Abcam, ab213784, Human Galectin-3BP ELISA Kit

Size: 1 x 96Tests
Human Galectin-3BP ELISA Kit is a Sandwich (quantitative) ELISA for the measurement of Human Galectin-3BP in Human in Cell Culture Media, Biofluids samples.
Key facts
Detection method:Colorimetric,
Sample types:Cell culture supernatant, Heparin Plasma, Serum,
Reacts with:Human,
Assay type:Sandwich (quantitative),
Sensitivity:< 10 pg/mL,
Range:156 - 10000 pg/mL,
Assay time:3h 30m,
Assay Platform:Pre-coated microplate (12 x 8 well strips)

Product details:
The Human Galectin-3BP Enzyme-Linked Immunosorbent Assay (ELISA) kit (ab213784) is designed for the quantitative measurement of Human Galectin-3BP in cell culture supernatants, serum and plasma (heparin).
The ELISA kit is based on standard sandwich enzyme-linked immune-sorbent assay technology. A monoclonal antibody from mouse specific for Galectin-3BP has been pre-coated onto 96-well plates. Standards (NSO; V19-D585) and test samples are added to the wells, a biotinylated detection monoclonal antibody from mouse specific for Galectin-3BP is added subsequently and then followed by washing with PBS or TBS buffer. Avidin-Biotin-Peroxidase Complex is added and unbound conjugates are washed away with PBS or TBS buffer. HRP substrate TMB is used to visualize HRP enzymatic reaction. TMB is catalyzed by HRP to produce a blue color product that changed into yellow after adding acidic stop solution. The density of yellow is proportional to the Human Galectin-3BP amount of sample captured in plate.
Galectin-3-binding protein is a protein that in humans is encoded by the LGALS3BP gene. The galectins are a family of beta-galactoside-binding proteins implicated in modulating cell–cell and cell–matrix interactions. Using fluorescence
in situ
hybridization, the full length 90K cDNA has been localized to chromosome 17q25. The native protein binds specifically to a human macrophage associated lectin known as Mac-2 and also binds to galectin 1.

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information--20°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
LGALS3BP also known as Galectin-3-binding protein (Mac-2 binding protein 90K) is a multifaceted glycoprotein with a mass of approximately 90 kDa. It typically interacts with galectins especially galectin-3 and is known for its adhesive properties. Researchers frequently observe it in various tissues including epithelial cells immune cells and in the extracellular matrix highlighting its involvement across different biological functions.
Biological function summary
The LGALS3BP glycoprotein modulates cell-cell and cell-matrix interactions. It does not operate alone; researchers have identified its presence in multiple complexes impacting several cellular processes such as immune modulation cell adhesion and migration. LGALS3BP can affect the immune response by influencing T-cell and natural killer cell activities which can alter the body's defense against pathogens and tumors.
Pathways
LGALS3BP significantly influences the signaling pathways involved with immune function and cellular adhesion. It plays an important role in the galectin pathway where it interacts with galectin-3 contributing to processes like cell growth and apoptosis. Additionally it affects the integrin-mediated signaling pathway enhancing cell adhesion and motility which is vital for cell migration and signaling dynamics. These interactions involve proteins such as integrins and other adhesion molecules that influence cellular communication and structural integrity.
LGALS3BP is strongly linked to cancer and inflammation-related conditions. Its overexpression is correlated with tumor progression and metastasis as seen in various cancers such as breast and colorectal cancer. LGALS3BP modulates its effects by interacting with galectin-3 influencing tumor-immune escape mechanisms and promoting tumor growth. Further its role in inflammatory disorders suggests it contributes to pathological processes through interactions with proteins that mediate inflammation and immune response.