CD107a Antibody [H4A3] (PE) | 99-601

CD107a Antibody [H4A3] (PE) | 99-601 | Gentaur UK, US & Europe Distribution

Host: Mouse

Reactivity: Human, Rhesus, African Green Monkey, Pigtail Macaque, Sooty Mangabey

Homology: N/A

Immunogen: Human adherent peripheral blood cells

Research Area: Innate Immunity

Tested Application: IHC-Fr, Flow, Blocking, IP, Depletion, Complement Mediated Cell Depletion

Application: CD107a Antibody [H4A3] for use in flow cytometry assays.

Specificiy: CD107a

Positive Control 1: N/A

Positive Control 2: N/A

Positive Control 3: N/A

Positive Control 4: N/A

Positive Control 5: N/A

Positive Control 6: N/A

Molecular Weight: N/A

Validation: N/A

Isoform: N/A

Purification: N/A

Clonality: Monoclonal

Clone: [H4A3]

Isotype: IgG1

Conjugate: PE

Physical State: Liquid

Buffer: Supplied in PBS/NaN3 and a stabilizing agent

Concentration: Lot specific

Storage Condition: Store vial at 2-8˚C

Alternate Name: LAMP-1, lysosome-associated membrane protein 1

User Note: Optimal dilutions for each application to be determined by the researcher.

BACKGROUND: CD107a, also known as lysosomal-associated membrane protein 1 (LAMP-1) , is a heavily glycosylated type I transmembrane protein that constitutes the major sialoglycoproteins on lysosomal membranes. It is a ligand for galaptin, an S-type lectin present in extracellular matrix, through its recognition of acetyllactosamine oligosaccharide chains, and is a ligand for E-selectin-mediated cell adhesion. CD107a is expressed by activated T cells, macrophages, dendritic cells, activated platelets, tonsillar epithelium, and some tumor cell lines, including U937 and KG1a. It is also a widely expressed intracellular antigen. LAMP-1 may function in protecting the inner surface of the lysosomal membrane by forming a barrier to lysosomal hydrolases. The upregulation of both CD107a and CD107b on the surface of tumor cell lines has been associated with their enhanced metastatic potential where they may increase adhesion to extracellular matrix and endothelium.