nac Search Results


n acetylcysteine  (MedChemExpress)
96
MedChemExpress n acetylcysteine
N Acetylcysteine, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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n acetylcysteine  (TargetMol)
99
TargetMol n acetylcysteine
N Acetylcysteine, supplied by TargetMol, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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n acetyl l cysteine  (Valiant Co Ltd)
93
Valiant Co Ltd n acetyl l cysteine
N Acetyl L Cysteine, supplied by Valiant Co Ltd, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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nlrp1  (Proteintech)
93
Proteintech nlrp1
Nlrp1, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ck nac activated kit  (Randox)
93
Randox ck nac activated kit
Ck Nac Activated Kit, supplied by Randox, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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plasmid expressing tev protease  (Addgene inc)
93
Addgene inc plasmid expressing tev protease
Expression and purification <t>of</t> <t>H-Siglec-15</t> (20-263aa). ( A ) Schematic representation of the plasmids used for the expression of H-Siglec-15 (20-263aa)-Fc. ( B ) The expression of H-Siglec-15 (20-263aa)-Fc (approximately 220 kDa) in the culture supernatant of Expi293F cells was analyzed by SDS-PAGE and Coomassie blue staining. Samples 1–4 represent the culture supernatants collected on the third, fourth, fifth, and sixth days posttransfection, respectively. Sample 5 included the culture supernatant and cell precipitate from the sixth day, whereas samples 6 and 7 included the flow-through and elution of H-Siglec-15 (20-263aa)-Fc, respectively. Sample 8 was the cleaning solution, and sample 9 was the protein concentrate. M denotes the molecular weight marker. ( C ) Western blot analysis of H-Siglec-15 (20-263aa)-Fc expression in the culture supernatant of Expi293F cells. Samples 1–9 correspond to the same samples as in B , with M indicating the molecular weight marker. ( D ) The expression of <t>TEV</t> protease (approximately 30 kDa) was detected by SDS-PAGE and Coomassie blue staining. Samples 10 and 11 represent the precipitate and supernatant following cell lysis, whereas samples 12, 13, 14, and 15 represent the flow-through and elution at 20 mM, 80 mM, and 200 mM imidazole, respectively. M denotes the molecular weight marker. ( E ) Cleavage of the H-Siglec-15 (20-263aa)-Fc protein by the TEV protease was analyzed via SDS-PAGE and Coomassie blue staining. Sample 16 contains the uncleaved H-Siglec-15 (20-263aa)-Fc protein (220 kDa), whereas sample 17 contains the cleaved H-Siglec-15 (20-263aa) protein (approximately 27 kDa). Sample 18 was the concentrated cleaved H-Siglec-15 (20-263aa) protein. M denotes the molecular weight marker. ( F ) Cleavage of the H-Siglec-15 (20-263aa)-Fc protein by the TEV protease was confirmed by Western blot analysis. Samples 19–21 correspond to the same samples as in E , with M indicating the molecular weight marker
Plasmid Expressing Tev Protease, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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multisite gateway tol2 kit compatible pme  (Addgene inc)
93
Addgene inc multisite gateway tol2 kit compatible pme
Expression and purification <t>of</t> <t>H-Siglec-15</t> (20-263aa). ( A ) Schematic representation of the plasmids used for the expression of H-Siglec-15 (20-263aa)-Fc. ( B ) The expression of H-Siglec-15 (20-263aa)-Fc (approximately 220 kDa) in the culture supernatant of Expi293F cells was analyzed by SDS-PAGE and Coomassie blue staining. Samples 1–4 represent the culture supernatants collected on the third, fourth, fifth, and sixth days posttransfection, respectively. Sample 5 included the culture supernatant and cell precipitate from the sixth day, whereas samples 6 and 7 included the flow-through and elution of H-Siglec-15 (20-263aa)-Fc, respectively. Sample 8 was the cleaning solution, and sample 9 was the protein concentrate. M denotes the molecular weight marker. ( C ) Western blot analysis of H-Siglec-15 (20-263aa)-Fc expression in the culture supernatant of Expi293F cells. Samples 1–9 correspond to the same samples as in B , with M indicating the molecular weight marker. ( D ) The expression of <t>TEV</t> protease (approximately 30 kDa) was detected by SDS-PAGE and Coomassie blue staining. Samples 10 and 11 represent the precipitate and supernatant following cell lysis, whereas samples 12, 13, 14, and 15 represent the flow-through and elution at 20 mM, 80 mM, and 200 mM imidazole, respectively. M denotes the molecular weight marker. ( E ) Cleavage of the H-Siglec-15 (20-263aa)-Fc protein by the TEV protease was analyzed via SDS-PAGE and Coomassie blue staining. Sample 16 contains the uncleaved H-Siglec-15 (20-263aa)-Fc protein (220 kDa), whereas sample 17 contains the cleaved H-Siglec-15 (20-263aa) protein (approximately 27 kDa). Sample 18 was the concentrated cleaved H-Siglec-15 (20-263aa) protein. M denotes the molecular weight marker. ( F ) Cleavage of the H-Siglec-15 (20-263aa)-Fc protein by the TEV protease was confirmed by Western blot analysis. Samples 19–21 correspond to the same samples as in E , with M indicating the molecular weight marker
Multisite Gateway Tol2 Kit Compatible Pme, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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malonyl nac  (MedChemExpress)
93
MedChemExpress malonyl nac
Expression and purification <t>of</t> <t>H-Siglec-15</t> (20-263aa). ( A ) Schematic representation of the plasmids used for the expression of H-Siglec-15 (20-263aa)-Fc. ( B ) The expression of H-Siglec-15 (20-263aa)-Fc (approximately 220 kDa) in the culture supernatant of Expi293F cells was analyzed by SDS-PAGE and Coomassie blue staining. Samples 1–4 represent the culture supernatants collected on the third, fourth, fifth, and sixth days posttransfection, respectively. Sample 5 included the culture supernatant and cell precipitate from the sixth day, whereas samples 6 and 7 included the flow-through and elution of H-Siglec-15 (20-263aa)-Fc, respectively. Sample 8 was the cleaning solution, and sample 9 was the protein concentrate. M denotes the molecular weight marker. ( C ) Western blot analysis of H-Siglec-15 (20-263aa)-Fc expression in the culture supernatant of Expi293F cells. Samples 1–9 correspond to the same samples as in B , with M indicating the molecular weight marker. ( D ) The expression of <t>TEV</t> protease (approximately 30 kDa) was detected by SDS-PAGE and Coomassie blue staining. Samples 10 and 11 represent the precipitate and supernatant following cell lysis, whereas samples 12, 13, 14, and 15 represent the flow-through and elution at 20 mM, 80 mM, and 200 mM imidazole, respectively. M denotes the molecular weight marker. ( E ) Cleavage of the H-Siglec-15 (20-263aa)-Fc protein by the TEV protease was analyzed via SDS-PAGE and Coomassie blue staining. Sample 16 contains the uncleaved H-Siglec-15 (20-263aa)-Fc protein (220 kDa), whereas sample 17 contains the cleaved H-Siglec-15 (20-263aa) protein (approximately 27 kDa). Sample 18 was the concentrated cleaved H-Siglec-15 (20-263aa) protein. M denotes the molecular weight marker. ( F ) Cleavage of the H-Siglec-15 (20-263aa)-Fc protein by the TEV protease was confirmed by Western blot analysis. Samples 19–21 correspond to the same samples as in E , with M indicating the molecular weight marker
Malonyl Nac, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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incubation with anti nacc1  (Proteintech)
92
Proteintech incubation with anti nacc1
Expression and purification <t>of</t> <t>H-Siglec-15</t> (20-263aa). ( A ) Schematic representation of the plasmids used for the expression of H-Siglec-15 (20-263aa)-Fc. ( B ) The expression of H-Siglec-15 (20-263aa)-Fc (approximately 220 kDa) in the culture supernatant of Expi293F cells was analyzed by SDS-PAGE and Coomassie blue staining. Samples 1–4 represent the culture supernatants collected on the third, fourth, fifth, and sixth days posttransfection, respectively. Sample 5 included the culture supernatant and cell precipitate from the sixth day, whereas samples 6 and 7 included the flow-through and elution of H-Siglec-15 (20-263aa)-Fc, respectively. Sample 8 was the cleaning solution, and sample 9 was the protein concentrate. M denotes the molecular weight marker. ( C ) Western blot analysis of H-Siglec-15 (20-263aa)-Fc expression in the culture supernatant of Expi293F cells. Samples 1–9 correspond to the same samples as in B , with M indicating the molecular weight marker. ( D ) The expression of <t>TEV</t> protease (approximately 30 kDa) was detected by SDS-PAGE and Coomassie blue staining. Samples 10 and 11 represent the precipitate and supernatant following cell lysis, whereas samples 12, 13, 14, and 15 represent the flow-through and elution at 20 mM, 80 mM, and 200 mM imidazole, respectively. M denotes the molecular weight marker. ( E ) Cleavage of the H-Siglec-15 (20-263aa)-Fc protein by the TEV protease was analyzed via SDS-PAGE and Coomassie blue staining. Sample 16 contains the uncleaved H-Siglec-15 (20-263aa)-Fc protein (220 kDa), whereas sample 17 contains the cleaved H-Siglec-15 (20-263aa) protein (approximately 27 kDa). Sample 18 was the concentrated cleaved H-Siglec-15 (20-263aa) protein. M denotes the molecular weight marker. ( F ) Cleavage of the H-Siglec-15 (20-263aa)-Fc protein by the TEV protease was confirmed by Western blot analysis. Samples 19–21 correspond to the same samples as in E , with M indicating the molecular weight marker
Incubation With Anti Nacc1, supplied by Proteintech, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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cho k1 galnact cells  (OriGene)
90
OriGene cho k1 galnact cells
Expression and purification <t>of</t> <t>H-Siglec-15</t> (20-263aa). ( A ) Schematic representation of the plasmids used for the expression of H-Siglec-15 (20-263aa)-Fc. ( B ) The expression of H-Siglec-15 (20-263aa)-Fc (approximately 220 kDa) in the culture supernatant of Expi293F cells was analyzed by SDS-PAGE and Coomassie blue staining. Samples 1–4 represent the culture supernatants collected on the third, fourth, fifth, and sixth days posttransfection, respectively. Sample 5 included the culture supernatant and cell precipitate from the sixth day, whereas samples 6 and 7 included the flow-through and elution of H-Siglec-15 (20-263aa)-Fc, respectively. Sample 8 was the cleaning solution, and sample 9 was the protein concentrate. M denotes the molecular weight marker. ( C ) Western blot analysis of H-Siglec-15 (20-263aa)-Fc expression in the culture supernatant of Expi293F cells. Samples 1–9 correspond to the same samples as in B , with M indicating the molecular weight marker. ( D ) The expression of <t>TEV</t> protease (approximately 30 kDa) was detected by SDS-PAGE and Coomassie blue staining. Samples 10 and 11 represent the precipitate and supernatant following cell lysis, whereas samples 12, 13, 14, and 15 represent the flow-through and elution at 20 mM, 80 mM, and 200 mM imidazole, respectively. M denotes the molecular weight marker. ( E ) Cleavage of the H-Siglec-15 (20-263aa)-Fc protein by the TEV protease was analyzed via SDS-PAGE and Coomassie blue staining. Sample 16 contains the uncleaved H-Siglec-15 (20-263aa)-Fc protein (220 kDa), whereas sample 17 contains the cleaved H-Siglec-15 (20-263aa) protein (approximately 27 kDa). Sample 18 was the concentrated cleaved H-Siglec-15 (20-263aa) protein. M denotes the molecular weight marker. ( F ) Cleavage of the H-Siglec-15 (20-263aa)-Fc protein by the TEV protease was confirmed by Western blot analysis. Samples 19–21 correspond to the same samples as in E , with M indicating the molecular weight marker
Cho K1 Galnact Cells, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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alizarin red  (Chem Impex International)
95
Chem Impex International alizarin red
Expression and purification <t>of</t> <t>H-Siglec-15</t> (20-263aa). ( A ) Schematic representation of the plasmids used for the expression of H-Siglec-15 (20-263aa)-Fc. ( B ) The expression of H-Siglec-15 (20-263aa)-Fc (approximately 220 kDa) in the culture supernatant of Expi293F cells was analyzed by SDS-PAGE and Coomassie blue staining. Samples 1–4 represent the culture supernatants collected on the third, fourth, fifth, and sixth days posttransfection, respectively. Sample 5 included the culture supernatant and cell precipitate from the sixth day, whereas samples 6 and 7 included the flow-through and elution of H-Siglec-15 (20-263aa)-Fc, respectively. Sample 8 was the cleaning solution, and sample 9 was the protein concentrate. M denotes the molecular weight marker. ( C ) Western blot analysis of H-Siglec-15 (20-263aa)-Fc expression in the culture supernatant of Expi293F cells. Samples 1–9 correspond to the same samples as in B , with M indicating the molecular weight marker. ( D ) The expression of <t>TEV</t> protease (approximately 30 kDa) was detected by SDS-PAGE and Coomassie blue staining. Samples 10 and 11 represent the precipitate and supernatant following cell lysis, whereas samples 12, 13, 14, and 15 represent the flow-through and elution at 20 mM, 80 mM, and 200 mM imidazole, respectively. M denotes the molecular weight marker. ( E ) Cleavage of the H-Siglec-15 (20-263aa)-Fc protein by the TEV protease was analyzed via SDS-PAGE and Coomassie blue staining. Sample 16 contains the uncleaved H-Siglec-15 (20-263aa)-Fc protein (220 kDa), whereas sample 17 contains the cleaved H-Siglec-15 (20-263aa) protein (approximately 27 kDa). Sample 18 was the concentrated cleaved H-Siglec-15 (20-263aa) protein. M denotes the molecular weight marker. ( F ) Cleavage of the H-Siglec-15 (20-263aa)-Fc protein by the TEV protease was confirmed by Western blot analysis. Samples 19–21 correspond to the same samples as in E , with M indicating the molecular weight marker
Alizarin Red, supplied by Chem Impex International, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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j broichhagen myc gbai addgene  (Addgene inc)
92
Addgene inc j broichhagen myc gbai addgene
Expression and purification <t>of</t> <t>H-Siglec-15</t> (20-263aa). ( A ) Schematic representation of the plasmids used for the expression of H-Siglec-15 (20-263aa)-Fc. ( B ) The expression of H-Siglec-15 (20-263aa)-Fc (approximately 220 kDa) in the culture supernatant of Expi293F cells was analyzed by SDS-PAGE and Coomassie blue staining. Samples 1–4 represent the culture supernatants collected on the third, fourth, fifth, and sixth days posttransfection, respectively. Sample 5 included the culture supernatant and cell precipitate from the sixth day, whereas samples 6 and 7 included the flow-through and elution of H-Siglec-15 (20-263aa)-Fc, respectively. Sample 8 was the cleaning solution, and sample 9 was the protein concentrate. M denotes the molecular weight marker. ( C ) Western blot analysis of H-Siglec-15 (20-263aa)-Fc expression in the culture supernatant of Expi293F cells. Samples 1–9 correspond to the same samples as in B , with M indicating the molecular weight marker. ( D ) The expression of <t>TEV</t> protease (approximately 30 kDa) was detected by SDS-PAGE and Coomassie blue staining. Samples 10 and 11 represent the precipitate and supernatant following cell lysis, whereas samples 12, 13, 14, and 15 represent the flow-through and elution at 20 mM, 80 mM, and 200 mM imidazole, respectively. M denotes the molecular weight marker. ( E ) Cleavage of the H-Siglec-15 (20-263aa)-Fc protein by the TEV protease was analyzed via SDS-PAGE and Coomassie blue staining. Sample 16 contains the uncleaved H-Siglec-15 (20-263aa)-Fc protein (220 kDa), whereas sample 17 contains the cleaved H-Siglec-15 (20-263aa) protein (approximately 27 kDa). Sample 18 was the concentrated cleaved H-Siglec-15 (20-263aa) protein. M denotes the molecular weight marker. ( F ) Cleavage of the H-Siglec-15 (20-263aa)-Fc protein by the TEV protease was confirmed by Western blot analysis. Samples 19–21 correspond to the same samples as in E , with M indicating the molecular weight marker
J Broichhagen Myc Gbai Addgene, supplied by Addgene inc, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Expression and purification of H-Siglec-15 (20-263aa). ( A ) Schematic representation of the plasmids used for the expression of H-Siglec-15 (20-263aa)-Fc. ( B ) The expression of H-Siglec-15 (20-263aa)-Fc (approximately 220 kDa) in the culture supernatant of Expi293F cells was analyzed by SDS-PAGE and Coomassie blue staining. Samples 1–4 represent the culture supernatants collected on the third, fourth, fifth, and sixth days posttransfection, respectively. Sample 5 included the culture supernatant and cell precipitate from the sixth day, whereas samples 6 and 7 included the flow-through and elution of H-Siglec-15 (20-263aa)-Fc, respectively. Sample 8 was the cleaning solution, and sample 9 was the protein concentrate. M denotes the molecular weight marker. ( C ) Western blot analysis of H-Siglec-15 (20-263aa)-Fc expression in the culture supernatant of Expi293F cells. Samples 1–9 correspond to the same samples as in B , with M indicating the molecular weight marker. ( D ) The expression of TEV protease (approximately 30 kDa) was detected by SDS-PAGE and Coomassie blue staining. Samples 10 and 11 represent the precipitate and supernatant following cell lysis, whereas samples 12, 13, 14, and 15 represent the flow-through and elution at 20 mM, 80 mM, and 200 mM imidazole, respectively. M denotes the molecular weight marker. ( E ) Cleavage of the H-Siglec-15 (20-263aa)-Fc protein by the TEV protease was analyzed via SDS-PAGE and Coomassie blue staining. Sample 16 contains the uncleaved H-Siglec-15 (20-263aa)-Fc protein (220 kDa), whereas sample 17 contains the cleaved H-Siglec-15 (20-263aa) protein (approximately 27 kDa). Sample 18 was the concentrated cleaved H-Siglec-15 (20-263aa) protein. M denotes the molecular weight marker. ( F ) Cleavage of the H-Siglec-15 (20-263aa)-Fc protein by the TEV protease was confirmed by Western blot analysis. Samples 19–21 correspond to the same samples as in E , with M indicating the molecular weight marker

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: Siglec-15 is a putative receptor for porcine epidemic diarrhea virus infection

doi: 10.1007/s00018-025-05672-2

Figure Lengend Snippet: Expression and purification of H-Siglec-15 (20-263aa). ( A ) Schematic representation of the plasmids used for the expression of H-Siglec-15 (20-263aa)-Fc. ( B ) The expression of H-Siglec-15 (20-263aa)-Fc (approximately 220 kDa) in the culture supernatant of Expi293F cells was analyzed by SDS-PAGE and Coomassie blue staining. Samples 1–4 represent the culture supernatants collected on the third, fourth, fifth, and sixth days posttransfection, respectively. Sample 5 included the culture supernatant and cell precipitate from the sixth day, whereas samples 6 and 7 included the flow-through and elution of H-Siglec-15 (20-263aa)-Fc, respectively. Sample 8 was the cleaning solution, and sample 9 was the protein concentrate. M denotes the molecular weight marker. ( C ) Western blot analysis of H-Siglec-15 (20-263aa)-Fc expression in the culture supernatant of Expi293F cells. Samples 1–9 correspond to the same samples as in B , with M indicating the molecular weight marker. ( D ) The expression of TEV protease (approximately 30 kDa) was detected by SDS-PAGE and Coomassie blue staining. Samples 10 and 11 represent the precipitate and supernatant following cell lysis, whereas samples 12, 13, 14, and 15 represent the flow-through and elution at 20 mM, 80 mM, and 200 mM imidazole, respectively. M denotes the molecular weight marker. ( E ) Cleavage of the H-Siglec-15 (20-263aa)-Fc protein by the TEV protease was analyzed via SDS-PAGE and Coomassie blue staining. Sample 16 contains the uncleaved H-Siglec-15 (20-263aa)-Fc protein (220 kDa), whereas sample 17 contains the cleaved H-Siglec-15 (20-263aa) protein (approximately 27 kDa). Sample 18 was the concentrated cleaved H-Siglec-15 (20-263aa) protein. M denotes the molecular weight marker. ( F ) Cleavage of the H-Siglec-15 (20-263aa)-Fc protein by the TEV protease was confirmed by Western blot analysis. Samples 19–21 correspond to the same samples as in E , with M indicating the molecular weight marker

Article Snippet: The helper plasmids pCMV-VSV-G (#8454) and pSPAX2 for packaging lentivirus (#12260), the plasmid pX459 (#48139) for Siglec-15 knockout and the plasmid expressing TEV protease (pET28-MBP-super TEV protease) (#171782) were obtained from Addgene (Boston, MA, USA).

Techniques: Expressing, Purification, SDS Page, Staining, Molecular Weight, Marker, Western Blot, Lysis