achromobacter protease Search Results


achromobacter protease  (FUJIFILM)
90
FUJIFILM achromobacter protease
Achromobacter Protease, supplied by FUJIFILM, 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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achromobacter protease - by Bioz Stars, 2026-08
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lysylendopeptidase (achromobacter protease  (FUJIFILM)
90
FUJIFILM lysylendopeptidase (achromobacter protease
Identification of the 190-kDa protein in NM1 complexes as BRG1. (A) Physical map of identified or predicted domains of BRG1, adapted from reference 29. BRG1 has a 1,613-amino-acid open reading frame. BRG1, like other members of the Swi2 family, contains multiple motifs characteristic of helicases and ATPases, although helicase activity has not been detected in these proteins. The ATPase/helicase domain spans amino acid residues 774 to 1237, and the bromodomain spans amino acid residues 1448 to 1523. BRG1 also contains a functional retinoblastoma protein binding motif (LXCXE) encompassing residues 1322 to 1326 (16). (B) The sequences of eight peptides derived from micropeptide sequencing of gel-purified p190 isolated from human cells are represented on the top line of each pair. Dots between residues indicate identity with the cDNA-derived human BRG1 sequence. Uncertainties in the reading of the sequencing cycles are indicated by underlining; X indicates an unreadable cycle. Uncertainties and unreadable cycles were not counted as identities, although they may be matches. The enzyme used to digest p190 prior to sequencing <t>(lysylendopeptidase)</t> cuts almost exclusively at lysine residues, so that each peptide sequence is expected to be immediately preceded by a lysine (K). As shown in the BRG1 sequence, a lysine occurs in BRG1 at each position where it is predicted to occur in p190, increasing the percent identity in the match. R represents the amino acid number of the initial lysine residue in BRG1 as reported in Khavari et al. (29). Peptides were recovered from regions throughout BRG1. (C) NM1-precipitated proteins from HeLa cell lysates were separated by SDS-PAGE, transferred to nitrocellulose, and probed by Western blotting with a BRG1-specific amino-terminal antipeptide antibody (lane 2) or preimmune serum (lane 1).
Lysylendopeptidase (Achromobacter Protease, supplied by FUJIFILM, 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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Average 90 stars, based on 1 article reviews
lysylendopeptidase (achromobacter protease - by Bioz Stars, 2026-08
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achromobacter lyticus protease (lys-c  (FUJIFILM)
90
FUJIFILM achromobacter lyticus protease (lys-c
Identification of the 190-kDa protein in NM1 complexes as BRG1. (A) Physical map of identified or predicted domains of BRG1, adapted from reference 29. BRG1 has a 1,613-amino-acid open reading frame. BRG1, like other members of the Swi2 family, contains multiple motifs characteristic of helicases and ATPases, although helicase activity has not been detected in these proteins. The ATPase/helicase domain spans amino acid residues 774 to 1237, and the bromodomain spans amino acid residues 1448 to 1523. BRG1 also contains a functional retinoblastoma protein binding motif (LXCXE) encompassing residues 1322 to 1326 (16). (B) The sequences of eight peptides derived from micropeptide sequencing of gel-purified p190 isolated from human cells are represented on the top line of each pair. Dots between residues indicate identity with the cDNA-derived human BRG1 sequence. Uncertainties in the reading of the sequencing cycles are indicated by underlining; X indicates an unreadable cycle. Uncertainties and unreadable cycles were not counted as identities, although they may be matches. The enzyme used to digest p190 prior to sequencing <t>(lysylendopeptidase)</t> cuts almost exclusively at lysine residues, so that each peptide sequence is expected to be immediately preceded by a lysine (K). As shown in the BRG1 sequence, a lysine occurs in BRG1 at each position where it is predicted to occur in p190, increasing the percent identity in the match. R represents the amino acid number of the initial lysine residue in BRG1 as reported in Khavari et al. (29). Peptides were recovered from regions throughout BRG1. (C) NM1-precipitated proteins from HeLa cell lysates were separated by SDS-PAGE, transferred to nitrocellulose, and probed by Western blotting with a BRG1-specific amino-terminal antipeptide antibody (lane 2) or preimmune serum (lane 1).
Achromobacter Lyticus Protease (Lys C, supplied by FUJIFILM, 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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Average 90 stars, based on 1 article reviews
achromobacter lyticus protease (lys-c - by Bioz Stars, 2026-08
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20 ng/ l achromobacter protease i (api)  (FUJIFILM)
90
FUJIFILM 20 ng/ l achromobacter protease i (api)
Identification of the 190-kDa protein in NM1 complexes as BRG1. (A) Physical map of identified or predicted domains of BRG1, adapted from reference 29. BRG1 has a 1,613-amino-acid open reading frame. BRG1, like other members of the Swi2 family, contains multiple motifs characteristic of helicases and ATPases, although helicase activity has not been detected in these proteins. The ATPase/helicase domain spans amino acid residues 774 to 1237, and the bromodomain spans amino acid residues 1448 to 1523. BRG1 also contains a functional retinoblastoma protein binding motif (LXCXE) encompassing residues 1322 to 1326 (16). (B) The sequences of eight peptides derived from micropeptide sequencing of gel-purified p190 isolated from human cells are represented on the top line of each pair. Dots between residues indicate identity with the cDNA-derived human BRG1 sequence. Uncertainties in the reading of the sequencing cycles are indicated by underlining; X indicates an unreadable cycle. Uncertainties and unreadable cycles were not counted as identities, although they may be matches. The enzyme used to digest p190 prior to sequencing <t>(lysylendopeptidase)</t> cuts almost exclusively at lysine residues, so that each peptide sequence is expected to be immediately preceded by a lysine (K). As shown in the BRG1 sequence, a lysine occurs in BRG1 at each position where it is predicted to occur in p190, increasing the percent identity in the match. R represents the amino acid number of the initial lysine residue in BRG1 as reported in Khavari et al. (29). Peptides were recovered from regions throughout BRG1. (C) NM1-precipitated proteins from HeLa cell lysates were separated by SDS-PAGE, transferred to nitrocellulose, and probed by Western blotting with a BRG1-specific amino-terminal antipeptide antibody (lane 2) or preimmune serum (lane 1).
20 Ng/ L Achromobacter Protease I (Api), supplied by FUJIFILM, 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/achromobacter+protease/10__1128_slash_aem__01978___06-130-10-16?v=FUJIFILM
Average 90 stars, based on 1 article reviews
20 ng/ l achromobacter protease i (api) - by Bioz Stars, 2026-08
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0.5 mg of achromobacter lyticus protease lys-c  (FUJIFILM)
90
FUJIFILM 0.5 mg of achromobacter lyticus protease lys-c
Identification of the 190-kDa protein in NM1 complexes as BRG1. (A) Physical map of identified or predicted domains of BRG1, adapted from reference 29. BRG1 has a 1,613-amino-acid open reading frame. BRG1, like other members of the Swi2 family, contains multiple motifs characteristic of helicases and ATPases, although helicase activity has not been detected in these proteins. The ATPase/helicase domain spans amino acid residues 774 to 1237, and the bromodomain spans amino acid residues 1448 to 1523. BRG1 also contains a functional retinoblastoma protein binding motif (LXCXE) encompassing residues 1322 to 1326 (16). (B) The sequences of eight peptides derived from micropeptide sequencing of gel-purified p190 isolated from human cells are represented on the top line of each pair. Dots between residues indicate identity with the cDNA-derived human BRG1 sequence. Uncertainties in the reading of the sequencing cycles are indicated by underlining; X indicates an unreadable cycle. Uncertainties and unreadable cycles were not counted as identities, although they may be matches. The enzyme used to digest p190 prior to sequencing <t>(lysylendopeptidase)</t> cuts almost exclusively at lysine residues, so that each peptide sequence is expected to be immediately preceded by a lysine (K). As shown in the BRG1 sequence, a lysine occurs in BRG1 at each position where it is predicted to occur in p190, increasing the percent identity in the match. R represents the amino acid number of the initial lysine residue in BRG1 as reported in Khavari et al. (29). Peptides were recovered from regions throughout BRG1. (C) NM1-precipitated proteins from HeLa cell lysates were separated by SDS-PAGE, transferred to nitrocellulose, and probed by Western blotting with a BRG1-specific amino-terminal antipeptide antibody (lane 2) or preimmune serum (lane 1).
0.5 Mg Of Achromobacter Lyticus Protease Lys C, supplied by FUJIFILM, 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/achromobacter+protease/10__1074_slash_jbc__273__8__4329-142-13-17?v=FUJIFILM
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0.5 mg of achromobacter lyticus protease lys-c - by Bioz Stars, 2026-08
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achromobacter protease i  (Ohta s Isan Co Ltd)
90
Ohta s Isan Co Ltd achromobacter protease i
Identification of the 190-kDa protein in NM1 complexes as BRG1. (A) Physical map of identified or predicted domains of BRG1, adapted from reference 29. BRG1 has a 1,613-amino-acid open reading frame. BRG1, like other members of the Swi2 family, contains multiple motifs characteristic of helicases and ATPases, although helicase activity has not been detected in these proteins. The ATPase/helicase domain spans amino acid residues 774 to 1237, and the bromodomain spans amino acid residues 1448 to 1523. BRG1 also contains a functional retinoblastoma protein binding motif (LXCXE) encompassing residues 1322 to 1326 (16). (B) The sequences of eight peptides derived from micropeptide sequencing of gel-purified p190 isolated from human cells are represented on the top line of each pair. Dots between residues indicate identity with the cDNA-derived human BRG1 sequence. Uncertainties in the reading of the sequencing cycles are indicated by underlining; X indicates an unreadable cycle. Uncertainties and unreadable cycles were not counted as identities, although they may be matches. The enzyme used to digest p190 prior to sequencing <t>(lysylendopeptidase)</t> cuts almost exclusively at lysine residues, so that each peptide sequence is expected to be immediately preceded by a lysine (K). As shown in the BRG1 sequence, a lysine occurs in BRG1 at each position where it is predicted to occur in p190, increasing the percent identity in the match. R represents the amino acid number of the initial lysine residue in BRG1 as reported in Khavari et al. (29). Peptides were recovered from regions throughout BRG1. (C) NM1-precipitated proteins from HeLa cell lysates were separated by SDS-PAGE, transferred to nitrocellulose, and probed by Western blotting with a BRG1-specific amino-terminal antipeptide antibody (lane 2) or preimmune serum (lane 1).
Achromobacter Protease I, supplied by Ohta s Isan Co Ltd, 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/achromobacter+protease/pm26431800-208-36-15?v=Ohta+s+Isan+Co+Ltd
Average 90 stars, based on 1 article reviews
achromobacter protease i - by Bioz Stars, 2026-08
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20 mg/ml achromobacter protease i  (FUJIFILM)
90
FUJIFILM 20 mg/ml achromobacter protease i
Identification of the 190-kDa protein in NM1 complexes as BRG1. (A) Physical map of identified or predicted domains of BRG1, adapted from reference 29. BRG1 has a 1,613-amino-acid open reading frame. BRG1, like other members of the Swi2 family, contains multiple motifs characteristic of helicases and ATPases, although helicase activity has not been detected in these proteins. The ATPase/helicase domain spans amino acid residues 774 to 1237, and the bromodomain spans amino acid residues 1448 to 1523. BRG1 also contains a functional retinoblastoma protein binding motif (LXCXE) encompassing residues 1322 to 1326 (16). (B) The sequences of eight peptides derived from micropeptide sequencing of gel-purified p190 isolated from human cells are represented on the top line of each pair. Dots between residues indicate identity with the cDNA-derived human BRG1 sequence. Uncertainties in the reading of the sequencing cycles are indicated by underlining; X indicates an unreadable cycle. Uncertainties and unreadable cycles were not counted as identities, although they may be matches. The enzyme used to digest p190 prior to sequencing <t>(lysylendopeptidase)</t> cuts almost exclusively at lysine residues, so that each peptide sequence is expected to be immediately preceded by a lysine (K). As shown in the BRG1 sequence, a lysine occurs in BRG1 at each position where it is predicted to occur in p190, increasing the percent identity in the match. R represents the amino acid number of the initial lysine residue in BRG1 as reported in Khavari et al. (29). Peptides were recovered from regions throughout BRG1. (C) NM1-precipitated proteins from HeLa cell lysates were separated by SDS-PAGE, transferred to nitrocellulose, and probed by Western blotting with a BRG1-specific amino-terminal antipeptide antibody (lane 2) or preimmune serum (lane 1).
20 Mg/Ml Achromobacter Protease I, supplied by FUJIFILM, 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/achromobacter+protease/pm15981298-52-19-22?v=FUJIFILM
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20 mg/ml achromobacter protease i - by Bioz Stars, 2026-08
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Image Search Results


Identification of the 190-kDa protein in NM1 complexes as BRG1. (A) Physical map of identified or predicted domains of BRG1, adapted from reference 29. BRG1 has a 1,613-amino-acid open reading frame. BRG1, like other members of the Swi2 family, contains multiple motifs characteristic of helicases and ATPases, although helicase activity has not been detected in these proteins. The ATPase/helicase domain spans amino acid residues 774 to 1237, and the bromodomain spans amino acid residues 1448 to 1523. BRG1 also contains a functional retinoblastoma protein binding motif (LXCXE) encompassing residues 1322 to 1326 (16). (B) The sequences of eight peptides derived from micropeptide sequencing of gel-purified p190 isolated from human cells are represented on the top line of each pair. Dots between residues indicate identity with the cDNA-derived human BRG1 sequence. Uncertainties in the reading of the sequencing cycles are indicated by underlining; X indicates an unreadable cycle. Uncertainties and unreadable cycles were not counted as identities, although they may be matches. The enzyme used to digest p190 prior to sequencing (lysylendopeptidase) cuts almost exclusively at lysine residues, so that each peptide sequence is expected to be immediately preceded by a lysine (K). As shown in the BRG1 sequence, a lysine occurs in BRG1 at each position where it is predicted to occur in p190, increasing the percent identity in the match. R represents the amino acid number of the initial lysine residue in BRG1 as reported in Khavari et al. (29). Peptides were recovered from regions throughout BRG1. (C) NM1-precipitated proteins from HeLa cell lysates were separated by SDS-PAGE, transferred to nitrocellulose, and probed by Western blotting with a BRG1-specific amino-terminal antipeptide antibody (lane 2) or preimmune serum (lane 1).

Journal:

Article Title: p300/CREB Binding Protein-Related Protein p270 Is a Component of Mammalian SWI/SNF Complexes

doi:

Figure Lengend Snippet: Identification of the 190-kDa protein in NM1 complexes as BRG1. (A) Physical map of identified or predicted domains of BRG1, adapted from reference 29. BRG1 has a 1,613-amino-acid open reading frame. BRG1, like other members of the Swi2 family, contains multiple motifs characteristic of helicases and ATPases, although helicase activity has not been detected in these proteins. The ATPase/helicase domain spans amino acid residues 774 to 1237, and the bromodomain spans amino acid residues 1448 to 1523. BRG1 also contains a functional retinoblastoma protein binding motif (LXCXE) encompassing residues 1322 to 1326 (16). (B) The sequences of eight peptides derived from micropeptide sequencing of gel-purified p190 isolated from human cells are represented on the top line of each pair. Dots between residues indicate identity with the cDNA-derived human BRG1 sequence. Uncertainties in the reading of the sequencing cycles are indicated by underlining; X indicates an unreadable cycle. Uncertainties and unreadable cycles were not counted as identities, although they may be matches. The enzyme used to digest p190 prior to sequencing (lysylendopeptidase) cuts almost exclusively at lysine residues, so that each peptide sequence is expected to be immediately preceded by a lysine (K). As shown in the BRG1 sequence, a lysine occurs in BRG1 at each position where it is predicted to occur in p190, increasing the percent identity in the match. R represents the amino acid number of the initial lysine residue in BRG1 as reported in Khavari et al. (29). Peptides were recovered from regions throughout BRG1. (C) NM1-precipitated proteins from HeLa cell lysates were separated by SDS-PAGE, transferred to nitrocellulose, and probed by Western blotting with a BRG1-specific amino-terminal antipeptide antibody (lane 2) or preimmune serum (lane 1).

Article Snippet: The gel fragments containing the p270, p190, p170, and p155 bands were excised and digested with lysylendopeptidase ( Achromobacter protease I; Wako).

Techniques: Activity Assay, Functional Assay, Protein Binding, Derivative Assay, Sequencing, Purification, Isolation, SDS Page, Western Blot