Anti-Human CD107a (LAMP-1) – Biotin

Human adult adherent peripheral blood cells

This Biotinylated antibody is formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.4, 1% BSA and 0.09% sodium azide as a preservative.

Liquid

This biotinylated antibody is stable when stored at 2-8°C. Do not freeze.

Research Use Only

2 – 8° C Wet Ice

IHC,
IF,
WB,
IP,

H4A3 activity is directed against human LAMP-1 (CD107a).

Lysosomes are membrane-bound vacuoles that digest foreign materials and perform specialized autolysis functions¹. LAMP-1 is a lysosome-associated membrane glycoprotein¹ involved in lysosomal biogenesis, pH regulation, autophagy, and cholesterol homeostasis that also plays a role in natural killer (NK) cell cytotoxicity and protects NK cells from degranulation-associated damage induced by their own cytotoxic granule content². Additionally, LAMP-1 presents carbohydrate ligands to selectins and facilitates microbial infection of Lassa virus and Mumps virus via interactions with viral glycoprotein and fusion protein F, respectively. LAMP-1 is highly abundant in lysosomes and can be used as a maker to determine the amount and distribution of lysosomes³.

H4A3 was generated by immunizing Sprague Dawley rats with NIH/3T3 cells⁴. Spleen cells were fused with murine myeloma P3X653-Ag8 cells. The antibody was deposited in the Developmental Studies Hybridoma Bank when first developed.

LAMP-1 primarily localizes to the periphery of the lysosome and is a constituent of the lysosome membrane. LAMP1 is ubiquitously expressed in human tissues.

Galaptin

P11279

1 Chen JW, Murphy TL, Willingham MC, et al. J Cell Biol. 101(1):85-95. 1985.
2 https://www.uniprot.org/uniprotkb/P11279/entry
3 Jensen SS, Aaberg-Jessen C, Christensen KG, et al. Int J Clin Exp Pathol. 6(7):1294-1305. 2013.
4 Hughes EN, August JT. J Biol Chem. 256(2):664-671. 1981.
5 Piccolo P, Sabatino V, Mithbaokar P, et al. Mol Genet Genomic Med. 7(9):e844. 2019.
6 Yu T, Chung C, Shen D, et al. Hum Mol Genet. 21(14):3205-3214. 2012.
7 Sudhan DR, Siemann DW. Clin Exp Metastasis. 30(7):891-902. 2013.
8 Faron M, Fletcher JR, Rasmussen JA, et al. Infect Immun. 81(8):2800-2811. 2013.
9 Fernandes MC, Flannery AR, Andrews N, et al. Cell Microbiol. 15(6):977-991. 2013.
10 Chapel A, Kieffer-Jaquinod S, Sagné C, et al. Mol Cell Proteomics. 12(6):1572-1588. 2013.
11 Del Giudice MG, Ugalde JE, Czibener C. Infect Immun. 81(3):956-964. 2013.
12 Roset MS, García Fernández L, DelVecchio VG, et al. Infect Immun. 81(2):521-530. 2013.
13 Notte A, Ninane N, Arnould T, et al. Cell Death Dis. 4(5):e638. 2013.
14 McDonough JA, Newton HJ, Klum S, et al. mBio. 4(1):e00606-12. 2013.
15 Newton HJ, Kohler LJ, McDonough JA, et al. PLoS Pathog. 10(7):e1004286. 2014.
16 Kohler LJ, Reed ShC, Sarraf SA, et al. mBio. 7(4):e01127-16. 2016.
17 Byndloss MX, Tsai AY, Walker GT, et al. mBio. 10(4):e01538-19. 2019.
18 Chong A, Starr T, Finn CE, et al. Mol Microbiol. 112(4):1270-1283. 2019.
19 Yang Z, Funke BH, Cripe LH, et al. Circ Cardiovasc Genet. 3(2):129-137. 2010.
20 Torres AG, Fabani MM, Vigorito E, et al. Nucleic Acids Res. 40(5):2152-2167. 2012.
21 Bekier ME 2nd, Wang L, Li J, et al. Mol Biol Cell. 28(21):2833-2842. 2017.