CREATE Health

Lund, Sweden

CREATE Health

Lund, Sweden
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A highly skilled team with a proven track record of successfully establishing and scaling up CLIA accredited reference laboratories based on ground breaking new technologies have been recruited to carry out the US market introduction of Immunovia's first test, IMMray™ PanCan-d, in the second half of 2018. Mats Grahn, CEO Immunovia, comments: "The market introduction of IMMray™ PanCan-d, our blood based test for earlier detection of pancreas cancer, is the main focus for Immunovia. We have therefore chosen to establish our USA operations headquarters in Boston, which is the major biotech hub in the world. A very experienced laboratory team will be moving into Immunovia´s own reference laboratory that will cover Eastern USA, adding to our commercial group that will also be located at the Boston facilities. This East coast laboratory complements the existing collaboration we have with Knight Diagnostic Laboratories in Portland, serving Western USA." Immunovia AB was founded in 2007 by investigators from the Department of Immunotechnology at Lund University and CREATE Health, the Center for Translational Cancer Research in Lund, Sweden. Immunovia´s core technology platform, IMMray™, is based on antibody biomarker microarray analysis. The company is now performing clinical validation studies for the commercialization of IMMray™ PanCan-d that could be the first blood based test for early diagnosis of pancreatic cancer. In the beginning of 2016, the company started a program focused on autoimmune diseases diagnosis, prognosis and therapy monitoring. The first test from this program, IMMray™ SLE-d, is a biomarker signature derived for differential diagnosis of lupus, now undergoing evaluation and validation. (Source: http://www.immunovia.com ) Immunovia's shares (IMMNOV) are listed on Nasdaq First North in Stockholm and Wildeco is the company's Certified Adviser. For more information, please contact: Mats Grahn Chief Executive Officer, CEO, Immunovia Tel.: +46-70-5320230 Email: mats.grahn@immunovia.com


Olsson N.,Lund University | Olsson N.,CREATE Health | Wingren C.,Lund University | Wingren C.,CREATE Health | And 8 more authors.
Molecular and Cellular Proteomics | Year: 2011

Antibody-based microarrays are a rapidly evolving affinity-proteomic methodology that recently has shown great promise in clinical applications. The resolution of these proteomic analyses is, however, directly related to the number of data-points, i.e. antibodies, included on the array. Currently, this is a key bottleneck because of limited availability of numerous highly characterized antibodies. Here, we present a conceptually new method, denoted global proteome survey, opening up the possibility to probe any proteome in a species-independent manner while still using a limited set of antibodies. We use context-independent-motif-specific antibodies directed against short amino acid motifs, where each motif is present in up to a few hundred different proteins. First, the digested proteome is exposed to these antibodies, whereby motif-containing peptides are enriched, which then are detected and identified by mass spectrometry. In this study, we profiled extracts from human colon tissue, yeast cells lysate, and mouse liver tissue to demonstrate proof-of-concept. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.


Sandin M.,CREATE Health | Antberg L.,CREATE Health | Levander F.,CREATE Health | James P.,CREATE Health
EuPA Open Proteomics | Year: 2015

Protein translocation between organelles in the cell is an important process that regulates many cellular functions. However, organelles can rarely be isolated to purity so several methods have been developed to analyse the fractions obtained by density gradient centrifugation. We present an analysis of the distribution of proteins amongst organelles in the human breast cell line, MDA-MB-231 using two approaches: an isotopic labelling and a label-free approach. © 2015 The Authors.


Olsson N.,Lund University | Olsson N.,CREATE Health | Wallin S.,Lund University | James P.,Lund University | And 5 more authors.
Protein Science | Year: 2012

Protein-peptide interactions are a common occurrence and essential for numerous cellular processes, and frequently explored in broad applications within biology, medicine, and proteomics. Therefore, understanding the molecular mechanism(s) of protein-peptide recognition, specificity, and binding interactions will be essential. In this study, we report the first detailed analysis of antibody-peptide interaction characteristics, by combining large-scale experimental peptide binding data with the structural analysis of eight human recombinant antibodies and numerous peptides, targeting tryptic mammalian and eukaryote proteomes. The results consistently revealed that promiscuous peptide-binding interactions, that is, both specific and degenerate binding, were exhibited by all antibodies, and the discovery was corroborated by orthogonal data, indicating that this might be a general phenomenon for low-affinity antibody-peptide interactions. The molecular mechanism for the degenerate peptide-binding specificity appeared to be executed through the use of 2-3 semi-conserved anchor residues in the C-terminal part of the peptides, in analogue to the mechanism utilized by the major histocompatibility complex-peptide complexes. In the long-term, this knowledge will be instrumental for advancing our fundamental understanding of protein-peptide interactions, as well as for designing, generating, and applying peptide specific antibodies, or peptide-binding proteins in general, in various biotechnical and medical applications. Published by Wiley-Blackwell. © 2012 The Protein Society.

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