LAMP-2 antibody cross reacts with LAMP2B and LAMP2C, but not LAMP2A.
Aufreinigung
LAMP-2 Antibody is affinity chromatography purified via peptide column.
Immunogen
LAMP-2 antibody was raised against a 17 amino acid synthetic peptide from near the carboxy terminus of human LAMP-2. The immunogen is located within the last 50 amino acids of LAMP-2.
LAMP2
Reaktivität: Human
FACS
Wirt: Maus
Monoclonal
H4B4
FITC
Applikationshinweise
LAMP-2 antibody can be used for the detection of LAMP-2 by Western blot at 1 - 2 μ,g/mL. Antibody can also be used for immunocytochemistry starting at 10 μ,g/mL and immunohistochemistry starting at 5 μ,g/mL.
Antibody validated: Western Blot in human samples, Immunohistochemistry in mouse samples and Immunocytochemistry in human samples. All other applications and species not yet tested.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Konzentration
1 mg/mL
Buffer
LAMP-2 Antibody is supplied in PBS containing 0.02 % sodium azide.
Konservierungsmittel
Sodium azide
Vorsichtsmaßnahmen
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung
-20 °C,4 °C
Informationen zur Lagerung
LAMP-2 antibody can be stored at 4°C for three months and -20°C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Target
LAMP2
(Lysosomal-Associated Membrane Protein 2 (LAMP2))
LAMP-2 Antibody: Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components and is negatively regulated by TOR (Target of rapamycin). LAMP-2, a highly glycosylated protein associated with the lysosome, has recently been shown to be important in autophagy as mice deficient in this protein failed to convert autophagic vacuoles into vacuoles leading to impaired degradation of long-lived proteins. This correlates with the finding that human LAMP-2 deficiency causing Danon's disease is associated with the accumulation of autophagic material in striated myocytes. LAMP-2 exists in multiple isoforms.