Recombinant Human LAMP1/CD107a (C-Fc)
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Amount : | 50 µg |
Content : | Lyophilized from a 0.2 µm filtered solution of 20mM PB,150mM NaCl,pH7.4. |
AA sequence : | Recombinant Human LAMP1 is produced by our Mammalian expression system and the target gene encoding Ala29-Met382 is expressed with a Fc tag at the C-terminus. |
Alternative Name : | Lysosome-Associated Membrane Glycoprotein 1, LAMP-1, Lysosome-Associated Membrane Protein 1, CD107 Antigen-Like Family Member A, CD107a, LAMP1 |
Source : Human Cells;
Lysosome-Associated Membrane Glycoprotein 1 (LAMP1) is a single-pass type I membrane protein belonging to the LAMP family. LAMP1 is expressed largely in the endosome-lysosome membranes of cells.It shuttles between lysosomes, endosomes, and the plasma membrane. LAMP1 functions to present carbohydrate ligands to selectins and it has also been implicated in tumor cell metastasis. It has been proposed LAMP1 can be used as a therapeutic agent for certain cancers, as well as a marker for lysosomal storage disorders and degranulation on lymphocytes such as CD8+ and NK cells. Cell surface LAMP1 and LAMP2 have been shown to promote adhesion of human peripheral blood mononuclear cells(PBMC) to vascular endothelium, therefore they are possibly involved in the adhesion of PBMCs to the site of inflammation.
Lysosome-Associated Membrane Glycoprotein 1 (LAMP1) is a single-pass type I membrane protein belonging to the LAMP family. LAMP1 is expressed largely in the endosome-lysosome membranes of cells.It shuttles between lysosomes, endosomes, and the plasma membrane. LAMP1 functions to present carbohydrate ligands to selectins and it has also been implicated in tumor cell metastasis. It has been proposed LAMP1 can be used as a therapeutic agent for certain cancers, as well as a marker for lysosomal storage disorders and degranulation on lymphocytes such as CD8+ and NK cells. Cell surface LAMP1 and LAMP2 have been shown to promote adhesion of human peripheral blood mononuclear cells(PBMC) to vascular endothelium, therefore they are possibly involved in the adhesion of PBMCs to the site of inflammation.
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