cell surface. Mature human NG2 consists of a 2195 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment, and a 77 aa cytoplasmic domain. Within aa 1583-2224, human NG2/CSPG4 shares 83% aa sequence identity with mouse and rat CSPG4. NG2 binds to the extracellular matrix proteins Laminin, Tenascin, and Collagens II, V, and VI as well as to the growth factors FGF-2 and PDGF-AA. NG2 is expressed on glial cell progenitors known as O2A cells or NG2 glia. These cells are neuronally responsive and differentiate primarily into oligodendrocytes but also into astrocytes. NG2 associates with PDGF R alpha and the AMPA R subunit GluR2. It is up-regulated on microglial cells during inflammation and contributes to the induction of inflammatory mediators. Various CSPGs in the brain inhibit neurite outgrowth through interactions with Nogo Receptor/NgR1 and NgR3. This recombinant protein product corresponds to the last 5 CSPG repeats, a region which can independently inhibit neurite outgrowth. NG2 is also expressed on vascular mural cells and capillaries. It promotes vascular endothelial cell (EC) migration and angiogenesis through interactions with Galectin-3 and Integrin alpha 3 beta 1 on EC, Plasminogen, and Angiostatin. NG2 is also expressed on a variety of tumors where it contributes to tumor cell adhesion, motility, and invasion... Read More | Background:VCAM-1, also known as CD106, is an immunoglobulin (Ig)-like adhesion molecule that is mainly expressed in endothelial cells and other cell types including macrophages, dendritic cells, neurons, smooth muscle cells, fibroblasts, and oocytes. It plays a critical role in inflammation by Background:VCAM-1, also known as CD106, is an immunoglobulin (Ig)-like adhesion molecule that is mainly expressed in endothelial cells and other cell types including macrophages, dendritic cells, neurons, smooth muscle cells, fibroblasts, and oocytes. It plays a critical role in inflammation by recruiting leukocytes to acute and chronic inflammation sites. Alternatively-spliced forms are known to occur, but the most common form is a type I transmembrane protein with a 674 aa extracellular domain (ECD) that includes seven C2-type immunoglobulin domains, a 22 aa transmembrane segment, and a 19 amino acid (aa) cytoplasmic tail. Within the ECD, human VCAM-1 shares 75% and 76% aa sequence identity with the mouse and rat VCAM-1, respectively. VCAM-1 binds to leukocyte integrins alpha 4 beta 1 (VLA-4) and alpha 4 beta 7. During the inflammatory adhesion mechanism, activated integrins halt rolling leukocytes and attach them firmly to the vascular endothelium. The VCAM-1:VLA-4/ alpha 4 beta 7 interaction is also thought to be involved in the extravasation of white blood cells through the blood vessel wall to sites of inflammation. ELISA techniques have shown that detectable levels of soluble VCAM-1 are present in the biological fluids of apparently normal individuals, but elevated levels of serum VCAM-1 are indicative of future Atrial Fibrillation incident as well as liver disease. Tumor cells use overexpression of VCAM-1 as means of escaping immune surveillance.Post-translational modifications：Sialoglycoprotein.Function:Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with the beta-1 integrin VLA4 on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/VLA4 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation... Read More |