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LAMP2A antibody - 437 005 K.D.

LAMP2A is a glycoprotein of the lysosomal membrane involved in chaperone-mediated autophagy
Guinea pig polyclonal purified antibody
Cat. No.: 437 005
Amount: 50 µg
Price: $460.00
Cat. No. 437 005 50 µg specific antibody, lyophilized. Affinity purified with the immunogen. Albumin and azide were added for stabilization. For reconstitution add 50 µl H2O to get a 1mg/ml solution in PBS. Then aliquot and store at -20°C to -80°C until use.
Applications
 
WB: 1 : 1000 (AP staining) gallery  
IP: not tested yet
ICC: 1 : 500 gallery  
IHC: not tested yet
IHC-P: 1 : 400 gallery  
Immunogen Synthetic peptide corresponding to AA 406 to 415 from mouse LAMP2A (UniProt Id: P17047-1)
Reactivity Reacts with: mouse (P17047-1), rat (P17046-1).
No signal: human (P13473-1).
Other species not tested yet.
Specificity K.D. validated
Data sheet 437_005.pdf
Cat. No.: 437 005
Amount: 50 µg
Price: $460.00
Background

LAMP2 (lysosomal-associated membrane protein 2), also referred to as CD107b, is a member of the LAMP protein family and a highly glycosylated single-pass type I transmembrane protein. It shuttles between lysosomes, endosomes, and the plasma membrane.

LAMP2 exists in three isoforms. Isoform LAMP2A is expressed for instance in liver, kidney, and placenta, and only low in brain.

LAMP2 proteins protect the lysosomal membrane from degradation by lysosomal hydrolases and participate in intracellular cholesterol trafficking, lysosomal biogenesis, and lysosomal motility along microtubules. In addition to these common functions, the different splice variants of LAMP2 have also specialized functions. LAMP2A serves as a receptor for cytosolic proteins that undergo degradation via chaperone-mediated autophagy (CMA). It facilitates the translocation of targeted proteins and peptides into the lysosome. LAMP2A is also implicated in MHCII presentation of cytoplasmic antigens as well as in the regulation of T-cell responses. Beyond that, LAMP2A is the rate-limiting factor for the neuronal uptake and degradation of aggregation prone proteins via CMA such as α-synuclein and huntingtin that are neurotoxic when aggregated.

Recent studies demonstrated that LAMP2A is involved in cancer progression by promoting tumor growth.