Mouse CD107a Monoclonal Antibody | anti-CD107a antibody

Anti-Hu CD107a Alexa Fluor488

• Gene Names: LAMP1; LAMPA; CD107a; LGP120
• Reactivity: Human, Non-human primates, Mouse
• Applications: Flow Cytometry, Functional Assay, Western Blot, Immunocytochemistry
• Purity: The purified antibody is conjugated with Alexa Fluor488 under optimum conditions. The conjugate is purified by size-exclusion chromatography.
• Synonyms: CD107a; Monoclonal Antibody; Anti-Hu CD107a Alexa Fluor488; LAMP-1; LAMPA; lysosomal associated membrane protein 1; anti-CD107a antibody

• Host: Mouse
• Reactivity: Human, Non-human primates, Mouse
• Clonality: Monoclonal
• Isotype: Mouse IgG1 kappa
• Clone Number: H4A3
• Specificity: The mouse monoclonal antibody H4A3 recognizes an extracellular/luminal epitope of CD107a, an approximately 100-120kDa glycoprotein expressed mainly on lysosomal, but also on the plasma membrane.
• Purity/Purification: The purified antibody is conjugated with Alexa Fluor488 under optimum conditions. The conjugate is purified by size-exclusion chromatography.
• Form/Format: Stabilizing phosphate buffered saline (PBS) solution containing 15mM sodium azide

• Applicable Applications for anti-CD107a antibody: Flow Cytometry (FC/FACS) (QC tested), Western Blot (WB), Immunocytochemistry (ICC)
• Application Notes: FC/FACS: The reagent is designed for analysis of human blood cells using 4ul reagent/100ul of whole blood or 10⁶ cells in a suspension. The content of a vial (0.4 ml) is sufficient for 100 tests. Intracellular and extracellular staining.
• Conjugation: Alexa Fluor488
• Immunogen: Human PBMC
• Preparation and Storage: Store in the dark at 2-8 degree C. Do not freeze. Avoid prolonged exposure to light. Do not use after expiration date stamped on vial label.

Flow Cytometry (FC/FACS)

(Flow cytometry analysis (intracellular staining) of human peripheral blood cells with anti-CD107a (H4A3) Alexa Fluor 488.)

Related Product Information for anti-CD107a antibody

CD107a (lysosome-associated membrane protein-1, LAMP-1), together with LAMP-2, is a major constituent of lysosomal membrane, 1-2% of total CD107a is found also on the plasma membrane. The LAMP proteins are involved in lysosome biogenesis and are required for fusion of lysosomes with phagosomes. Increased CD107a immunoreactivity is observed in neurones, and in glial cells surrounding senile plaques in Alzheimers disease cases and is localized mainly in medullary epithelial cells, single macrophages and lymphocytes in acute thymic involution. CD107a is a good marker of mast cell activation.

References

*Majer F, Vlaskova H, Krol L, Kalina T, Kubanek M, Stolnaya L, Dvorakova L, Elleder M, Sikora J: Danon disease: a focus on processing of the novel LAMP2 mutation and comments on the beneficial use of peripheral white blood cells in the diagnosis of LAMP2 deficiency. Gene. 2012 May 1;498(2):183-95., URL: http://www.ncbi.nlm.nih.gov/pubmed/term=majer+f+v,*Mao H, Tu W, Liu Y, Qin G, Zheng J, Chan PL, Lam KT, Peiris JS, Lau YL: Inhibition of human natural killer cell activity by influenza virions and hemagglutinin. J Virol. 2010 May;84(9):4148-57., URL: http://www.ncbi.nlm.nih.gov/pubmed/20164232,*Yu CI, Gallegos M, Marches F, Zurawski G, Ramilo O, García-Sastre A, Banchereau J, Palucka AK: Broad influenza-specific CD8+ T-cell responses in humanized mice vaccinated with influenza virus vaccines. Blood. 2008 Nov 1;112(9):3671-8., URL: https://www.ncbi.nlm.nih.gov/pubmed/18713944,*Tomescu C, Chehimi J, Maino VC, Montaner LJ: NK cell lysis of HIV-1-infected autologous CD4 primary T cells: requirement for IFN-mediated NK activation by plasmacytoid dendritic cells. J Immunol. 2007 Aug 15;179(4):2097-104., URL: https://www.ncbi.nlm.nih.gov/pubmed/17675468,*Carlsten M, Björkström NK, Norell H, Bryceson Y, van Hall T, Baumann BC, Hanson M, Schedvins K, Kiessling R, Ljunggren HG, Malmberg KJ: DNAX accessory molecule-1 mediated recognition of freshly isolated ovarian carcinoma by resting natural killer cells. Cancer Res. 2007 Feb 1;67(3):1317-25., URL: https://www.ncbi.nlm.nih.gov/pubmed/17283169,*Marcenaro S, Gallo F, Martini S, Santoro A, Griffiths GM, Aricó M, Moretta L, Pende D: Analysis of natural killer-cell Functional Application (FUNC)tion in familial hemophagocytic lymphohistiocytosis (FHL): defective CD107a surface expression heralds Munc13-4 defect and discriminates between genetic subtypes of the disease. Blood. 2006 Oct 1;108(7):2316-23., URL: https://www.ncbi.nlm.nih.gov/pubmed/16778144,*Deetz CO, Hebbeler AM, Propp NA, Cairo C, Tikhonov I, Pauza CD: Gamma interferon secretion by human Vgamma2Vdelta2 T cells after stimulation with antibody against the T-cell receptor plus the Toll-Like receptor 2 agonist Pam3Cys. Infect Immun. 2006 Aug;74(8):4505-11., URL: https://www.ncbi.nlm.nih.gov/pubmed/16861636,*Furuta K, Ikeda M, Nakayama Y, Nakamura K, Tanaka M, Hamasaki N, Himeno M, Hamilton SR, August JT: Expression of lysosome-associated membrane proteins in human colorectal neoplasms and inflammatory diseases. Am J Pathol. 2001 Aug;159(2):449-55., URL: https://www.ncbi.nlm.nih.gov/pubmed/11485903,*Mane SM, Marzella L, Bainton DF, Holt VK, Cha Y, Hildreth JE, August JT: Purification and characterization of human lysosomal membrane glycoproteins. Arch Biochem Biophys. 1989 Jan;268(1):360-78., URL: https://www.ncbi.nlm.nih.gov/pubmedterm=mane%20sm
*Grützkau A, Smorodchenko A, Lippert U, Kirchhof L, Artuc M, Henz BM: LAMP-1 and LAMP-2, but not LAMP-3, are reliable markers for activation-induced secretion of human mast cells. Cytometry A. 2004 Sep;61(1):62-8., URL: https://www.ncbi.nlm.nih.gov/pubmed/15351990ordin,*Barrachina M, Maes T, Buesa C, Ferrer I: Lysosome-associated membrane protein 1 (LAMP-1) in Alzheimer's disease. Neuropathol Appl Neurobiol. 2006 Oct;32(5):505-16., URL: https://www.ncbi.nlm.nih.gov/pubmed/16972884ordin,*Sarafian VS, Marinova TT: Lysosomal membrane-associated glycoproteins are differentially expressed in acute and chronic human thymic involution. Acta Biol Hung. 2006 Sep;57(3):315-22., URL: https://www.ncbi.nlm.nih.gov/pubmed/17048695ordin,*Eskelinen EL: Roles of LAMP-1 and LAMP-2 in lysosome biogenesis and autophagy. Mol Aspects Med. 2006 Oct-Dec;27(5-6):495-502., URL: https://www.ncbi.nlm.nih.gov/pubmed/16973206ordin,*Hunyh KK, Eskelinen EL, Scott CC, Malevanets A, Saftig P, Grinstein S: LAMP proteins are required for fusion of lysosomes with phagosomes. EMBO J. 2007 Jan 24;26(2):313-24., URL: https://www.ncbi.nlm.nih.gov/pubmed/17245426ordin

NCBI and Uniprot Product Information

• NCBI GI #: 112380628
• NCBI GeneID: 3916
• NCBI Accession #: NP_005552.3
• NCBI GenBank Nucleotide #: NM_005561.3
• UniProt Accession #: P11279; Q8WU33; Q96I40; Q9BRD2; Q9NP13
• Molecular Weight: 44,882 Da
• NCBI Official Full Name: lysosome-associated membrane glycoprotein 1
• NCBI Official Synonym Full Names: lysosomal-associated membrane protein 1
• NCBI Official Symbol: LAMP1
• NCBI Official Synonym Symbols: LAMPA; CD107a; LGP120
• NCBI Protein Information: lysosome-associated membrane glycoprotein 1; LAMP-1; CD107 antigen-like family member A; lysosome-associated membrane protein 1
• UniProt Protein Name: Lysosome-associated membrane glycoprotein 1
• UniProt Gene Name: LAMP1
• UniProt Synonym Gene Names: LAMP-1
• UniProt Entry Name: LAMP1_HUMAN

NCBI Description

The protein encoded by this gene is a member of a family of membrane glycoproteins. This glycoprotein provides selectins with carbohydrate ligands. It may also play a role in tumor cell metastasis. [provided by RefSeq, Jul 2008]

Uniprot Description

LAMP1: Presents carbohydrate ligands to selectins. Also implicated in tumor cell metastasis. Belongs to the LAMP family.

Protein type: Membrane protein, integral

Chromosomal Location of Human Ortholog: 13q34

Cellular Component: integral to plasma membrane; lysosome; dendrite; multivesicular body; membrane; cell soma; late endosome; cytoplasm; melanosome; plasma membrane; endosome membrane; sarcolemma; external side of plasma membrane

Molecular Function: protein domain specific binding; protein binding; enzyme binding

Biological Process: positive regulation of natural killer cell degranulation; induction of apoptosis by granzyme; protein stabilization; viral reproduction; autophagic cell death; autophagy; positive regulation of natural killer cell mediated cytotoxicity