Government-Owned Inventions; Availability for Licensing, 20957-20958 [E9-10450]
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Federal Register / Vol. 74, No. 86 / Wednesday, May 6, 2009 / Notices
Collaborative Research Opportunity:
The NIH Chemical Genomics Center is
seeking statements of capability or
interest from parties interested in
collaborative research to further
develop, evaluate, or commercialize
appropriate lead compounds described
in U.S. Provisional Application No. 61/
199,763. Please contact Dr. Craig J.
Thomas via e-mail
(craigt@nhgri.nih.gov) for more
information.
Polyclonal Antibodies to the Kidney
Protein Sodium-Hydrogen Exchanger 3
(NHE3)
Description of Technology:
Antibodies to NHE3, useful for
immunoblotting and
immunocytochemistry, are available to
resell for research purposes. NHE3 is a
membrane Na+/H+ exchanger involved
in maintenance of fluid volume
homeostasis in the kidney. It is
expressed on the apical membrane of
the renal proximal tubule and plays a
major role in NaCl and HCO3
absorption. The inventor has developed
rabbit polyclonal antibodies directed
against a peptide sequence common to
human, rat and mouse NHE3.
Applications: Western blotting and
immunocytochemistry.
Inventor: Mark A. Knepper (NHLBI).
Related Publication: Unpublished.
Patent Status: HHS Reference No. E–
253–2008/0—Research Tool. Patent
protection is not being pursued for this
technology.
Licensing Status: This technology is
available as a research tool under a
Biological Materials License.
Licensing Contact: Steve Standley,
Ph.D.; 301–435–4074;
sstand@od.nih.gov.
mstockstill on PROD1PC66 with NOTICES
Polyclonal Antibodies to ThiazideSensitive Sodium-Chloride
Cotransporter (NCC)
Description of Technology:
Antibodies to thiazide-sensitive sodiumchloride cotransporter (NCC), useful for
immunoblotting and
immunocytochemistry, are available to
resell for research purposes. NCC is
found on the apical membrane of the
distal convoluted tubule, where it is the
principal mediator of Na+ and CI
reabsorption in this segment of the
nephron. NCC is the target of thiazide
diuretics used in the treatment of
hypertension. The inventors have
developed rabbit polyclonal antibodies
directed against a peptide sequence in
the C-terminal region of NCC.
Applications: Western blotting and
immunohistochemistry.
Inventor: Mark A. Knepper (NHLBI).
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18:36 May 05, 2009
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Related Publication: HL Biner, MP
Arpin-Bott, J Loffing, X Wang, M
Knepper, SC Hebert, B Kaissling.
Human cortical distal nephron:
distribution of electrolyte and water
transport pathways. J Am Soc Nephrol.
2002 Apr;13(4):836–847.
Patent Status: HHS Reference No. E–
254–2008/0—Research Tool. Patent
protection is not being pursued for this
technology.
Licensing Status: This technology is
available as a research tool under a
Biological Materials License.
Licensing Contact: Steve Standley,
Ph.D.; 301–435–4074;
sstand@od.nih.gov.
Polyclonal Antibodies to NKCC2, a
Kidney-Specific Member of the Cation
Chloride Co-transporter Family,
SLC12A1
Description of Technology:
Antibodies to NKCC2, useful for
immunoblotting and
immunocytochemistry, are available to
resell for research purposes. NKCC2 is
found on the apical surface of the thick
ascending limb of the loop of Henle,
where it facilitates transport of sodium,
potassium, and chloride ions from the
lumen of the renal thick ascending limb
into the cell. Transport of sodium
dilutes the luminal fluid, decreasing its
osmolality creating an osmotic driving
force for water reabsorption in the
connecting tubule and cortical
collecting duct under the influence of
the hormone vasopressin. NKCC2 is
blocked by loop diuretics such as
furosemide. The inventor has developed
rabbit polyclonal antibodies directed
against a peptide sequence in the Nterminal tail of NKCC2.
Applications: Western blotting and
immunocytochemistry.
Inventor: Mark A. Knepper (NHLBI).
Related Publications:
1. GH Kim, CA Ecelbarger, C Mitchell,
RK Packer, JB Wade, MA Knepper.
Vasopressin increases Na-K–2CI
cotransporter expression in thick
ascending limb of Henle’s loop. Am J
Physiol. 1999 Jan;276(1 Pt 2):F96–F103.
2. HL Brooks, AJ Allred, KT Beutler,
TM Cofiman, MA Knepper. Targeted
proteomic profiling of renal Na+
transporter and channel abundances in
angiotensin II type 1a receptor knockout
mice. Hypertension. 2002 Feb;39(2 Pt
2):470–473.
Patent Status: HHS Reference No. E–
255–2008/0—Research Tool. Patent
protection is not being pursued for this
technology.
Licensing Status: This technology is
available as a research tool under a
Biological Materials License.
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20957
Licensing Contact: Steve Standley,
Ph.D.; 301–435–4074;
sstand@od.nih.gov.
Polyclonal Antibodies to the Kidney
Protein Urea Transporter 1 (UTA1)
Description of Technology:
Antibodies to UTA1, useful for
immunoblotting and
immunocytochemistry, are available to
resell for research purposes. Urea
Transporter 1 (UTA1) is activated by
vasopressin and is responsible for urea
transport across the apical membrane
into the intracellular space within the
renal inner medullary collecting duct.
The inventor has developed rabbit
polyclonal antibodies directed against a
peptide sequence in human UTA1.
Antibody also recognizes UTA3, another
product of the same gene.
Applications: Western blotting and
immunocytochemistry.
Inventor: Mark A. Knepper (NHLBI).
Related Publication: S Nielsen, J
Terris, CP Smith, MA Hediger, CA
Ecelbarger, MA Knepper. Cellular and
subcellular localization of the
vasopressin-regulated urea transporter
in rat kidney. Proc Natl Acad Sci USA.
1996 May 28;93(11):5495–500.
Patent Status: HHS Reference No. E–
268–2008/0—Research Tool. Patent
protection is not being pursued for this
technology.
Licensing Status: This technology is
available as a research tool under a
Biological Materials License.
Licensing Contact: Steve Standley,
Ph.D.; 301–435–4074;
sstand@od.nih.gov.
Dated: April 28, 2009.
Richard U. Rodriguez,
Director, Division of Technology Development
and Transfer, Office of Technology Transfer,
National Institutes of Health.
[FR Doc. E9–10452 Filed 5–5–09; 8:45 am]
BILLING CODE 4140–01–P
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
National Institutes of Health
Government-Owned Inventions;
Availability for Licensing
AGENCY: National Institutes of Health,
Public Health Service, HHS.
ACTION: Notice.
SUMMARY: The inventions listed below
are owned by an agency of the U.S.
Government and are available for
licensing in the U.S. in accordance with
35 U.S.C. 207 to achieve expeditious
commercialization of results of
federally-funded research and
E:\FR\FM\06MYN1.SGM
06MYN1
20958
Federal Register / Vol. 74, No. 86 / Wednesday, May 6, 2009 / Notices
development. Foreign patent
applications are filed on selected
inventions to extend market coverage
for companies and may also be available
for licensing.
ADDRESSES: Licensing information and
copies of the U.S. patent applications
listed below may be obtained by writing
to the indicated licensing contact at the
Office of Technology Transfer, National
Institutes of Health, 6011 Executive
Boulevard, Suite 325, Rockville,
Maryland 20852–3804; telephone: 301/
496–7057; fax: 301/402–0220. A signed
Confidential Disclosure Agreement will
be required to receive copies of the
patent applications.
mstockstill on PROD1PC66 with NOTICES
Genetic Mutations Associated With
Stuttering
Description of Technology: NIH
investigators, for the first time,
identified specific mutations associated
with stuttering. These mutations are
located within the genes encoding three
enzymes, Glc-NAc phosphotransferase
catalytic subunit [GNPTAB], Glc-NAc
phosphotransferase recognition subunit
[GNPTG], and N-acetylglucosamine-1phosphodiester alpha-Nacetylglucosaminidase [NAGPA].
Together these constitute the pathway
that targets lysosomal enzymes to their
proper location. This pathway is
associated with lysosomal storage
disorders, and thereby this discovery
provides potential novel therapeutic
targets for amelioration of stuttering.
This discovery has the potential to
facilitate DNA-based (micro-array)
testing among individuals who stutter,
as well as enzyme-replacement therapy
and small-molecule chaperone therapy
for treatment of stuttering. The
mutations described in this invention
may account for up to 5–10% of this
disorder in individuals who stutter,
estimated to represent 60,000–120,000
individuals in the United States.
Applications: Genetic diagnosis of
stuttering disorder; Therapeutics for
stuttering disorder.
Development Status: Early stage.
Market: According to the Stuttering
Foundation of America, stuttering
affects over 3 million individuals in the
United States.
Inventors: Dennis T. Drayna (NIDCD),
Changsoo P. Kang (NIDCD), et al.
Patent Status: U.S. Provisional
Application No. 61/150,954 filed 02 Feb
2009 (HHS Reference No. E–084–2009/
0–US–01).
Licensing Status: Available for
licensing.
Licensing Contact: Suryanarayana
(Sury) Vepa, Ph.D., J.D.; 301–435–5020;
vepas@mail.nih.gov.
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18:36 May 05, 2009
Jkt 217001
Mast Cells Defective in the Syk Protein
Tyrosine Kinase
Description of Technology: NIH
investigators, through screening for
variants of RBL–2H3 cells, have
identified and developed TB1A2 mast
cells that are defective in the expression
of the Syk protein tyrosine kinase.
These cells had no detectable Syk
protein by immunoblotting or in vitro
kinase reaction, and no detectable Syk
mRNA by Northern hybridization.
These TB1A2 cells failed to secrete or
generate cytokines after high affinity
receptor for immunoglobulin E (Fc
epsilon RI) stimulation. In these Sykdeficient TB1A2 cells, aggregation of
these receptors did not induce
histamine release and there was no
detectable increase in total cellular
protein tyrosine phosphorylation.
However, stimulation of these cells with
the calcium ionophore did induce
degranulation. These cells provide a
useful experimental model to study the
role of Syk tyrosine kinase in signal
transduction pathways in immune cells.
Inventors: Juan Zhang, Elsa H.
Berenstein, and Reuben P. Siraganian
(NIDCR).
Publication: J Zhang, EH Berenstein,
RL Evans, RP Siraganian. Transfection
of Syk protein tyrosine kinase
reconstitutes high affinity IgE receptormediated degranulation in a Syknegative variant of rat basophilic
leukemia RBL–2H3 cells. J Exp Med.
1996 July 1;184(1):71–79.
Patent Status: HHS Reference No. E–
342–2008/0—Research Tool. Patent
protection is not being pursued for this
technology.
Licensing Status: Available for
licensing under a Biological Materials
License Agreement.
Licensing Contact: Suryanarayana
(Sury) Vepa, Ph.D., J.D.; 301–435–5020;
vepas@mail.nih.gov.
Collaborative Research Opportunity:
The National Institute of Dental and
Craniofacial Research, Oral Infection
and Immunity Branch, Receptors and
Signal Transduction Section, is seeking
statements of capability or interest from
parties interested in collaborative
research to further develop, evaluate, or
commercialize this technology. Please
contact David W. Bradley, Ph.D. at 301–
402–0540 or bradleyda@nidcr.nih.gov
for more information.
Novel Means of Regulation of Gene
Expression: Modular and Artificial
Splicing Factors
Description of Technology: This
discovery provides a new therapeutic
approach for treatment of diseases
caused by altered gene regulation
PO 00000
Frm 00060
Fmt 4703
Sfmt 4703
resulting from defective alternative
splicing of genes. This technology offers
the following advantages over currently
available methods for regulating
splicing: (a) Delivery can be through
standard gene therapy methods, such as
viral vectors, (b) site of delivery of the
artificial splicing factors can be
controlled, which enables targeted
expression and limited side effects, and
(c) the artificial splicing factors
described here can be readily adapted to
a variety of splicing effector modules.
This invention provides proteins that
combine an RNA recognition module
that can specifically target an
endogenous pre-mRNA with splicing
effector modules that alter splicing to
favor a particular isoform of a mature
mRNA.
The artificial splicing factors
disclosed here can be used to treat
conditions requiring directed alternative
splicing. For example, the artificial
splicing factors described here can be
used in combination with other antitumor drugs as a cancer treatment.
Other examples where this technology
may find use include diabetes (insulin
receptor), psoriasis (fibronectin),
polycystic kidney disease (PKD2), and
prostate cancer (fibroblast growth factor
receptor 2).
Applications: Therapeutics for
diabetes, psoriasis, polycystic kidney
disease, and prostate cancer; Research
Tools.
Development Status: Early stage.
Inventors: Traci M. T. Hall (NIEHS), et
al.
Patent Status: U.S. Provisional
Application No. 61/140,326 filed 23 Dec
2008 (HHS Reference No. E–334–2008/
0–US–01).
Licensing Status: Available for
licensing.
Licensing Contact: Suryanarayana
(Sury) Vepa, Ph.D., J.D.; 301–435–5020;
vepas@mail.nih.gov.
Collaborative Research Opportunity:
The NIEHS Division of Intramural
Research is seeking statements of
capability or interest from parties
interested in collaborative research to
further develop, evaluate, or
commercialize Modular and Artificial
Splicing Factors. Please contact
Elizabeth M. Denholm, Ph.D. at 919–
541–0981 or denholme@niehs.nih.gov or
Traci Hall, Ph.D. at hall4@niehs.nih.gov
for more information.
Dated: April 29, 2009.
Richard U. Rodriguez,
Director, Division of Technology Development
and Transfer, Office of Technology Transfer,
National Institutes of Health.
[FR Doc. E9–10450 Filed 5–5–09; 8:45 am]
BILLING CODE 4140–01–P
E:\FR\FM\06MYN1.SGM
06MYN1
Agencies
[Federal Register Volume 74, Number 86 (Wednesday, May 6, 2009)]
[Notices]
[Pages 20957-20958]
From the Federal Register Online via the Government Printing Office [www.gpo.gov]
[FR Doc No: E9-10450]
-----------------------------------------------------------------------
DEPARTMENT OF HEALTH AND HUMAN SERVICES
National Institutes of Health
Government-Owned Inventions; Availability for Licensing
AGENCY: National Institutes of Health, Public Health Service, HHS.
ACTION: Notice.
-----------------------------------------------------------------------
SUMMARY: The inventions listed below are owned by an agency of the U.S.
Government and are available for licensing in the U.S. in accordance
with 35 U.S.C. 207 to achieve expeditious commercialization of results
of federally-funded research and
[[Page 20958]]
development. Foreign patent applications are filed on selected
inventions to extend market coverage for companies and may also be
available for licensing.
ADDRESSES: Licensing information and copies of the U.S. patent
applications listed below may be obtained by writing to the indicated
licensing contact at the Office of Technology Transfer, National
Institutes of Health, 6011 Executive Boulevard, Suite 325, Rockville,
Maryland 20852-3804; telephone: 301/496-7057; fax: 301/402-0220. A
signed Confidential Disclosure Agreement will be required to receive
copies of the patent applications.
Genetic Mutations Associated With Stuttering
Description of Technology: NIH investigators, for the first time,
identified specific mutations associated with stuttering. These
mutations are located within the genes encoding three enzymes, Glc-NAc
phosphotransferase catalytic subunit [GNPTAB], Glc-NAc
phosphotransferase recognition subunit [GNPTG], and N-
acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
[NAGPA]. Together these constitute the pathway that targets lysosomal
enzymes to their proper location. This pathway is associated with
lysosomal storage disorders, and thereby this discovery provides
potential novel therapeutic targets for amelioration of stuttering.
This discovery has the potential to facilitate DNA-based (micro-array)
testing among individuals who stutter, as well as enzyme-replacement
therapy and small-molecule chaperone therapy for treatment of
stuttering. The mutations described in this invention may account for
up to 5-10% of this disorder in individuals who stutter, estimated to
represent 60,000-120,000 individuals in the United States.
Applications: Genetic diagnosis of stuttering disorder;
Therapeutics for stuttering disorder.
Development Status: Early stage.
Market: According to the Stuttering Foundation of America,
stuttering affects over 3 million individuals in the United States.
Inventors: Dennis T. Drayna (NIDCD), Changsoo P. Kang (NIDCD), et
al.
Patent Status: U.S. Provisional Application No. 61/150,954 filed 02
Feb 2009 (HHS Reference No. E-084-2009/0-US-01).
Licensing Status: Available for licensing.
Licensing Contact: Suryanarayana (Sury) Vepa, Ph.D., J.D.; 301-435-
5020; vepas@mail.nih.gov.
Mast Cells Defective in the Syk Protein Tyrosine Kinase
Description of Technology: NIH investigators, through screening for
variants of RBL-2H3 cells, have identified and developed TB1A2 mast
cells that are defective in the expression of the Syk protein tyrosine
kinase. These cells had no detectable Syk protein by immunoblotting or
in vitro kinase reaction, and no detectable Syk mRNA by Northern
hybridization. These TB1A2 cells failed to secrete or generate
cytokines after high affinity receptor for immunoglobulin E (Fc epsilon
RI) stimulation. In these Syk-deficient TB1A2 cells, aggregation of
these receptors did not induce histamine release and there was no
detectable increase in total cellular protein tyrosine phosphorylation.
However, stimulation of these cells with the calcium ionophore did
induce degranulation. These cells provide a useful experimental model
to study the role of Syk tyrosine kinase in signal transduction
pathways in immune cells.
Inventors: Juan Zhang, Elsa H. Berenstein, and Reuben P. Siraganian
(NIDCR).
Publication: J Zhang, EH Berenstein, RL Evans, RP Siraganian.
Transfection of Syk protein tyrosine kinase reconstitutes high affinity
IgE receptor-mediated degranulation in a Syk-negative variant of rat
basophilic leukemia RBL-2H3 cells. J Exp Med. 1996 July 1;184(1):71-79.
Patent Status: HHS Reference No. E-342-2008/0--Research Tool.
Patent protection is not being pursued for this technology.
Licensing Status: Available for licensing under a Biological
Materials License Agreement.
Licensing Contact: Suryanarayana (Sury) Vepa, Ph.D., J.D.; 301-435-
5020; vepas@mail.nih.gov.
Collaborative Research Opportunity: The National Institute of
Dental and Craniofacial Research, Oral Infection and Immunity Branch,
Receptors and Signal Transduction Section, is seeking statements of
capability or interest from parties interested in collaborative
research to further develop, evaluate, or commercialize this
technology. Please contact David W. Bradley, Ph.D. at 301-402-0540 or
bradleyda@nidcr.nih.gov for more information.
Novel Means of Regulation of Gene Expression: Modular and Artificial
Splicing Factors
Description of Technology: This discovery provides a new
therapeutic approach for treatment of diseases caused by altered gene
regulation resulting from defective alternative splicing of genes. This
technology offers the following advantages over currently available
methods for regulating splicing: (a) Delivery can be through standard
gene therapy methods, such as viral vectors, (b) site of delivery of
the artificial splicing factors can be controlled, which enables
targeted expression and limited side effects, and (c) the artificial
splicing factors described here can be readily adapted to a variety of
splicing effector modules. This invention provides proteins that
combine an RNA recognition module that can specifically target an
endogenous pre-mRNA with splicing effector modules that alter splicing
to favor a particular isoform of a mature mRNA.
The artificial splicing factors disclosed here can be used to treat
conditions requiring directed alternative splicing. For example, the
artificial splicing factors described here can be used in combination
with other anti-tumor drugs as a cancer treatment. Other examples where
this technology may find use include diabetes (insulin receptor),
psoriasis (fibronectin), polycystic kidney disease (PKD2), and prostate
cancer (fibroblast growth factor receptor 2).
Applications: Therapeutics for diabetes, psoriasis, polycystic
kidney disease, and prostate cancer; Research Tools.
Development Status: Early stage.
Inventors: Traci M. T. Hall (NIEHS), et al.
Patent Status: U.S. Provisional Application No. 61/140,326 filed 23
Dec 2008 (HHS Reference No. E-334-2008/0-US-01).
Licensing Status: Available for licensing.
Licensing Contact: Suryanarayana (Sury) Vepa, Ph.D., J.D.; 301-435-
5020; vepas@mail.nih.gov.
Collaborative Research Opportunity: The NIEHS Division of
Intramural Research is seeking statements of capability or interest
from parties interested in collaborative research to further develop,
evaluate, or commercialize Modular and Artificial Splicing Factors.
Please contact Elizabeth M. Denholm, Ph.D. at 919-541-0981 or
denholme@niehs.nih.gov or Traci Hall, Ph.D. at hall4@niehs.nih.gov for
more information.
Dated: April 29, 2009.
Richard U. Rodriguez,
Director, Division of Technology Development and Transfer, Office of
Technology Transfer, National Institutes of Health.
[FR Doc. E9-10450 Filed 5-5-09; 8:45 am]
BILLING CODE 4140-01-P