alanine mutant Search Results


ubxd1 plasmids pcdna3.1(+) streptagii wt with aa 1–264  (BioCat GmbH)
90
BioCat GmbH ubxd1 plasmids pcdna3.1(+) streptagii wt with aa 1–264
a Western blot analysis of cellular ubiquitin conjugates co-isolating in pulldowns of <t>StrepTagII-UBXD1</t> or only the StrepTagII peptide expressed in HEK293 cells as indicated. In presence of UBXD1, ubiquitin conjugates were detected. b UBXD1 constructs overexpressed in HEK293 and E. coli cells to narrow down the ubiquitin binding region. Domains color-coded as follows: N-terminus (1–133, dark blue) with VIM helix (50–65, gray), PUB domain (150–264, light blue) and UBX domain (333–411, pink). c Deletion of the UBX domain (333–411) abolishes ubiquitin binding by UBXD1. UBXD1 or indicated truncation variants were expressed in HEK293 cells and lysates used for ubiquitin-GST (Ub-GST) pulldowns. Co-isolated UBXD1 was detected with UBXD1-specific antibodies. d Ub-GST pulldowns with purified UBXD1, UBXD1-ΔLinker-UBX-C, UBXD1-Linker-UBX-C or UBXD1-PUB. All blots ( a , c , d ) were performed as n = 1 independent experiments. For all GST control blots see Supplementary Fig. . Source data are provided as a source data file.
Ubxd1 Plasmids Pcdna3.1(+) Streptagii Wt With Aa 1–264, supplied by BioCat GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/alanine+mutant/sdm+for+the+ubxd1+alanine+mutants/pmc10241913-343-13-25
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ubxd1 plasmids pcdna3.1(+) streptagii wt with aa 1–264 - by Bioz Stars, 2026-09
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the mutant in which serine 195 has been replaced by an alanine (ala-tpa)  (Genentech inc)
90
Genentech inc the mutant in which serine 195 has been replaced by an alanine (ala-tpa)
a Western blot analysis of cellular ubiquitin conjugates co-isolating in pulldowns of <t>StrepTagII-UBXD1</t> or only the StrepTagII peptide expressed in HEK293 cells as indicated. In presence of UBXD1, ubiquitin conjugates were detected. b UBXD1 constructs overexpressed in HEK293 and E. coli cells to narrow down the ubiquitin binding region. Domains color-coded as follows: N-terminus (1–133, dark blue) with VIM helix (50–65, gray), PUB domain (150–264, light blue) and UBX domain (333–411, pink). c Deletion of the UBX domain (333–411) abolishes ubiquitin binding by UBXD1. UBXD1 or indicated truncation variants were expressed in HEK293 cells and lysates used for ubiquitin-GST (Ub-GST) pulldowns. Co-isolated UBXD1 was detected with UBXD1-specific antibodies. d Ub-GST pulldowns with purified UBXD1, UBXD1-ΔLinker-UBX-C, UBXD1-Linker-UBX-C or UBXD1-PUB. All blots ( a , c , d ) were performed as n = 1 independent experiments. For all GST control blots see Supplementary Fig. . Source data are provided as a source data file.
The Mutant In Which Serine 195 Has Been Replaced By An Alanine (Ala Tpa), supplied by Genentech inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/alanine+mutant/the+mutant+in+which+serine+195+has+been+replaced+by+an+alanine++ala+tpa+/10__1074_slash_jbc__m306184200-63-8-25
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the mutant in which serine 195 has been replaced by an alanine (ala-tpa) - by Bioz Stars, 2026-09
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nanoglo with 20 um furimazine  (Promega)
90
Promega nanoglo with 20 um furimazine
a Western blot analysis of cellular ubiquitin conjugates co-isolating in pulldowns of <t>StrepTagII-UBXD1</t> or only the StrepTagII peptide expressed in HEK293 cells as indicated. In presence of UBXD1, ubiquitin conjugates were detected. b UBXD1 constructs overexpressed in HEK293 and E. coli cells to narrow down the ubiquitin binding region. Domains color-coded as follows: N-terminus (1–133, dark blue) with VIM helix (50–65, gray), PUB domain (150–264, light blue) and UBX domain (333–411, pink). c Deletion of the UBX domain (333–411) abolishes ubiquitin binding by UBXD1. UBXD1 or indicated truncation variants were expressed in HEK293 cells and lysates used for ubiquitin-GST (Ub-GST) pulldowns. Co-isolated UBXD1 was detected with UBXD1-specific antibodies. d Ub-GST pulldowns with purified UBXD1, UBXD1-ΔLinker-UBX-C, UBXD1-Linker-UBX-C or UBXD1-PUB. All blots ( a , c , d ) were performed as n = 1 independent experiments. For all GST control blots see Supplementary Fig. . Source data are provided as a source data file.
Nanoglo With 20 Um Furimazine, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/alanine+mutant/glutathione+beads+loaded+with+20+%CE%BCg+gst+protein++gst+fc%CE%B3ri+cy+fusion+protein++or+serine+to+alanine+mutants+of+fc%CE%B3ri+cy/us10184936-1338-6-9
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nanoglo with 20 um furimazine - by Bioz Stars, 2026-09
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mutant tat protein at lysine19 residue (substituted to alanine, k19a)  (DIATHEVA Inc)
90
DIATHEVA Inc mutant tat protein at lysine19 residue (substituted to alanine, k19a)
a Western blot analysis of cellular ubiquitin conjugates co-isolating in pulldowns of <t>StrepTagII-UBXD1</t> or only the StrepTagII peptide expressed in HEK293 cells as indicated. In presence of UBXD1, ubiquitin conjugates were detected. b UBXD1 constructs overexpressed in HEK293 and E. coli cells to narrow down the ubiquitin binding region. Domains color-coded as follows: N-terminus (1–133, dark blue) with VIM helix (50–65, gray), PUB domain (150–264, light blue) and UBX domain (333–411, pink). c Deletion of the UBX domain (333–411) abolishes ubiquitin binding by UBXD1. UBXD1 or indicated truncation variants were expressed in HEK293 cells and lysates used for ubiquitin-GST (Ub-GST) pulldowns. Co-isolated UBXD1 was detected with UBXD1-specific antibodies. d Ub-GST pulldowns with purified UBXD1, UBXD1-ΔLinker-UBX-C, UBXD1-Linker-UBX-C or UBXD1-PUB. All blots ( a , c , d ) were performed as n = 1 independent experiments. For all GST control blots see Supplementary Fig. . Source data are provided as a source data file.
Mutant Tat Protein At Lysine19 Residue (Substituted To Alanine, K19a), supplied by DIATHEVA Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/alanine+mutant/mutant+tat+protein+at+lysine19+residue++substituted+to+alanine++k19a+/pmc08329121-48-17-34
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mutant tat protein at lysine19 residue (substituted to alanine, k19a) - by Bioz Stars, 2026-09
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alanine mutant genes  (Synbio Technologies LLC)
90
Synbio Technologies LLC alanine mutant genes
a Western blot analysis of cellular ubiquitin conjugates co-isolating in pulldowns of <t>StrepTagII-UBXD1</t> or only the StrepTagII peptide expressed in HEK293 cells as indicated. In presence of UBXD1, ubiquitin conjugates were detected. b UBXD1 constructs overexpressed in HEK293 and E. coli cells to narrow down the ubiquitin binding region. Domains color-coded as follows: N-terminus (1–133, dark blue) with VIM helix (50–65, gray), PUB domain (150–264, light blue) and UBX domain (333–411, pink). c Deletion of the UBX domain (333–411) abolishes ubiquitin binding by UBXD1. UBXD1 or indicated truncation variants were expressed in HEK293 cells and lysates used for ubiquitin-GST (Ub-GST) pulldowns. Co-isolated UBXD1 was detected with UBXD1-specific antibodies. d Ub-GST pulldowns with purified UBXD1, UBXD1-ΔLinker-UBX-C, UBXD1-Linker-UBX-C or UBXD1-PUB. All blots ( a , c , d ) were performed as n = 1 independent experiments. For all GST control blots see Supplementary Fig. . Source data are provided as a source data file.
Alanine Mutant Genes, supplied by Synbio Technologies LLC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/alanine+mutant/alanine+mutant+genes/pmc08545432-299-8-16
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alanine mutant genes - by Bioz Stars, 2026-09
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recombinant catalytically inactive serine-to-alanine mutant  (ActiveSite Pharmaceuticals)
90
ActiveSite Pharmaceuticals recombinant catalytically inactive serine-to-alanine mutant
a Western blot analysis of cellular ubiquitin conjugates co-isolating in pulldowns of <t>StrepTagII-UBXD1</t> or only the StrepTagII peptide expressed in HEK293 cells as indicated. In presence of UBXD1, ubiquitin conjugates were detected. b UBXD1 constructs overexpressed in HEK293 and E. coli cells to narrow down the ubiquitin binding region. Domains color-coded as follows: N-terminus (1–133, dark blue) with VIM helix (50–65, gray), PUB domain (150–264, light blue) and UBX domain (333–411, pink). c Deletion of the UBX domain (333–411) abolishes ubiquitin binding by UBXD1. UBXD1 or indicated truncation variants were expressed in HEK293 cells and lysates used for ubiquitin-GST (Ub-GST) pulldowns. Co-isolated UBXD1 was detected with UBXD1-specific antibodies. d Ub-GST pulldowns with purified UBXD1, UBXD1-ΔLinker-UBX-C, UBXD1-Linker-UBX-C or UBXD1-PUB. All blots ( a , c , d ) were performed as n = 1 independent experiments. For all GST control blots see Supplementary Fig. . Source data are provided as a source data file.
Recombinant Catalytically Inactive Serine To Alanine Mutant, supplied by ActiveSite Pharmaceuticals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/alanine+mutant/recombinant+catalytically+inactive+serine+to+alanine+mutant/pm23785123-87-4-8
Average 90 stars, based on 1 article reviews
recombinant catalytically inactive serine-to-alanine mutant - by Bioz Stars, 2026-09
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cdna constructs for each cmrap1 alanine mutant and bfmrap1 alanine mutant  (GenScript corporation)
90
GenScript corporation cdna constructs for each cmrap1 alanine mutant and bfmrap1 alanine mutant
a Western blot analysis of cellular ubiquitin conjugates co-isolating in pulldowns of <t>StrepTagII-UBXD1</t> or only the StrepTagII peptide expressed in HEK293 cells as indicated. In presence of UBXD1, ubiquitin conjugates were detected. b UBXD1 constructs overexpressed in HEK293 and E. coli cells to narrow down the ubiquitin binding region. Domains color-coded as follows: N-terminus (1–133, dark blue) with VIM helix (50–65, gray), PUB domain (150–264, light blue) and UBX domain (333–411, pink). c Deletion of the UBX domain (333–411) abolishes ubiquitin binding by UBXD1. UBXD1 or indicated truncation variants were expressed in HEK293 cells and lysates used for ubiquitin-GST (Ub-GST) pulldowns. Co-isolated UBXD1 was detected with UBXD1-specific antibodies. d Ub-GST pulldowns with purified UBXD1, UBXD1-ΔLinker-UBX-C, UBXD1-Linker-UBX-C or UBXD1-PUB. All blots ( a , c , d ) were performed as n = 1 independent experiments. For all GST control blots see Supplementary Fig. . Source data are provided as a source data file.
Cdna Constructs For Each Cmrap1 Alanine Mutant And Bfmrap1 Alanine Mutant, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/alanine+mutant/cdna+constructs+for+each+cmrap1+alanine+mutant+and+bfmrap1+alanine+mutant/pmc09688151-54-21-35
Average 90 stars, based on 1 article reviews
cdna constructs for each cmrap1 alanine mutant and bfmrap1 alanine mutant - by Bioz Stars, 2026-09
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crystals of an activesite mutant protein bearing an alanine substitution for the conserved residue glu137  (ActiveSite Pharmaceuticals)
90
ActiveSite Pharmaceuticals crystals of an activesite mutant protein bearing an alanine substitution for the conserved residue glu137
a Western blot analysis of cellular ubiquitin conjugates co-isolating in pulldowns of <t>StrepTagII-UBXD1</t> or only the StrepTagII peptide expressed in HEK293 cells as indicated. In presence of UBXD1, ubiquitin conjugates were detected. b UBXD1 constructs overexpressed in HEK293 and E. coli cells to narrow down the ubiquitin binding region. Domains color-coded as follows: N-terminus (1–133, dark blue) with VIM helix (50–65, gray), PUB domain (150–264, light blue) and UBX domain (333–411, pink). c Deletion of the UBX domain (333–411) abolishes ubiquitin binding by UBXD1. UBXD1 or indicated truncation variants were expressed in HEK293 cells and lysates used for ubiquitin-GST (Ub-GST) pulldowns. Co-isolated UBXD1 was detected with UBXD1-specific antibodies. d Ub-GST pulldowns with purified UBXD1, UBXD1-ΔLinker-UBX-C, UBXD1-Linker-UBX-C or UBXD1-PUB. All blots ( a , c , d ) were performed as n = 1 independent experiments. For all GST control blots see Supplementary Fig. . Source data are provided as a source data file.
Crystals Of An Activesite Mutant Protein Bearing An Alanine Substitution For The Conserved Residue Glu137, supplied by ActiveSite Pharmaceuticals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/alanine+mutant/crystals+of+an+activesite+mutant+protein+bearing+an+alanine+substitution+for+the+conserved+residue+glu137/10__1107_slash_s2053230x16000753-45-13-3
Average 90 stars, based on 1 article reviews
crystals of an activesite mutant protein bearing an alanine substitution for the conserved residue glu137 - by Bioz Stars, 2026-09
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human fbxw8 mutant cds  (VectorBuilder GmbH)
90
VectorBuilder GmbH human fbxw8 mutant cds
a Western blot analysis of cellular ubiquitin conjugates co-isolating in pulldowns of <t>StrepTagII-UBXD1</t> or only the StrepTagII peptide expressed in HEK293 cells as indicated. In presence of UBXD1, ubiquitin conjugates were detected. b UBXD1 constructs overexpressed in HEK293 and E. coli cells to narrow down the ubiquitin binding region. Domains color-coded as follows: N-terminus (1–133, dark blue) with VIM helix (50–65, gray), PUB domain (150–264, light blue) and UBX domain (333–411, pink). c Deletion of the UBX domain (333–411) abolishes ubiquitin binding by UBXD1. UBXD1 or indicated truncation variants were expressed in HEK293 cells and lysates used for ubiquitin-GST (Ub-GST) pulldowns. Co-isolated UBXD1 was detected with UBXD1-specific antibodies. d Ub-GST pulldowns with purified UBXD1, UBXD1-ΔLinker-UBX-C, UBXD1-Linker-UBX-C or UBXD1-PUB. All blots ( a , c , d ) were performed as n = 1 independent experiments. For all GST control blots see Supplementary Fig. . Source data are provided as a source data file.
Human Fbxw8 Mutant Cds, supplied by VectorBuilder GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/alanine+mutant/human+fbxw8+mutant+cds+with+substitution+of+lysines+and+arginines+into+alanines+in+the+n+terminus/pm38561547-437-0-19
Average 90 stars, based on 1 article reviews
human fbxw8 mutant cds - by Bioz Stars, 2026-09
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alanine mutant  (Synbio Technologies LLC)
90
Synbio Technologies LLC alanine mutant
a Western blot analysis of cellular ubiquitin conjugates co-isolating in pulldowns of <t>StrepTagII-UBXD1</t> or only the StrepTagII peptide expressed in HEK293 cells as indicated. In presence of UBXD1, ubiquitin conjugates were detected. b UBXD1 constructs overexpressed in HEK293 and E. coli cells to narrow down the ubiquitin binding region. Domains color-coded as follows: N-terminus (1–133, dark blue) with VIM helix (50–65, gray), PUB domain (150–264, light blue) and UBX domain (333–411, pink). c Deletion of the UBX domain (333–411) abolishes ubiquitin binding by UBXD1. UBXD1 or indicated truncation variants were expressed in HEK293 cells and lysates used for ubiquitin-GST (Ub-GST) pulldowns. Co-isolated UBXD1 was detected with UBXD1-specific antibodies. d Ub-GST pulldowns with purified UBXD1, UBXD1-ΔLinker-UBX-C, UBXD1-Linker-UBX-C or UBXD1-PUB. All blots ( a , c , d ) were performed as n = 1 independent experiments. For all GST control blots see Supplementary Fig. . Source data are provided as a source data file.
Alanine Mutant, supplied by Synbio Technologies LLC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/alanine+mutant/alanine+mutant/bio_rxiv__2020__09__28__317578-271-8-16
Average 90 stars, based on 1 article reviews
alanine mutant - by Bioz Stars, 2026-09
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quadruple alanine mutant  (GenScript corporation)
90
GenScript corporation quadruple alanine mutant
a Western blot analysis of cellular ubiquitin conjugates co-isolating in pulldowns of <t>StrepTagII-UBXD1</t> or only the StrepTagII peptide expressed in HEK293 cells as indicated. In presence of UBXD1, ubiquitin conjugates were detected. b UBXD1 constructs overexpressed in HEK293 and E. coli cells to narrow down the ubiquitin binding region. Domains color-coded as follows: N-terminus (1–133, dark blue) with VIM helix (50–65, gray), PUB domain (150–264, light blue) and UBX domain (333–411, pink). c Deletion of the UBX domain (333–411) abolishes ubiquitin binding by UBXD1. UBXD1 or indicated truncation variants were expressed in HEK293 cells and lysates used for ubiquitin-GST (Ub-GST) pulldowns. Co-isolated UBXD1 was detected with UBXD1-specific antibodies. d Ub-GST pulldowns with purified UBXD1, UBXD1-ΔLinker-UBX-C, UBXD1-Linker-UBX-C or UBXD1-PUB. All blots ( a , c , d ) were performed as n = 1 independent experiments. For all GST control blots see Supplementary Fig. . Source data are provided as a source data file.
Quadruple Alanine Mutant, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/alanine+mutant/quadruple+alanine+mutant/10__1158_slash_1541___7786__mcr___14___0088___t-52-10-14
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quadruple alanine mutant - by Bioz Stars, 2026-09
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gld-3 (879–894) single alanine point mutants  (GenScript corporation)
90
GenScript corporation gld-3 (879–894) single alanine point mutants
a Western blot analysis of cellular ubiquitin conjugates co-isolating in pulldowns of <t>StrepTagII-UBXD1</t> or only the StrepTagII peptide expressed in HEK293 cells as indicated. In presence of UBXD1, ubiquitin conjugates were detected. b UBXD1 constructs overexpressed in HEK293 and E. coli cells to narrow down the ubiquitin binding region. Domains color-coded as follows: N-terminus (1–133, dark blue) with VIM helix (50–65, gray), PUB domain (150–264, light blue) and UBX domain (333–411, pink). c Deletion of the UBX domain (333–411) abolishes ubiquitin binding by UBXD1. UBXD1 or indicated truncation variants were expressed in HEK293 cells and lysates used for ubiquitin-GST (Ub-GST) pulldowns. Co-isolated UBXD1 was detected with UBXD1-specific antibodies. d Ub-GST pulldowns with purified UBXD1, UBXD1-ΔLinker-UBX-C, UBXD1-Linker-UBX-C or UBXD1-PUB. All blots ( a , c , d ) were performed as n = 1 independent experiments. For all GST control blots see Supplementary Fig. . Source data are provided as a source data file.
Gld 3 (879–894) Single Alanine Point Mutants, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/alanine+mutant/gld+3++879+894++single+alanine+point+mutants/pmc03568228-378-5-23
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gld-3 (879–894) single alanine point mutants - by Bioz Stars, 2026-09
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Image Search Results


a Western blot analysis of cellular ubiquitin conjugates co-isolating in pulldowns of StrepTagII-UBXD1 or only the StrepTagII peptide expressed in HEK293 cells as indicated. In presence of UBXD1, ubiquitin conjugates were detected. b UBXD1 constructs overexpressed in HEK293 and E. coli cells to narrow down the ubiquitin binding region. Domains color-coded as follows: N-terminus (1–133, dark blue) with VIM helix (50–65, gray), PUB domain (150–264, light blue) and UBX domain (333–411, pink). c Deletion of the UBX domain (333–411) abolishes ubiquitin binding by UBXD1. UBXD1 or indicated truncation variants were expressed in HEK293 cells and lysates used for ubiquitin-GST (Ub-GST) pulldowns. Co-isolated UBXD1 was detected with UBXD1-specific antibodies. d Ub-GST pulldowns with purified UBXD1, UBXD1-ΔLinker-UBX-C, UBXD1-Linker-UBX-C or UBXD1-PUB. All blots ( a , c , d ) were performed as n = 1 independent experiments. For all GST control blots see Supplementary Fig. . Source data are provided as a source data file.

Journal: Nature Communications

Article Title: The UBX domain in UBXD1 organizes ubiquitin binding at the C-terminus of the VCP/p97 AAA-ATPase

doi: 10.1038/s41467-023-38604-4

Figure Lengend Snippet: a Western blot analysis of cellular ubiquitin conjugates co-isolating in pulldowns of StrepTagII-UBXD1 or only the StrepTagII peptide expressed in HEK293 cells as indicated. In presence of UBXD1, ubiquitin conjugates were detected. b UBXD1 constructs overexpressed in HEK293 and E. coli cells to narrow down the ubiquitin binding region. Domains color-coded as follows: N-terminus (1–133, dark blue) with VIM helix (50–65, gray), PUB domain (150–264, light blue) and UBX domain (333–411, pink). c Deletion of the UBX domain (333–411) abolishes ubiquitin binding by UBXD1. UBXD1 or indicated truncation variants were expressed in HEK293 cells and lysates used for ubiquitin-GST (Ub-GST) pulldowns. Co-isolated UBXD1 was detected with UBXD1-specific antibodies. d Ub-GST pulldowns with purified UBXD1, UBXD1-ΔLinker-UBX-C, UBXD1-Linker-UBX-C or UBXD1-PUB. All blots ( a , c , d ) were performed as n = 1 independent experiments. For all GST control blots see Supplementary Fig. . Source data are provided as a source data file.

Article Snippet: At a density of 50–60% cells are transfected with the UBXD1 plasmids (pcDNA3.1(+), StrepTagII, wt with aa 1–441, 1–411, 1–332, or 1–264, Gene synthesis by BioCat GmbH, Heidelberg, Germany) or empty vector with a StrepTagII with 293Free reagent and incubated for 24 h for overexpression of UBXD1 and disrupted with lysis buffer (PBS buffer, 0.05% Igepal, pH 7.4, Halt protease and phosphatase inhibitor cocktail (Cat. 78440, Thermo Scientific, Germany).

Techniques: Western Blot, Ubiquitin Proteomics, Construct, Binding Assay, Isolation, Purification, Control