LAMP-1 Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P, IF, E |
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Primary Accession | P11279 |
Other Accession | NP_005552, 3916 |
Reactivity | Human, Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | IgG |
Calculated MW | Predicted: 46 kDa Observed: 100 kDa |
Application Notes | LAMP-1 antibody can be used for the detection of LAMP-1 by Western blot at 1 - 2 μg/mL. Antibody can also be used for immunohistochemistry starting at 2.5 μg/mL. For immunofluorescence start at 20 μg/mL. |
Gene ID | 3916 |
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Other Names | LAMP-1 Antibody: LAMPA, CD107a, LGP120, Lysosome-associated membrane glycoprotein 1, CD107 antigen-like family member A, LAMP-1, lysosomal-associated membrane protein 1 |
Target/Specificity | LAMP-1 antibody was raised against a 15 amino acid synthetic peptide from near the center of human LAMP-1. The immunogen is located within amino acids 230 - 280 of LAMP-1. |
Reconstitution & Storage | LAMP-1 antibody can be stored at 4℃ for three months and -20℃, 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. |
Precautions | LAMP-1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | LAMP1 {ECO:0000303|PubMed:23632890, ECO:0000312|HGNC:HGNC:6499} |
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Function | Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, lysosomal pH regulation, autophagy and cholesterol homeostasis (PubMed:37390818). Acts as an important regulator of lysosomal lumen pH regulation by acting as a direct inhibitor of the proton channel TMEM175, facilitating lysosomal acidification for optimal hydrolase activity (PubMed:37390818). Also plays an important role in NK-cells cytotoxicity (PubMed:2022921, PubMed:23632890). Mechanistically, participates in cytotoxic granule movement to the cell surface and perforin trafficking to the lytic granule (PubMed:23632890). In addition, protects NK-cells from degranulation-associated damage induced by their own cytotoxic granule content (PubMed:23847195). Presents carbohydrate ligands to selectins (PubMed:7685349). |
Cellular Location | Lysosome membrane; Single-pass type I membrane protein. Endosome membrane; Single- pass type I membrane protein. Late endosome membrane; Single-pass type I membrane protein. Cell membrane; Single-pass type I membrane protein. Cytolytic granule membrane; Single-pass type I membrane protein. Note=This protein shuttles between lysosomes, endosomes, and the plasma membrane (By similarity). Colocalizes with OSBPL1A at the late endosome (PubMed:16176980). {ECO:0000250|UniProtKB:P05300, ECO:0000269|PubMed:16176980, ECO:0000269|PubMed:17897319} |
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Provided below are standard protocols that you may find useful for product applications.
Background
LAMP-1 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). A protein recently found to be involved in autophagy, LAMP-2, is a highly glycosylated protein associated with the lysosome. LAMP-1 shares much homology to LAMP-2 and is thought to have overlapping functions. Mice lacking LAMP-1 had very minor defects compared to those deficient in LAMP-2 expression. However, the loss of both proteins resulted in embryonic lethality, suggesting that each protein possesses some unique and necessary functions.
References
Gozuacik D and Kimchi A. Autophagy as a cell death and tumor suppressor mechanism. Oncogene. 2004; 23:2891-906.
Kisen GO, Tessitore L, Costelli P, et al. Reduced autophagic activity in primary rat hepatocellular carcinoma and ascites hepatoma cells. Carcinogenesis1993; 14:2501-5.
Kamada Y, Funakoshi T, Shintani T, et al. Tor-mediated induction of autophagy via Apg1 protein kinase complex. J. Cell. Biol. 2000; 150:1507-13.
Chen JW, Murphy TL, Willingham MC, et al. Identification of two lysosomal membrane glycoproteins. J. Cell Biol. 1985; 101:85-95.
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