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- BD OMICS-Guard Sample Preservation Buffer
- BD Rhapsody™ ATAC-Seq Assays
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Profile of activated platelets analyzed on a FACScan (BDIS, San Jose, CA)
Flow cytometric analysis of CD107a expression in Jurkat cells. Jurkat cells were fixed with BD Cytofix™ Fixation Buffer (Cat. No. 554655) and were then washed and stained in BD Perm/Wash™ Buffer (Cat. No. 554723) with either FITC Mouse IgG1, κ Isotype Control (Cat. No. 555748; dashed line histogram) or FITC Mouse Anti-Human CD107a antibody (Cat. No. 555800/560949; solid line histogram). The fluorescence histogram showing CD107a expression (or Ig Isotype control staining) was derived from gated events with the forward and side light-scatter characteristics of intact Jurkat cells. Flow cytometry and data analysis were performed using a BD LSRFortessa™ Cell Analyzer System and FlowJo™ software.
BD Pharmingen™ FITC Mouse Anti-Human CD107a
BD Pharmingen™ FITC Mouse Anti-Human CD107a
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권장 분석 절차
BD® CompBeads can be used as surrogates to assess fluorescence spillover (Compensation). When fluorochrome conjugated antibodies are bound to BD® CompBeads, they have spectral properties very similar to cells. However, for some fluorochromes there can be small differences in spectral emissions compared to cells, resulting in spillover values that differ when compared to biological controls. It is strongly recommended that when using a reagent for the first time, users compare the spillover on cells and BD® CompBeads to ensure that BD® CompBeads are appropriate for your specific cellular application.
제품 고시
- This reagent has been pre-diluted for use at the recommended Volume per Test. We typically use 1 × 10^6 cells in a 100-µl experimental sample (a test).
- An isotype control should be used at the same concentration as the antibody of interest.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- For fluorochrome spectra and suitable instrument settings, please refer to our Multicolor Flow Cytometry web page at www.bdbiosciences.com/colors.
- Please refer to http://regdocs.bd.com to access safety data sheets (SDS).
The H4A3 monoclonal antibody specifically binds to CD107a which is also known as Lysosomal-associated membrane protein 1 (LAMP-1). LAMP-1 is a ~110 kDa type I transmembrane protein that is heavily glycosylated and widely expressed by cells primarily on the luminal surface of their lysosomes. It is also expressed on the surface of activated platelets, activated lymphocytes, cytotoxic T cells and NK cells, and some tumor cell lines, including U937 and KG1a. LAMP-1 can serve as a ligand for E-selectin-mediated cell adhesion. LAMP-1 and LAMP-2 (CD107b) are carriers for poly-N-acetyllactosamines and are able to display sialyl Le[x] termini.
This antibody is routinely tested by flow cytometric analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.
개발 참고 자료 (10)
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Alto NM, Soderling J, Scott JD. Rab32 is an A-kinase anchoring protein and participates in mitochondrial dynamics. J Biol Chem. 2002; 158(4):659-668. (Biology). 참조 보기
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Chen JW, Cha Y, Yuksel KU, Gracy RW, August JT. Isolation and sequencing of a cDNA clone encoding lysosomal membrane glycoprotein mouse LAMP-1. Sequence similarity to proteins bearing onco-differentiation antigens. J Biol Chem. 1988; 263(18):8754-8758. (Biology). 참조 보기
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Febbraio M, Silverstein RL. Identification and characterization of LAMP-1 as an activation-dependent platelet surface glycoprotein. J Biol Chem. 1990; 265(30):18531-18537. (Biology). 참조 보기
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Fukuda M, Viitala J, Matteson J, Carlsson SR. Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Comparison of their deduced amino acid sequences. J Biol Chem. 1988; 263(35):18920-18928. (Biology). 참조 보기
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Fukuda M. Lysosomal membrane glycoproteins. Structure, biosynthesis, and intracellular trafficking. J Biol Chem. 1991; 266(32):21327-21330. (Biology). 참조 보기
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Hocking DC, Kowalski K. A cryptic fragment from fibronectin's III1 module localizes to lipid rafts and stimulates cell growth and contractility. J Cell Biol. 2002; 158(1):175-184. (Biology). 참조 보기
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Mane SM, Marzella L, Bainton DF, et al. Purification and characterization of human lysosomal membrane glycoproteins. Arch Biochem Biophys. 1989`; 268(1):360-378. (Immunogen: Electron microscopy, Flow cytometry, Immunoaffinity chromatography, Immunohistochemistry, Immunoprecipitation). 참조 보기
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Sawada R, Lowe JB, Fukuda M. E-selectin-dependent adhesion efficiency of colonic carcinoma cells is increased by genetic manipulation of their cell surface lysosomal membrane glycoprotein-1 expression levels. J Biol Chem. 1993; 268(17):12675-12681. (Biology). 참조 보기
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Schlossman SF. Stuart F. Schlossman .. et al., ed. Leucocyte typing V : white cell differentiation antigens : proceedings of the fifth international workshop and conference held in Boston, USA, 3-7 November, 1993. Oxford: Oxford University Press; 1995.
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Spoerl Z, Stumpf M, Noegel AA, Hasse A. Oligomerization, F-actin interaction, and membrane association of the ubiquitous mammalian coronin 3 are mediated by its carboxyl terminus. J Biol Chem. 2002; 277(50):48858-48867. (Biology: Blocking). 참조 보기
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