LAMP2/CD107b Protein, Mouse (HEK293, His)

The LAMP2/CD107b protein is a lysosomal membrane glycoprotein critical for lysosomal biogenesis, pH regulation, and autophagy. As a direct inhibitor of TMEM175, LAMP2 promotes lysosomal acidification and optimizes hydrolase activity. LAMP2/CD107b Protein, Mouse (HEK293, His) is the recombinant mouse-derived LAMP2/CD107b protein, expressed by HEK293 , with C-His labeled tag. The total length of LAMP2/CD107b Protein, Mouse (HEK293, His) is 354 a.a., with molecular weight of 70-80 kDa.

LAMP2/CD107b protein, a lysosomal membrane glycoprotein, plays a crucial role in lysosome biogenesis, lysosomal pH regulation, and autophagy. Acting as a direct inhibitor of the proton channel TMEM175, LAMP2 facilitates lysosomal acidification, optimizing hydrolase activity. Additionally, it is a key regulator of chaperone-mediated autophagy, binding target proteins like GAPDH, NLRP3, and MLLT11, and guiding them for lysosomal degradation. Functioning downstream of chaperones such as HSPA8/HSC70, LAMP2 aids in the recruitment of substrate proteins to lysosomes. LAMP2 is vital for lysosomal protein degradation in response to starvation and is essential for the fusion of autophagosomes with lysosomes during autophagy. Its absence leads to impaired fusion and inefficient degradation of autophagic contents. Furthermore, LAMP2 contributes to MHCII-mediated presentation of exogenous antigens. Structurally, LAMP2 exists as a monomer and forms large homooligomers, interacting with proteins like HSPA8, HSP90, MLLT11, ABCB9, FURIN, and TMEM175 to execute its diverse cellular functions.

Mouse

HEK293

C-His

P17047 (L26-N379)

16784  [NCBI]

70-80 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.