Anti-Legumain Magnetic Beads-IP Kit Product Components
Components | Storage |
Anti-Legumain Magnetic Beads1,3 | 2-8℃ for 12 months |
NP40 Cell Lysis Buffer2 | -20℃ for 12 months |
5×TBST(pH7.4) | |
1×TBST(pH7.4) | |
ddH2O | |
CD166 Positive Cell Lysate | -20℃ for 12 months |
Alkaline Elution Buffer | 2-8℃ for 12 months |
Acidity Elution Buffer | 2-8℃ for 12 months |
Neutralization Buffer | 2-8℃ for 12 months |
[1] The IP KIT contains anti-Legumain magnetic Beads (2 mg/mL) in phosphate buffered saline (PBS, pH 7.4) with sodium azide (0.1%).
[2] Using NP-40 cell lysate buffer in the kit is required,otherwise,the magnetic beads may be precipitated.
[3] Shipping: Magnetic Beads kits are shipped at ambient temperature in which magnetic beads are provided in liquid buffer.
Anti-Legumain Magnetic Beads-IP Kit Product Description
The Anti-Legumain magnetic Beads, conjugated with Anti-Legumain antibody, are used for immuneprecipitation (IP) of Legumain proteins which expressed in vitro expression systems. For IP, the beads are added to a sample containing Legumain proteins to form a bead-protein complex. The complex is removed from the solution manually using a magnetic separator. The bound Legumain proteins are dissociated from the magnetic beads using an elution buffer. Anti-Legumain Magnetic Beads-IP Kit Antibody Information
Immunogen
Recombinant Sus scrofa (Pig) Legumain / LGMN Protein (Catalog#62001-W08H)
Species Reactivity
Sus scrofa (Pig) Legumain / LG
Source
Polyclonal Sus scrofa (Pig) Rabbit IgG
Preparation
Produced in rabbits immunized with purified, recombinant Sus scrofa (Pig) Legumain / LGMN (Catalog#62001-W08H; XP_001927117.4; Met1-Tyr433). Legumain / LGMN specific IgG was purified by Sus scrofa (Pig) Legumain / LGMN affinity chromatography.
Applications
Immunoprecipitation (IP), Minimum Protein Purification
Legumain Background Information
The Mammalian Legumain, also known as LGMN, also called asparaginyl endopeptidase (AEP), is a cysteine protease belonging to peptidase family C13 with a strict specificity for hydrolysis of asparaginyl bonds. Known previously only from plants and invertebrates, Legumain is discovered as a lysosomal endopeptidase in mammals. Mammalian Legumain is a cysteine endopeptidase, inhibited by iodoacetamide and maleimides, but unaffected by compound E64. The Mammalian Legumain is involved in the processing of bacterial peptides and endogenous proteins for MHC class II presentation in the lysosomal/endosomal systems. Legumain has been observed to be highly expressed in several types of solid tumors. It was demonstrated in membrane-associated vesicles concentrated at the invadopodia of tumor cells and on cell surfaces where it colocalized with integrins. Legumain was demonstrated to activate progelatinase A. Cells overexpressing Legumain possessed increased migratory and invasive activity in vitro and adopted an invasive and metastatic phenotype in vivo, inferring significance of Legumain in tumor invasion and metastasis. In addition, Legumain is expressed in both murine and human atherosclerotic lesions. The macrophage-specific expression of Legumain in vivo and ability of Legumain to induce chemotaxis of monocytes and endothelial cells in vitro suggest that Legumain may play a functional role in atherogenesis.
References
Schwarz G, et al. (2002) Characterization of legumain. Biol Chem. 383(11): 1813-6. Liu C, et al. (2003) Overexpression of legumain in tumors is significant for invasion/metastasis and a candidate enzymatic target for prodrug therapy. Cancer Res. 63(11): 2957-64. Murthy RV, et al. (2005) Legumain expression in relation to clinicopathologic and biological variables in colorectal cancer. Clin Cancer Res. 11(6): 2293-9. Gawenda J, et al. (2007) Legumain expression as a prognostic factor in breast cancer patients. Breast Cancer Res Treat. 102(1): 1-6. Clerin V, et al. (2007) Expression of the cysteine protease legumain in vascular lesions and functional implications in atherogenesis. Atherosclerosis. 201(1): 53-66. Lew?“n S, et al. (2008) A Legumain-based minigene vaccine targets the tumor stroma and suppresses breast cancer growth and angiogenesis. Cancer Immunol Immunother. 57(4): 507-15.