vcam-1

VCAM-1 (CD106, INCAM-110) is a cell adhesion molecule and a member of the immunoglobulin superfamily. It's important function is a recognition of cell-cell. Appears to function in leukocyte-endothelial cell adhesion. Interacts with integrin alpha-4 beta-1 (ITGA4 ITGB1) on leukocytes, and mediates both adhesion and signal transduction. The VCAM1 ITGA4 ITGB1 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation。

Vascular cell adhesion molecule 1 (VCAM-1) is a cell surface protein belonging to the immunoglobulin superfamily, the protein is expressed by activated endothelial cells and certain leukocytes (such as macrophages). IL-1 beta, IL-4, TNF-alpha and IFN-gamma induced the expression of VCAM-1. The human and mouse VCAM-1 proteins share approximately 76% amino acid similarity. Mouse VCAM-1 is Important in cell-cell recognition. it appears to function in leukocyte-endothelial cell adhesion, and interacts with integrin alpha-4 beta-1 (ITGA4 ITGB1) on leukocytes, and mediates both adhesion and signal transduction.

VCAM-1 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 76 kDa and the accession number is P19320-1.

VCAM-1 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 75.8 kDa and the accession number is Q3UPN1.

VCAM-1 Protein, Mouse, Recombinant (His & hFc) is expressed in HEK293 mammalian cells with His and hFc tag. The predicted molecular weight is 102 kDa and the accession number is Q3UPN1.

VCAM-1 Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 100.8 kDa and the accession number is P19320-1.

VCAM-1 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with His and Avi tag. The predicted molecular weight is 77.36 kDa and the accession number is NP_001069.1.

Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with integrin alpha-4 beta-1 (ITGA4 ITGB1) on leukocytes, and mediates both adhesion and signal transduction. The VCAM1 ITGA4 ITGB1 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation. VCAM-1 Protein, Rat, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 77.4 kDa and the accession number is P29534.

VCAM-1 Protein, Human, Recombinant (hFc), Biotinylated is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 101 kDa and the accession number is P19320-1.

Galectin-9 is a cytoplasmic protein that contains two galectin domains. Galectin-9 is an S-type lectin that is over-expressed in Hodgkin's disease tissue. Galectin-9 binds galactosides and has high affinity for the Forssman pentasaccharide. Galectin-9 plays a role in thymocyte-epithelial interactions relevant to the biology of the thymus and Inhibits cell proliferation. Galectin-9 is a ligand for HAVCR2 TIM3 and induces T-helper type 1 lymphocyte (Th1) death. In addition, Galectin-9 suppresses tumor cell metastasis by interfering with the associations CD44, VCAM-1, Integrin α4β1

Moesin is a member of the ERM family which includes ezrin and radixin. ERM proteins, highly related members of the larger protein 4.1 superfamily, can exist in an active or inactive conformation. It seems that ERM proteins function as cross-linkers between plasma membranes and actin-based cytoskeletons. The sole Drosophila ERM protein, moesin, functions to promote cortical actin assembly and apical-basal polarity. As a result, cells lacking moesin lose epithelial characteristics and adopt invasive migratory behavior. It is localized to filopodia and other membranous protrusions that are important for cell-cell recognition and signaling and cell movement. Moesin contains 1 FERM domain and is expressed in all tissues and cultured cells studied. Moesin has been shown to interact with CD43, Neutrophil cytosolic factor 1, VCAM-1, Neutrophil cytosolic factor 4, ICAM3, and EZR.

ADAM9 (A disintegrin and metallopeptidase domain 9, MDC9, meltrin gamma), is a type 1 transmembrane protein that has been associated with cancer development and metastases. ADAM9 is consistently overexpressed in various human cancers, and plays a role in tumorigenesis in mouse models. ADAM9 cleaves and releases a number of molecules with important roles in tumorigenesis and angiogenesis, such as EGF, FGFR2iiib, Tie-2, Flk-1, EphB4, CD40, VCAM-1, and VE-cadherin, and could represent a potential therapeutic target in tumors where it is highly expressed. ADAM9 belongs to a family of transmembrane, disintegrin-containing metalloproteinases involved in protein ectodomain shedding and cell-cell and cell-matrix interactions. ADAM-9 adhesive domain plays a role in regulating the motility of cells by interaction with beta1 integrins and modulates MMP synthesis.