SBIR TOPIC 294 PHASE 1 - DEVELOPMENT OF GLYCOSYLATION - SPECIFIC RESEARCH
Award Information
Agency: Department of Health and Human Services
Branch: N/A
Contract: N43CO110078
Agency Tracking Number: N43CO110078
Amount:
$148,569.00
Phase:
Phase I
Program:
SBIR
Awards Year:
2011
Solicitation Year:
2011
Solicitation Topic Code:
NCI
Solicitation Number:
N/A
Small Business Information
815 WENNEKER DR, SAINT LOUIS, MO, 63124-2041
DUNS:
100512883
HUBZone Owned:
N
Woman Owned:
N
Socially and Economically Disadvantaged:
Y
Principal Investigator
Name: LING TAN
Phone: (314) 997-5918
Email: TIANL@MEDIOMICS.COM
Phone: (314) 997-5918
Email: TIANL@MEDIOMICS.COM
Business Contact
Name: LING TAN
Phone: (314) 997-5918
Email: TIANL@MEDIOMICS.COM
Phone: (314) 997-5918
Email: TIANL@MEDIOMICS.COM
Research Institution
Name: Stub
Abstract
Glycosylation changes are a universal feature of malignant transformation and tumor progression. Changes in expression levels of certain glycoproteins and altered glycosylation patterns have been detected in most of the major human cancer types and at different stages of tumor progression. The early detection of glycosylation changes is therefore crucial for cancer diagnosis and treatment. Currently, the methods for glycosylation analysis require expensive instruments and are time consuming. Thus, thereis a need to develop new reagents and simpler methods to study carbohydrate modifications of proteins in cancer biology. Our long term goal is to develop new research reagents for basic cancer researchers in the form of antibodies against N- or O-linked carbohydrate antigens in proteins. In the Phase I proposal, we propose to generate over 32 chicken polyclonal (Task 1) and 2-3 monoclonal IgY (Task 2) against specific Oglycosylation sites. In addition, we will use our proprietary PINCER platform technology to develop 5 costeffective, simple and fast assays (Task 3) to detect protein glycosylation using existing commercially available antibodies. We expect that these PINCER reagents can be used to not only develop homogeneous assays for detecting protein glycosylation, but can also be used as unique imaging reagents. * Information listed above is at the time of submission. *