e coli alkaline phosphatase bap  (TaKaRa)


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    TaKaRa e coli alkaline phosphatase bap
    E Coli Alkaline Phosphatase Bap, supplied by TaKaRa, 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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    e coli alkaline phosphatase bap  (TaKaRa)


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    TaKaRa e coli alkaline phosphatase bap
    E Coli Alkaline Phosphatase Bap, supplied by TaKaRa, 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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    e coli alkaline phosphatase bap  (TaKaRa)


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    TaKaRa e coli alkaline phosphatase bap
    Determination of the topology of ROP2 in the PVM. (A) The processing of ROP2 in <t>T.</t> <t>gondii</t> . The gene encoding ROP2 predicts a 64-kD protein including an NH 2 -terminal signal sequence (SS) . Signal sequence cleavage in the parasite ER is followed by an additional processing event ( ; ). Cleavage at aa 98 predicts a 53.5-kD protein, somewhat smaller than the observed 55 kD for the mature protein ( ; ), while cleavage at aa 80 would predict a 57.5-kD protein. The protein can be divided into the NH 2 -terminal domain (aa 98–465) and the transmembrane domain and COOH-terminus (aa 46–561). A chimera of <t>BAP</t> and the COOH-terminal domain of ROP2hc (aa 466–561) was constructed (BAP-ROP2TM/CT). (B) Immunoprecipitation of 35 S-Met–labeled in vitro–synthesized NH 2 -terminal domain (aa 98–465) and BAP-ROP2TM/CT with an antiserum against the R/DG fraction of the parasite. R/DG immunoprecipitates the NH 2 -terminal domain but not BAP-ROP2TM/CT, indicating that the NH 2 -terminal domain of ROP2 is exposed to the host cytoplasm.
    E Coli Alkaline Phosphatase Bap, supplied by TaKaRa, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/e coli alkaline phosphatase bap/product/TaKaRa
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    e coli alkaline phosphatase bap - by Bioz Stars, 2023-09
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    1) Product Images from "The Toxoplasma gondii protein ROP2 mediates host organelle association with the parasitophorous vacuole membrane"

    Article Title: The Toxoplasma gondii protein ROP2 mediates host organelle association with the parasitophorous vacuole membrane

    Journal: The Journal of Cell Biology

    doi: 10.1083/jcb.200101073

    Determination of the topology of ROP2 in the PVM. (A) The processing of ROP2 in T. gondii . The gene encoding ROP2 predicts a 64-kD protein including an NH 2 -terminal signal sequence (SS) . Signal sequence cleavage in the parasite ER is followed by an additional processing event ( ; ). Cleavage at aa 98 predicts a 53.5-kD protein, somewhat smaller than the observed 55 kD for the mature protein ( ; ), while cleavage at aa 80 would predict a 57.5-kD protein. The protein can be divided into the NH 2 -terminal domain (aa 98–465) and the transmembrane domain and COOH-terminus (aa 46–561). A chimera of BAP and the COOH-terminal domain of ROP2hc (aa 466–561) was constructed (BAP-ROP2TM/CT). (B) Immunoprecipitation of 35 S-Met–labeled in vitro–synthesized NH 2 -terminal domain (aa 98–465) and BAP-ROP2TM/CT with an antiserum against the R/DG fraction of the parasite. R/DG immunoprecipitates the NH 2 -terminal domain but not BAP-ROP2TM/CT, indicating that the NH 2 -terminal domain of ROP2 is exposed to the host cytoplasm.
    Figure Legend Snippet: Determination of the topology of ROP2 in the PVM. (A) The processing of ROP2 in T. gondii . The gene encoding ROP2 predicts a 64-kD protein including an NH 2 -terminal signal sequence (SS) . Signal sequence cleavage in the parasite ER is followed by an additional processing event ( ; ). Cleavage at aa 98 predicts a 53.5-kD protein, somewhat smaller than the observed 55 kD for the mature protein ( ; ), while cleavage at aa 80 would predict a 57.5-kD protein. The protein can be divided into the NH 2 -terminal domain (aa 98–465) and the transmembrane domain and COOH-terminus (aa 46–561). A chimera of BAP and the COOH-terminal domain of ROP2hc (aa 466–561) was constructed (BAP-ROP2TM/CT). (B) Immunoprecipitation of 35 S-Met–labeled in vitro–synthesized NH 2 -terminal domain (aa 98–465) and BAP-ROP2TM/CT with an antiserum against the R/DG fraction of the parasite. R/DG immunoprecipitates the NH 2 -terminal domain but not BAP-ROP2TM/CT, indicating that the NH 2 -terminal domain of ROP2 is exposed to the host cytoplasm.

    Techniques Used: Sequencing, Construct, Immunoprecipitation, Labeling, In Vitro, Synthesized

    Interaction of ROP2hc and its derivatives with murine liver mitochondria and ER. (A) Mitochondria and ER-enriched microsomes were prepared as described in Materials and methods. After the loading of 100 μg total protein, the mitochondrial proteins COXI and COXIII were detected exclusively in the mitochondrial but not on the ER preparation. The ER was detected using anti-KDEL and anti-calnexin antibodies. Both antibodies illuminated their targets in the ER prep. Although no KDEL signal was visible in the mitochondrial prep, a trace calnexin signal was apparent. This is likely due to the mitochondrion-associated ER or MAM fraction, which is highly enriched in liver . (B) The binding of ROP2hc, Δ98–127ROP2hcGFP, aa 98–127GFP, and GFP to mitochondria and ER was determined without further treatment and after extraction with 0.1 M Na 2 CO 3 , pH11.5 (Carbonate +), as indicated. Equivalent volumes of the organelle pellets (P) and supernatants (S) were resolved by SDS-PAGE and exposed by fluorography. Both ROP2hc and its derivatives bind efficiently to both mitochondria and ER. ROP2hc binding to mitochondria is resistant to extraction with carbonate (top panel). In contrast, binding to ER is not as strong and exhibits both extractable- and carbonate-resistant binding (top panel). Deletion of the proposed 30-aa NH 2 -terminal mitochondrial targeting signal (Δ98–127ROP2hcGFP) does not significantly affect binding to either mitochondria or ER (second panel). Furthermore, Δ98–127ROP2hcGFP is partially extracted from mitochondria by carbonate treatment, but is completely resistant to extraction from ER (second panel). The 30-aa NH 2 -terminal signal promotes the binding of the passenger protein GFP to mitochondria but not ER (third panel). Carbonate treatment promotes the fractionation of aa 98–127GFP into the pellet fraction with both organelles (third panel). This suggests the protein may be precipitated due to its basic nature by the carbonate treatment. Finally, the soluble passenger protein GFP exhibits no binding to either mitochondria or ER under any conditions (bottom panel). (C) Based on sucrose floatation gradients, the apparent membrane association of ROP2hc to mitochondria and ER is not due to neither the precipitation or aggregation of the protein. ROP2hc bound to organelle membranes in the absence (NT, no treatment) and after carbonate extraction (Carbo) was incorporated into 55% sucrose and a continuous sucrose gradient (55–20%) established as described in the Materials and methods. In the absence of carbonate extraction (Mito-NT, ER-NT), the majority of the signal in all cases floated into the gradient, coinciding with the distribution of the organelles based on Coomassie blue staining of the gels (unpublished data) indicating true membrane association. After carbonate extraction (Mito-Carbo, ER-Carbo) ROP2hc continues to float into the gradient, indicating its association with organelle membranes in maintained and resistant to extraction with carbonate. Had the protein been extracted or merely precipitated, a significant signal would be observed in fractions 1 and 2 (load fractions). This indicates ROP2hc interacts with both mitochondria and ER with high affinity behaving like an integral membrane protein. (D) Neither ROP2hc nor Δ98–127ROP2hc are cotranslationally imported into canine microsomes. Cotranslational import of ROP2hc, Δ98–127ROP2hc, and E. coli BLA was performed as described in the Materials and methods. Although both ROP2hc (lane 1) and Δ98–127ROP2hc (lane 4) were synthesized, they were not translocated either partially or completely into the ER lumen and remain protease sensitive (PK, lanes 2 and 5). In contrast, BLA was efficiently imported into the microsomes and processed from the precursor (p, lane 7) to the mature form (m, lanes 7 and 8). Only the mature form is protease protected (PK, lane 8) and the protection is sensitive to detergent treatment (PK, Tx, lane 9), indicating the microsomes are import competent.
    Figure Legend Snippet: Interaction of ROP2hc and its derivatives with murine liver mitochondria and ER. (A) Mitochondria and ER-enriched microsomes were prepared as described in Materials and methods. After the loading of 100 μg total protein, the mitochondrial proteins COXI and COXIII were detected exclusively in the mitochondrial but not on the ER preparation. The ER was detected using anti-KDEL and anti-calnexin antibodies. Both antibodies illuminated their targets in the ER prep. Although no KDEL signal was visible in the mitochondrial prep, a trace calnexin signal was apparent. This is likely due to the mitochondrion-associated ER or MAM fraction, which is highly enriched in liver . (B) The binding of ROP2hc, Δ98–127ROP2hcGFP, aa 98–127GFP, and GFP to mitochondria and ER was determined without further treatment and after extraction with 0.1 M Na 2 CO 3 , pH11.5 (Carbonate +), as indicated. Equivalent volumes of the organelle pellets (P) and supernatants (S) were resolved by SDS-PAGE and exposed by fluorography. Both ROP2hc and its derivatives bind efficiently to both mitochondria and ER. ROP2hc binding to mitochondria is resistant to extraction with carbonate (top panel). In contrast, binding to ER is not as strong and exhibits both extractable- and carbonate-resistant binding (top panel). Deletion of the proposed 30-aa NH 2 -terminal mitochondrial targeting signal (Δ98–127ROP2hcGFP) does not significantly affect binding to either mitochondria or ER (second panel). Furthermore, Δ98–127ROP2hcGFP is partially extracted from mitochondria by carbonate treatment, but is completely resistant to extraction from ER (second panel). The 30-aa NH 2 -terminal signal promotes the binding of the passenger protein GFP to mitochondria but not ER (third panel). Carbonate treatment promotes the fractionation of aa 98–127GFP into the pellet fraction with both organelles (third panel). This suggests the protein may be precipitated due to its basic nature by the carbonate treatment. Finally, the soluble passenger protein GFP exhibits no binding to either mitochondria or ER under any conditions (bottom panel). (C) Based on sucrose floatation gradients, the apparent membrane association of ROP2hc to mitochondria and ER is not due to neither the precipitation or aggregation of the protein. ROP2hc bound to organelle membranes in the absence (NT, no treatment) and after carbonate extraction (Carbo) was incorporated into 55% sucrose and a continuous sucrose gradient (55–20%) established as described in the Materials and methods. In the absence of carbonate extraction (Mito-NT, ER-NT), the majority of the signal in all cases floated into the gradient, coinciding with the distribution of the organelles based on Coomassie blue staining of the gels (unpublished data) indicating true membrane association. After carbonate extraction (Mito-Carbo, ER-Carbo) ROP2hc continues to float into the gradient, indicating its association with organelle membranes in maintained and resistant to extraction with carbonate. Had the protein been extracted or merely precipitated, a significant signal would be observed in fractions 1 and 2 (load fractions). This indicates ROP2hc interacts with both mitochondria and ER with high affinity behaving like an integral membrane protein. (D) Neither ROP2hc nor Δ98–127ROP2hc are cotranslationally imported into canine microsomes. Cotranslational import of ROP2hc, Δ98–127ROP2hc, and E. coli BLA was performed as described in the Materials and methods. Although both ROP2hc (lane 1) and Δ98–127ROP2hc (lane 4) were synthesized, they were not translocated either partially or completely into the ER lumen and remain protease sensitive (PK, lanes 2 and 5). In contrast, BLA was efficiently imported into the microsomes and processed from the precursor (p, lane 7) to the mature form (m, lanes 7 and 8). Only the mature form is protease protected (PK, lane 8) and the protection is sensitive to detergent treatment (PK, Tx, lane 9), indicating the microsomes are import competent.

    Techniques Used: Binding Assay, SDS Page, Fractionation, Staining, Synthesized

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    TaKaRa e coli alkaline phosphatase bap
    E Coli Alkaline Phosphatase Bap, supplied by TaKaRa, 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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    Average 93 stars, based on 1 article reviews
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