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anti u2af 65 antibody  (Santa Cruz Biotechnology)


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    Santa Cruz Biotechnology anti u2af 65 antibody
    Anti U2af 65 Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 89 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti u2af 65 antibody/product/Santa Cruz Biotechnology
    Average 93 stars, based on 89 article reviews
    anti u2af 65 antibody - by Bioz Stars, 2026-03
    93/100 stars

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    Domains of UHM and ULM-containing proteins relevant to this study. A, human CAPERα (NCBI RefSeq NP_004893) compared with human paralogues CAPERβ (NP_060577), U2AF65 (NP_009210), Puf60 (NP_001258027), and SPF45 (NP_001139019). B, human ULM-containing splicing factors SF1 (NP_004621) and SF3b155 (NP_036565). Circled P, phosphorylated SF1 SPSP motif. HEAT, helical repeats; KH-QUA2, K-Homology Quaking-Homology-2; RS, arginine-serine-rich; RRM, RNA recognition motif (blue); UHM, <t>U2AF</t> homology motif (cyan); ULM, U2AF ligand motif (magenta); Zn, zinc knuckle. Sequence boundaries of domains relevant to this study and the residue numbers of C termini are indicated above. C, ULM “consensus” compared with known sequences of human splicing factor ULMs. ULM tryptophans are highlighted in yellow.
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    Domains of UHM and ULM-containing proteins relevant to this study. A, human CAPERα (NCBI RefSeq NP_004893) compared with human paralogues CAPERβ (NP_060577), U2AF65 (NP_009210), Puf60 (NP_001258027), and SPF45 (NP_001139019). B, human ULM-containing splicing factors SF1 (NP_004621) and SF3b155 (NP_036565). Circled P, phosphorylated SF1 SPSP motif. HEAT, helical repeats; KH-QUA2, K-Homology Quaking-Homology-2; RS, arginine-serine-rich; RRM, RNA recognition motif (blue); UHM, <t>U2AF</t> homology motif (cyan); ULM, U2AF ligand motif (magenta); Zn, zinc knuckle. Sequence boundaries of domains relevant to this study and the residue numbers of C termini are indicated above. C, ULM “consensus” compared with known sequences of human splicing factor ULMs. ULM tryptophans are highlighted in yellow.
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    anti u2af 65  (Santa Cruz Biotechnology)
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    Domains of UHM and ULM-containing proteins relevant to this study. A, human CAPERα (NCBI RefSeq NP_004893) compared with human paralogues CAPERβ (NP_060577), U2AF65 (NP_009210), Puf60 (NP_001258027), and SPF45 (NP_001139019). B, human ULM-containing splicing factors SF1 (NP_004621) and SF3b155 (NP_036565). Circled P, phosphorylated SF1 SPSP motif. HEAT, helical repeats; KH-QUA2, K-Homology Quaking-Homology-2; RS, arginine-serine-rich; RRM, RNA recognition motif (blue); UHM, <t>U2AF</t> homology motif (cyan); ULM, U2AF ligand motif (magenta); Zn, zinc knuckle. Sequence boundaries of domains relevant to this study and the residue numbers of C termini are indicated above. C, ULM “consensus” compared with known sequences of human splicing factor ULMs. ULM tryptophans are highlighted in yellow.
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    anti-u2af 65  (Santa Cruz Biotechnology)
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    Domains of UHM and ULM-containing proteins relevant to this study. A, human CAPERα (NCBI RefSeq NP_004893) compared with human paralogues CAPERβ (NP_060577), U2AF65 (NP_009210), Puf60 (NP_001258027), and SPF45 (NP_001139019). B, human ULM-containing splicing factors SF1 (NP_004621) and SF3b155 (NP_036565). Circled P, phosphorylated SF1 SPSP motif. HEAT, helical repeats; KH-QUA2, K-Homology Quaking-Homology-2; RS, arginine-serine-rich; RRM, RNA recognition motif (blue); UHM, <t>U2AF</t> homology motif (cyan); ULM, U2AF ligand motif (magenta); Zn, zinc knuckle. Sequence boundaries of domains relevant to this study and the residue numbers of C termini are indicated above. C, ULM “consensus” compared with known sequences of human splicing factor ULMs. ULM tryptophans are highlighted in yellow.
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    Image Search Results


    Domains of UHM and ULM-containing proteins relevant to this study. A, human CAPERα (NCBI RefSeq NP_004893) compared with human paralogues CAPERβ (NP_060577), U2AF65 (NP_009210), Puf60 (NP_001258027), and SPF45 (NP_001139019). B, human ULM-containing splicing factors SF1 (NP_004621) and SF3b155 (NP_036565). Circled P, phosphorylated SF1 SPSP motif. HEAT, helical repeats; KH-QUA2, K-Homology Quaking-Homology-2; RS, arginine-serine-rich; RRM, RNA recognition motif (blue); UHM, U2AF homology motif (cyan); ULM, U2AF ligand motif (magenta); Zn, zinc knuckle. Sequence boundaries of domains relevant to this study and the residue numbers of C termini are indicated above. C, ULM “consensus” compared with known sequences of human splicing factor ULMs. ULM tryptophans are highlighted in yellow.

    Journal: The Journal of Biological Chemistry

    Article Title: Cancer-relevant Splicing Factor CAPERα Engages the Essential Splicing Factor SF3b155 in a Specific Ternary Complex *

    doi: 10.1074/jbc.M114.558825

    Figure Lengend Snippet: Domains of UHM and ULM-containing proteins relevant to this study. A, human CAPERα (NCBI RefSeq NP_004893) compared with human paralogues CAPERβ (NP_060577), U2AF65 (NP_009210), Puf60 (NP_001258027), and SPF45 (NP_001139019). B, human ULM-containing splicing factors SF1 (NP_004621) and SF3b155 (NP_036565). Circled P, phosphorylated SF1 SPSP motif. HEAT, helical repeats; KH-QUA2, K-Homology Quaking-Homology-2; RS, arginine-serine-rich; RRM, RNA recognition motif (blue); UHM, U2AF homology motif (cyan); ULM, U2AF ligand motif (magenta); Zn, zinc knuckle. Sequence boundaries of domains relevant to this study and the residue numbers of C termini are indicated above. C, ULM “consensus” compared with known sequences of human splicing factor ULMs. ULM tryptophans are highlighted in yellow.

    Article Snippet: For experiments with cell extracts, bound proteins were analyzed by SDS-PAGE and immunoblotting with anti-U2AF 65 (mouse mAb, clone MC3; Sigma), anti-CAPERα (mouse mAb P14; Santa Cruz), and anti-GST (mouse mAb B14; Santa Cruz Biotechnology).

    Techniques: Sequencing

    Isothermal titration calorimetry of CAPERα UHM binding ULMs or ULM-containing proteins Average values and S.D. of two independent experiments. Δ G ° was calculated using Δ G ° = −RTln( K D −1 ), and − T Δ S ° was calculated using Δ G ° = Δ H ° − T Δ S °, T = 303 K. Values for each class of multiple sites in the wild-type SF3b155 domain describe binding of one CAPERα UHM to one of these SF3b155 sites. Representative isotherms are given with c-values in supplemental Fig. 1 . Boundaries of SF3b155, -W293, -W338 are residues 190–344; ULM5 is residues 333–342 (KRKSRWDETP); ULM5L is residues 333–355 (KRKSRWDETPASQMGGSTPVLTP).

    Journal: The Journal of Biological Chemistry

    Article Title: Cancer-relevant Splicing Factor CAPERα Engages the Essential Splicing Factor SF3b155 in a Specific Ternary Complex *

    doi: 10.1074/jbc.M114.558825

    Figure Lengend Snippet: Isothermal titration calorimetry of CAPERα UHM binding ULMs or ULM-containing proteins Average values and S.D. of two independent experiments. Δ G ° was calculated using Δ G ° = −RTln( K D −1 ), and − T Δ S ° was calculated using Δ G ° = Δ H ° − T Δ S °, T = 303 K. Values for each class of multiple sites in the wild-type SF3b155 domain describe binding of one CAPERα UHM to one of these SF3b155 sites. Representative isotherms are given with c-values in supplemental Fig. 1 . Boundaries of SF3b155, -W293, -W338 are residues 190–344; ULM5 is residues 333–342 (KRKSRWDETP); ULM5L is residues 333–355 (KRKSRWDETPASQMGGSTPVLTP).

    Article Snippet: For experiments with cell extracts, bound proteins were analyzed by SDS-PAGE and immunoblotting with anti-U2AF 65 (mouse mAb, clone MC3; Sigma), anti-CAPERα (mouse mAb P14; Santa Cruz), and anti-GST (mouse mAb B14; Santa Cruz Biotechnology).

    Techniques: Isothermal Titration Calorimetry, Binding Assay