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James Thomas Kellis

from Santa Barbara, CA
Age ~66
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Also known as:
James T Kellis, James M Kellis, James T Kells, Jas T Kellis, James N, Ellisjr K James, Jim Kellis, John Kellis
Related to:
Gina Kellis, 53Melanie KellisJeffrey Kellis, 35Becky GreenGenevieve Kellis, 28Vianny Daniels, 46
Connected to:
Brian B Kellis, 37Charles C Kellis, 82Heidi N Kellis, 54John E Kellis, 71Kathy L Kellis, 67Wayne C Kellis, 67Alexander KellishNathan R Kellison, 44Selina N Kellison, 39Alex I Kellman, 33

James Kellis Phones & Addresses

  • Santa Barbara, CA
  • Mammoth Lakes, CA
  • Oakhurst, CA
  • Tustin, CA
  • San Carlos, CA
  • Portola Valley, CA
  • Woodside, CA
  • Palo Alto, CA
  • Laguna Beach, CA
  • San Mateo, CA
  • Orange, CA

Work

Company: Chatoff properties & campos casuals Position: Realestate agent and regional sales manager

Skills

Microsoft Excel • Microsoft Word • Research • Powerpoint • Sales • Leadership • Training • Photoshop

Resumes

Resumes

James Kellis Photo 1

Realestate Agent And Regional Sales Manager

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Work:
Chatoff Properties & Campos Casuals
Realestate Agent and Regional Sales Manager
Skills:
Microsoft Excel
Microsoft Word
Research
Powerpoint
Sales
Leadership
Training
Photoshop

Publications

Us Patents

Enzymatic Modification Of The Surface Of A Polyester Fiber Or Article

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US Patent:
20020007518, Jan 24, 2002
Filed:
Jul 3, 2001
Appl. No.:
09/898370
Inventors:
James Kellis - Portola Valley CA, US
Ayrookaran Poulose - Belmont CA, US
Mee-Young Yoon - Palo Alto CA, US
International Classification:
D06M010/00
C09B067/00
US Classification:
008/115510
Abstract:
A method is provided for improving the uptake of a cationic compound onto a polyester article starting material, comprising the steps of: (a) obtaining a polyesterase enzyme; (b) contacting said polyesterase enzyme with said polyester article starting material under conditions and for a time suitable for said polyesterase to produce surface modification of said polyester article starting material and produce a surface modified polyester; (c) contacting said modified polyester article, subsequently or simultaneously with said step (b) with a cationic compound whereby adherence of said cationic compound to said modified polyester is increased compared to said polyester starting material. Also disclosed is a method for increasing the hydrophilicity of a polyester to improve fabric characteristics such as stain resistance, wettability and/or dyeability.

Brightness Control Of Displays Using Exponential Current Source

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US Patent:
20030011625, Jan 16, 2003
Filed:
Jul 13, 2001
Appl. No.:
09/904960
Inventors:
James Kellis - Tustin CA, US
International Classification:
G09G003/32
US Classification:
345/690000
Abstract:
An apparatus and method of controlling brightness of a display device by providing a brightness control current that is exponentially related to digital inputs, so as to maintain perceived uniformity in changes to the level of display brightness. One embodiment of the apparatus comprises at least one digital input, an attenuator which receives the digital input and a reference voltage, and which outputs an attenuated voltage based on the digital input; a voltage-to-current converting amplifier circuit converts the attenuated voltage to current; and a current mirror circuit connected to an LED array provides current to control the LED array, wherein the control current is substantially exponentially related to the at least one digital input. Another embodiment comprises an input trimming resistor network used to enhance the accuracy of the output current values by compensating for the circuit variances as additional current mirrors are added to the apparatus.

Multiply-Substituted Protease Variants

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US Patent:
20030073222, Apr 17, 2003
Filed:
Nov 2, 2001
Appl. No.:
10/033325
Inventors:
Ayrookaran Poulose - Belmont CA, US
Volker Schellenberger - Palo Alto CA, US
James Kellis - Portola Valley CA, US
Christian Paech - Daly City CA, US
Joanne Nadherny - San Francisco CA, US
Donald Naki - San Francisco CA, US
Katherine Collier - Redwood City CA, US
Robert Caldwell - Belmont CA, US
Andre Baeck - Bonheiden, BE
International Classification:
C12N009/52
C07H021/04
C12P021/02
C12N001/21
C11D003/386
US Classification:
435/220000, 435/252310, 435/069100, 435/320100, 536/023200, 510/226000, 510/392000
Abstract:
Novel protease variants derived from the DNA sequences of naturally-occurring or recombinant non-human proteases are disclosed. The variant proteases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant protease to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor protease. Such variant proteases have properties which are different from those of the precursor protease, such as altered wash performance. The substituted amino acid residue corresponds to position 103 in combination with one or more of the following substitutions at residue positions corresponding to positions 1, 3, 4, 8, 10, 12, 13, 15, 16, 17,18, 19, 20, 21, 22, 24, 27, 33, 37, 38, 42, 43, 48, 55, 57, 58, 61, 62, 68, 72, 75, 76, 77, 78, 79, 86, 87, 89, 97, 98, 99, 101, 102, 104, 106, 107, 109, 111, 114, 116, 117, 119, 121, 123, 126, 128, 130, 131, 133, 134, 137, 140, 141, 142, 146, 147, 158, 159, 160, 166, 167, 170, 173, 174, 177, 181, 182, 183, 184, 185, 188, 192, 194, 198, 203, 204, 205, 206, 209, 210, 211, 212, 213, 214, 215, 216, 217, 218, 222, 224, 227, 228, 230, 232, 236, 237, 238, 240, 242, 243, 244, 245, 246, 247, 248, 249, 251, 252, 253, 254, 255, 256, 257, 258, 259, 260, 261, 262, 263, 265, 268, 269, 270, 271, 272, 274 and 275 of subtilisin, wherein when a substitution at a position corresponding to residue position 103 is combined with a substitution at a position corresponding to residue position 76, there is also a substitution at one or more residue positions other than residue positions corresponding to positions 27, 99, 101, 104, 107, 109, 123, 128, 166, 204, 206, 210, 216, 217, 218, 222, 260, 265, or 274 of subtilisin.

Multiply-Substituted Protease Variants

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US Patent:
20030119690, Jun 26, 2003
Filed:
Aug 27, 2002
Appl. No.:
10/228572
Inventors:
Ayrookaran Poulose - Belmont CA, US
Volker Schellenberger - Palo Alto CA, US
James Kellis - Portola Valley CA, US
Christian Paech - Daly City CA, US
Joanne Nadherny - San Francisco CA, US
Donald Naki - San Francisco CA, US
Katherine Collier - Redwood City CA, US
Robert Caldwell - Belmont CA, US
Andre Baeck - Bonheiden, BE
International Classification:
A23B007/10
C07H021/04
C12P021/02
C12N001/21
C12N009/54
C12N015/74
C11D003/38
US Classification:
510/226000, 510/320000, 435/221000, 435/069100, 435/252310, 435/320100, 536/023200, 426/053000
Abstract:
Novel protease variants derived from the DNA sequences of naturally-occurring or recombinant non-human proteases are disclosed. The variant proteases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant protease to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor protease. Such variant proteases have properties which are different from those of the precursor protease, such as altered wash performance. The substituted amino acid residue correspond to positions 62, 212, 230, 232, 252 and 257 of subtilisin.

High Throughput Mutagenesis Screening Method

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US Patent:
20030171543, Sep 11, 2003
Filed:
Mar 5, 2002
Appl. No.:
10/092227
Inventors:
Richard Bott - Burlingame CA, US
James Kellis - Portola Valley CA, US
Thomas Morrison - Winchester MA, US
International Classification:
G01N033/53
C12N015/85
C07K014/00
C12P021/02
C12N005/06
US Classification:
530/350000, 435/007100, 435/320100, 435/455000, 435/325000, 435/069100
Abstract:
A high throughput mutagenesis screening method selects sites for saturation scanning using protein structural considerations. Site-saturation libraries are created and screened using assays for sites having protein properties of interest. The sites are categorized for the properties of interest, trends, if any, are identified; and, a variant having a desired property is selected for additional library creation procedures. The additional libraries are created using feedback from the determined categories. One set of additional libraries repeats construction of the previous libraries using the feedback. A second set of additional libraries are new libraries created at sites that are expected to be beneficial based on the feedback. The categories may be coded, using color or other indicia, to allow easy identification of trends.

High Throughput Mutagenesis Screening Method

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US Patent:
20030199068, Oct 23, 2003
Filed:
Mar 5, 2002
Appl. No.:
10/091912
Inventors:
Richard Bott - Burlingame CA, US
James Kellis - Portola Valley CA, US
Thomas Morrison - Winchester MA, US
International Classification:
C12N009/16
C07H021/04
C12N001/21
C12N015/74
US Classification:
435/196000, 435/069100, 435/320100, 435/252300, 536/023200
Abstract:
A high throughput mutagenesis screening method selects sites for saturation scanning using protein structural considerations. Site-saturation libraries are created and screened using assays for sites having protein properties of interest. The sites are categorized for the properties of interest, trends, if any, are identified; and, a variant having a desired property is selected for additional library creation procedures. The additional libraries are created using feedback from the determined categories. One set of additional libraries repeats construction of the previous libraries using the feedback. A second set of additional libraries are new libraries created at sites that are expected to be beneficial based on the feedback. The categories may be coded, using color or other indicia, to allow easy identification of trends.

Multiply-Substituted Protease Variants With Altered Net Charge For Use In Detergents

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US Patent:
20030228995, Dec 11, 2003
Filed:
Apr 25, 2003
Appl. No.:
10/423649
Inventors:
Ayrookaran Poulose - Belmont CA, US
Volker Schellenberger - Palo Alto CA, US
James Kellis - Portola Valley CA, US
Christian Paech - Daly City CA, US
Joanne Nadherny - San Francisco CA, US
Donald Naki - San Francisco CA, US
Katherine Collier - Redwood City CA, US
Robert Caldwell - Belmont CA, US
International Classification:
C11D003/386
C07H021/04
A23B007/10
C12N009/56
C12N001/21
C12P021/02
C12N015/74
US Classification:
510/320000, 435/069100, 435/222000, 435/252300, 435/320100, 536/023200, 426/053000
Abstract:
Novel protease variants derived from the DNA sequences of naturally-occurring or recombinant non-human proteases are disclosed. The variant proteases, in general, are obtained by in vitro modification of a precursor DNA sequence encoding the naturally-occurring or recombinant protease to generate the substitution of a plurality of amino acid residues in the amino acid sequence of a precursor protease. Protease variants are provided that contain substitutions of the amino acids at one or more residue positions so that the substitution alters the charge at that position to make the charge more negative or less positive compared to a precursor protease and thus the protease variant is more effective in a low detergent concentration system than a precursor protease. Also provided are protease variants containing substitutions of the amino acids at one or more residue positions so that the substitution alters the charge at that position to make the charge more positive or less negative compared to a precursor protease and thus the protease variant is more effective in a high detergent concentration system than a precursor protease. Protease variants are provided that contain substitutions of the amino acids at one or more residue positions so that the substitution alters the charge at that position to make the charge more negative or less positive compared to a precursor protease and thus the protease variant is more effective in a medium detergent concentration system than a precursor protease. Also provided are protease variants containing substitutions of the amino acids at one or more residue positions so that the substitution alters the charge at that position to make the charge more positive or less negative compared to a precursor protease and thus the protease variant is more effective in a medium detergent concentration system than a precursor protease. Further provided is a method of producing a protease variant that is more effective in a low detergent concentration system, medium detergent concentration system and high detergent concentration system than a precursor protease.

Method Of Assaying For A Preferred Enzyme And/Or Preferred Detergent Composition

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US Patent:
20040261193, Dec 30, 2004
Filed:
Jul 26, 2004
Appl. No.:
10/899751
Inventors:
Volker Schellenberger - Palo Alto CA, US
Donald Naki - San Francisco CA, US
Katherine Collier - Redwood City CA, US
James Kellis - Portola Valley CA, US
Joanne Nadherny - San Francisco CA, US
International Classification:
D06M010/00
US Classification:
008/115510
Abstract:
An improved method for assaying the wash performance of new enzymes and/or new detergent formulations is described
Control profile
James Thomas Kellis from Santa Barbara, CA, age ~66 Get Report