Shared Resources
Shared Resources

Laser Capture Microdissection 
Director: Munir Alam, PhD

Shared Resource Summary:

The Laser Capture Microdissection Shared Resource is led by Munir Alam, PhD and is located in the Medical Sciences Research Building II.  The laser capture microscope allows for microdissection of small regions of interest within a slide-mounted tissue section, down to a single cell. Molecules, such as RNA or protein, can then be isolated from the target cells.

Personnel/Contact Information:

Director: S. Munir Alam, PhD
Office Phone: (919) 668-6372
Lab Phone: (919) 668-6995
Fax: (919) 684-5380
Email: alam0004@mc.duke.edu
Manager: Shelley Stewart 
Lab Phone: (919) 668-6995
Fax: (919) 684-5380
Email: shelley.stewart@duke.edu
 
Location: 4042-4044 MSRB II, DUMC Box 103020, Durham, NC 27710
 

Getting Started:

  1. Please see the Common Tools sidebar to register to use facilities, or request a job, and to retrieve data. 

  2. Please schedule a consultation meeting and fill out the request for job form.

  3. For a schedule of fees for services, please contact DHVI Shared Resources business office.

Facilities and Instruments:

  • Arcturus Autopix (photo)

Services Provided:

  • Laser capture microdissection

Protocols and Methods:

(in development)

Affiliated Centers:

  • Center for HIV-AIDS Vaccine Immunology (www.chavi.org)
  • Collaboration for AIDS Vaccine Discovery (CAVD)- Bill and Melinda Gates Foundation (www.cavd.com)

Publications:

2006-2008
 
Liao et al. A group M consensus envelope glycoprotein induces antibodies that neutralize susbsets of subtype B and C HIV-1 primary viruses. Virology, 2006; 353(2):268-282.

Yu et al. Detection of Ebola virus envelope using monoclonal and polyclonal antibodies in ELISA, surface plasmon resonance and a quartz crystal microbalance immunosensor.  J. Virol Methods. 2006; 137(2):219-228.
 
Dennison et al., Neuronal SNAREs do ot trigger fusion between synthetic membranes but do promote PEG-mediated membrane fusion. Biophys. J. 2006, 90(5):1661-1675.
 
Lam et al.  Using microcantilever defelction to detect HIV-1 envelope glycoprotein gp120. Nanomedicine: Nanotechnology, Biology and Medicine. 2006, 2(4):222-229.
 
Alam et al. The Role of Antibody Polyspecificity and Lipid Reactivity in Binding of Broadly Neutralizing anti-HIV-1 Envelope Human Monoclonal Antibodies 2F5 and 4E10 to gp41 Membrane Proximal Envelope epitopes. J. Immunol. 2007, 178:4424-4435.
 
Staats et al. In Vitro and in vivo characterization of Anthrax anti-protective antigen and anti-lethal factor monoclonal antibodies after passive transfer in a mouse lethal toxin challenge model to define correlates of immunity. Infect. Immun., 2007, 75:5443-5442.
 
Wang et al., Incorporation of high levels of chimeric human immunodeficiency virus envelope glycoporteins into virus-like particles. J. Virol., 2007, 81(20):10869-78.
 
Alam, S.M. et al. Human Immunodeficiency Virus Type 1 gp41 antibodies that mask membrane proximal region epitopes: Antibody binding kinetics, Induction, and Potential for regulation in acute infection. J. Virol., 2008, 82(1):115-125.
 
Zhang et al., Cross-reactive human immunodeficiency virus type 1-neutralizing human monoclonal antibody that recognizes a novel conformational epitope on gp41 and lacks reactivity against self-antigens. J. Virol., 2008, 82(14): 6869-68679.
 
Haynes & Alam. HIV-1 hides an Achilles’ heel in virion lipids. Immunity, 2008 28(1): 10-12.
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