Mark H Knuth, Age 6443 Hawk Feather Cir, Madison, WI 53717

Mark Knuth Phones & Addresses

43 Hawk Feather Cir, Madison, WI 53717 (608) 203-5435

Verona, WI

Rockton, IL

50651 Deer Ridge Dr, Granger, IN 46530 (574) 277-7183

43 Hawk Feather Cir, Madison, WI 53717 (574) 277-7183

Work

Position: Technicians and Related Support Occupations

Education

Degree: High school graduate or higher

Emails

Mentions for Mark H Knuth

Mark Knuth resumes & CV records

Resumes

Mark Knuth Photo 18

New Product Development Engineering Manager

Location:
43 Hawk Feather Cir, Madison, WI 53717
Industry:
Executive Office
Work:
RenewAire, LLC since Dec 2010
NEW PRODUCT DEVELOPMENT ENGINEERING MANAGER
Velvac Inc. Jun 2008 - Nov 2009
VICE PRESIDENT OF ENGINEERING
Parts Now! LLC Nov 2006 - Feb 2008
DIRECTOR OF OPERATIONS
Atwood Mobile Products - Creation Operations Aug 2005 - Nov 2006
GENERAL MANAGER
Atwood Mobile Products - Charlotte Operations Apr 2003 - Aug 2005
GENERAL MANAGER
Atwood Mobile Products Jan 2002 - Apr 2003
DIRECTOR OF LEAN MANUFACTURING
Atwood Mobile Products Jun 1994 - Jan 2002
ENGINEERING MANAGER
Sundstrand Corporation Jan 1984 - Mar 1989
Engineer
Education:
Indiana University South Bend 1998 - 2003
MBA, Finance, Accounting
Southern Illinois University, Carbondale 1980 - 1983
BSMET, Engineering
Rock Valley College 1977 - 1980
AAS, Machine Design
Skills:
Lean Manufacturing, Product Development, Engineering, Project Management, Business Development, Continuous Improvement, Process Improvement, Manufacturing, Six Sigma, Strategic Planning, Team Building, Operations Management
Languages:
English
Mark Knuth Photo 19

Mark Knuth

Mark Knuth Photo 20

Leader In Energy Recovery Technologies

Location:
Madison, Wisconsin Area
Industry:
Executive Office

Publications & IP owners

Us Patents

Purification Of Somatotropin From Transformed Microorganisms

US Patent:
6586575, Jul 1, 2003
Filed:
May 23, 1995
Appl. No.:
08/447381
Inventors:
Timothy W. Evans - Township of Park MI
Mark W. Knuth - Madison WI
Assignee:
Pharmacia Upjohn Company - Kalamazoo MI
International Classification:
C07K 1700
US Classification:
530399, 530350, 530351, 435 691, 435 694
Abstract:
This invention discloses a commercially advantageous process for extraction and purification of protein from microorganisms. The initial steps of the process are useful for purifying many insoluble proteins while later steps are designed to renature denatured somatotropins produced by transformed microorganisms. The process is especially useful for purifying recombinantly-produced bovine somatotropin.

High Level Expression And Facile Purification Of Proteins, Peptides And Conjugates For Immunization, Purification And Detection Applications

US Patent:
6764689, Jul 20, 2004
Filed:
Jun 30, 1999
Appl. No.:
09/345264
Inventors:
Mark W. Knuth - Waunakee WI
Mary Haak-Frendscho - Madison WI
John W. Shultz - Verona WI
Scott A. Lesley - Oregon WI
Catherine E. Villars - McFarland WI
Assignee:
Promega Corporation - Madison WI
International Classification:
A61K 3939
US Classification:
4242781, 4241921, 4241931, 530324, 530350, 530403
Abstract:
A process for producing and purifying peptides and for producing peptide/protein antigens for antibody production is described. The process utilizes fusion proteins and specifically fusion proteins in which the fusion protein carrier segment includes an amino acid sequence at least about 65 amino acids long and in which the amino acid sequence does not contain negative or positive charged side chains of amino acids.

Purification Of Somatotropin From Transformed Microorganisms

US Patent:
6916914, Jul 12, 2005
Filed:
Jun 13, 1986
Appl. No.:
08/256297
Inventors:
Timothy W. Evans - Three Rivers MI, US
Mark W. Knuth - Madison WI, US
Assignee:
Pharmacia & Upjohn Co. - Kalamazoo MI
International Classification:
A23J001/00
C07K014/00
US Classification:
530422, 530350, 530351, 530399, 435 694
Abstract:
This invention discloses a commercially advantageous process for extraction and purification of protein from microorganisms. The initial steps of the process are useful for purifying many insoluble proteins while later steps are designed to renature denatured somatotropins produced by transformed microorganisms. The process is especially useful for purifying recombinantly-produced bovine somatotropin.

Isolated Agarase Enzyme From Flavobacterium Sp. Strain Nr19, Cloned Genes Therefor, And Expression Thereof In Transformed Host Cells

US Patent:
5869310, Feb 9, 1999
Filed:
Jun 3, 1996
Appl. No.:
8/655704
Inventors:
Mark W. Knuth - Waunakee WI
Kimberly K. Knoche - Middleton WI
Susanne Selman - Madison WI
James R. Hartnett - Madison WI
Assignee:
Promega Corporation - Madison WI
International Classification:
C12N 938
C12N 924
C12N 100
US Classification:
435207
Abstract:
Novel purified agarase enzymes from Flavobacterium sp. strain NR19 and cloned genes encoding the agarase enzymes are disclosed. Transformed host cells which express the novel agarase enzymes in isolatable quantities are also described. Also disclosed are antibodies specifically reactive with the novel agarases.

Isolated Agarase Enzyme From Flavobacterium Sp. Strain Nr19, Cloned Genes Therefor, And Expression Thereof In Transformed Host Cells

US Patent:
6001636, Dec 14, 1999
Filed:
Jun 30, 1998
Appl. No.:
9/107755
Inventors:
Mark W. Knuth - Waunakee WI
Kimberly K. Knoche - Middleton WI
Susanne Selman - Madison WI
James R. Hartnett - Madison WI
Assignee:
Promega Corporation - Madison WI
International Classification:
C12N 120
C12N 924
C12N 938
C12N 1500
C07H 2104
US Classification:
4352523
Abstract:
Novel purified agarase enzymes from Flavobacterium sp. strain NR19 and cloned genes encoding the agarase enzymes are disclosed. Transformed host cells which express the novel agarase enzymes in isolatable quantities are also described. Also disclosed are antibodies specifically reactive with the novel agarases.

Use Of Agarase Enzyme To Isolate Nucleic Acids

US Patent:
5814487, Sep 29, 1998
Filed:
Feb 13, 1997
Appl. No.:
8/799552
Inventors:
Mark W. Knuth - Waunakee WI
Susanne Selman - Madison WI
Assignee:
Promega Corporation - Madison WI
International Classification:
C12P 1944
C12P 1914
C12N 924
C08B 100
US Classification:
435 74
Abstract:
A process for isolating nucleic acids from agarose, and particularly regular agarose, is described wherein the agarose is augmented with a chaotropic substance and hydrolyzed by a novel purified agarase enzyme from Flavobacterium sp. strain NR19.

High Level Expression And Facile Purification Of Proteins, Peptides And Conjugates For Immunization, Purification And Detection Applications

US Patent:
6069230, May 30, 2000
Filed:
Nov 10, 1994
Appl. No.:
8/338382
Inventors:
Mark W. Knuth - Waunakee WI
Mary Haak-Frendscho - Madison WI
John W. Shultz - Verona WI
Scott A. Lesley - Oregon WI
Catherine E. Villars - McFarland WI
Assignee:
Promega Corporation - Madison WI
International Classification:
C07K 1400
US Classification:
530324
Abstract:
A process for pro and purifying peptides and for producing peptide/protein antigens for antibody production is described. The process utilizes fusion proteins and specifically fusion proteins in which the fusion protein carrier segment includes an amino acid sequence at least about 65 amino acids long and in which the amino acid sequence does not contain negative or positive charged side chains of amino acids.

High Level Expression And Facile Purification Of Proteins, Peptides And Conjugates For Immunization, Purification And Detection Applications

US Patent:
5989554, Nov 23, 1999
Filed:
Oct 16, 1998
Appl. No.:
9/174060
Inventors:
Mark W. Knuth - Waunakee WI
Mary Haak-Frendscho - Madison WI
John W. Shultz - Verona WI
Scott A. Lesley - Oregon WI
Catherine E. Villars - McFarland WI
Assignee:
Promega Corporation - Madison WI
International Classification:
A61K 3900
A61K 39385
US Classification:
4241921
Abstract:
A process for producing and purifying peptides and for producing peptide/protein antigens for antibody production is described. The process utilizes fusion proteins and specifically fusion proteins in which the fusion protein carrier segment includes an amino acid sequence at least about 65 amino acids long and in which the amino acid sequence does not contain negative or positive charged side chains of amino acids.

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