In July 2007, tar spot symptoms observed on citrus leaves Geiger, sebestena Cordia L. (boraginaceae), in the landscape and commercial nursery in Homestead, FL. This disease appears to be spreading and locally severe. Symptoms are circular, little spots hypertrophy of about 5 to 8 cm in diameter, slightly chlorotic on abaxial surface and has a lot of stromal blackened circular, 0.2-0.4 mm, on the lower surface of leaves. Old and yellowing leaves, the area around the fixed point of pale green.
Embedded in the stroma much Perithecia, 173-312 m diameter, circular to irregular in shape, with a neck that as many as 200 pM lateral length and 73-104 m in diameter. ASCI, 77-92 × 11 to 13 um, are elongated, two-celled ascospores, 50-61 × 3 to 5 um which have narrowing of the striking wall dividing cells. Dimensions and appearance of pathogens fits tightly with those published for Diatractium cordianum (Ellis & Kelsey) Syd (1). Young, asymptomatic C. sebestena leaves were sprayed to runoff with ascospores suspension of approximately 104 ml-1 were harvested from the affected leaves. inoculated leaves were placed on a paper towel saturated with water in petri dishes and kept in a growth chamber at 25 ° C with fluorescent light at 10 h day-1.
Symptoms similar to those observed in the affected trees in the landscape began to evolve after 21 days and Perithecia clear after 28 days. An ITS 1, 2 ITS and 5.8S rDNA sequences deposited in GenBank (Accession No. EU541488). A herbarium specimens deposited in the US National Fungus Collections (BPI No. 878 441). It is a new host record for D. cordianum and is the first time the pathogens have been reported in the United States. previous record comes from Venezuela and several Caribbean islands, including Cuba and Jamaica.
Symptoms of this disease has not been observed in Texas wild olive, Cordia boissieri, near exposed C. sebestena. P. F. Cannon (1) suggests that the disease has no economic impact. However, the striking nature of the C sebestena symptoms and the importance of this tree in South Florida ornamental trade (2) shows that this disease can be significant in the last host. References: (1) P. F. Cannon. Mycol. Res. 92: 327, 1989. (2) D. E. F. G. Gilman and Watson
First Report of Tar Spot on Orange Geiger, Cordia sebestena, Caused by Diatractium cordianum in Florida.
Randomized, controlled clinical pilot study of venous leg ulcers treated with two types of shockwave therapy.
Background. Venous leg ulcers difficult to heal wounds. The basis of their physiotherapeutic treatment is compression therapy. However, over the years, looking for additional or other methods to supplement the treatment of venous ulcers, which would shorten the duration of treatment, are ongoing. One such method is shockwave therapy.
Method. The aim of our study was to compare radial shockwave therapy (R-ESWT) with a focused shockwave therapy (F-ESWT) in the treatment of venous leg ulcers. Patients were randomly assigned to a group of trees. In the first group of radial shockwave therapy (0.17mJ / mm2, 100 impulses / cm2, 5 Hz), the second group focused shockwave therapy (0.173mJ / mm2, 100 impulses / cm2, 5 Hz) is used and in the third group used a standard treatment. Patients in the shockwave therapy group were given 6 treatments at intervals of five days.
Total area, circumference, Gilman index, maximum length and maximum width of the ulcer was measured. The third group of patients with wet gauze dressing with salt and gently compressing the elastic bandage used (SWC standard wound care).
Description: Bid Antibody: Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells. Disruption of this process has been implicated in a variety of diseases such as cancer. The Bcl-2 family of proteins is comprised of critical regulators of apoptosis that can be divided into two classes: those that inhibit apoptosis and those that promote cell death. Bid, a pro-apoptotic Bcl-2 family member, is cleaved by caspase-8 in response to apoptotic signals, exposing the Bcl-2 homology 3 (BH3) domain which is normally buried in the full-length protein. The cleaved complex is myris-toylated and translocated to the mitochondrial membrane where it may induce mitochondrial Bax and Bak to oligomerize.
Description: Bid Antibody: Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells. Disruption of this process has been implicated in a variety of diseases such as cancer. The Bcl-2 family of proteins is comprised of critical regulators of apoptosis that can be divided into two classes: those that inhibit apoptosis and those that promote cell death. Bid, a pro-apoptotic Bcl-2 family member, is cleaved by caspase-8 in response to apoptotic signals, exposing the Bcl-2 homology 3 (BH3) domain which is normally buried in the full-length protein. The cleaved complex is myris-toylated and translocated to the mitochondrial membrane where it may induce mitochondrial Bax and Bak to oligomerize.
Description: Bid Antibody: Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells. Disruption of this process has been implicated in a variety of diseases such as cancer. The Bcl-2 family of proteins is comprised of critical regulators of apoptosis that can be divided into two classes: those that inhibit apoptosis and those that promote cell death. Bid, a pro-apoptotic Bcl-2 family member, is cleaved by caspase-8 in response to apoptotic signals, exposing the Bcl-2 homology 3 (BH3) domain which is normally buried in the full-length protein. The cleaved complex is myris-toylated and translocated to the mitochondrial membrane where it may induce mitochondrial Bax and Bak to oligomerize.
Description: Bid Antibody: Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells. Disruption of this process has been implicated in a variety of diseases such as cancer. The Bcl-2 family of proteins is comprised of critical regulators of apoptosis that can be divided into two classes: those that inhibit apoptosis and those that promote cell death. Bid, a pro-apoptotic Bcl-2 family member, is cleaved by caspase-8 in response to apoptotic signals, exposing the Bcl-2 homology 3 (BH3) domain which is normally buried in the full-length protein. The cleaved complex is myris-toylated and translocated to the mitochondrial membrane where it may induce mitochondrial Bax and Bak to oligomerize.
Description: A polyclonal antibody against BID. Recognizes BID from Human. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC
Description: A polyclonal antibody against BID. Recognizes BID from Human. This antibody is Unconjugated. Tested in the following application: ELISA, IHC; Recommended dilution: IHC:1:1000-1:2000
Description: A polyclonal antibody against BID. Recognizes BID from Human. This antibody is Unconjugated. Tested in the following application: WB, ELISA;WB:1/500-1/2000.ELISA:1/10000
Description: A polyclonal antibody against BID. Recognizes BID from Human, Mouse. This antibody is Unconjugated. Tested in the following application: WB, IHC, ELISA;WB:1/500-1/2000.IHC:1/100-1/300.ELISA:1/10000
Description: A polyclonal antibody against BID. Recognizes BID from Human. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC;ELISA:1:1000-1:5000, WB:1:200-1:2000, IHC:1:25-1:100
Description: A polyclonal antibody against BID. Recognizes BID from Human. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC;ELISA:1:1000-1:5000, WB:1:200-1:2000, IHC:1:25-1:100
Description: The major proteolytic product p15 BID allows the release of cytochrome c (By similarity). Isoform 1, isoform 2 and isoform 4 induce ICE-like proteases and apoptosis. Isoform 3 does not induce apoptosis. Counters the protective effect of Bcl-2. [UniProt]
Description: The major proteolytic product p15 BID allows the release of cytochrome c (By similarity). Isoform 1, isoform 2 and isoform 4 induce ICE-like proteases and apoptosis. Isoform 3 does not induce apoptosis. Counters the protective effect of Bcl-2. [UniProt]
Description: Bid is a death agonist that heterodimerizes with either agonist BAX or antagonist BCL2. Bid is a member of the BCL-2 family of cell death regulators. It is a mediator of mitochondrial damage induced by caspase-8 (CASP8); CASP8 cleaves this encoded protein, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release.
Description: Bid is a death agonist that heterodimerizes with either agonist BAX or antagonist BCL2. Bid is a member of the BCL-2 family of cell death regulators. It is a mediator of mitochondrial damage induced by caspase-8 (CASP8); CASP8 cleaves this encoded protein, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release.
Description: BID (BH3-Interacting Domain Death Agonist), is a pro-apoptotic member of the Bcl-2 protein family. The BCL2 family of proteins consists of both antagonists and agonists that regulate apoptosis and compete through dimerization. By fluorescence in situ hybridization, Wang et al. (1998) mapped the human BID gene to 22q11. Luo et al. (1998) reported the purification of a cytosolic protein that induces cytochrome c release from mitochondria in response to caspase-8, the apical caspase activated by cell surface death receptors such as FAS and TNF.
Description: BID (BH3-Interacting Domain Death Agonist), is a pro-apoptotic member of the Bcl-2 protein family. The BCL2 family of proteins consists of both antagonists and agonists that regulate apoptosis and compete through dimerization. By fluorescence in situ hybridization, the human BID gene is mapped to 22q11. It is reported the purification of a cytosolic protein that induces cytochrome c release from mitochondria in response to caspase-8, the apical caspase activated by cell surface death receptors such as FAS and TNF.
Description: Bid (BH3-Interacting Domain Death Agonist), is a pro-apoptotic member of the Bcl-2 protein family. The BCL2 family of proteins consists of both antagonists and agonists that regulate apoptosis and compete through dimerization. By fluorescence in situ hybridization, Wang et al.(1998) mapped the human BID gene to 22q11. Luo et al.(1998) reported the purification of a cytosolic protein that induces cytochrome c release from mitochondria in response to caspase-8, the apical caspase activated by cell surface death receptors such as FAS and TNF.
Description: Bid (BH3-Interacting Domain Death Agonist), is a pro-apoptotic member of the Bcl-2 protein family. The BCL2 family of proteins consists of both antagonists and agonists that regulate apoptosis and compete through dimerization. By fluorescence in situ hybridization, Wang et al. (1998) mapped the human BID gene to 22q11. Luo et al. (1998) reported the purification of a cytosolic protein that induces cytochrome c release from mitochondria in response to caspase-8, the apical caspase activated by cell surface death receptors such as FAS and TNF.
Description: BH3-Interacting Domain Death Agonist (BID) is a member of the Bcl-2 protein family which regulates outer mitochondrial membrane permeability. BID is a pro-apoptotic member that causes cytochrome c to be released from the mitochondria intermembrane space into the cytosol. Interaction of Bid with Bak causes altered mitochondrial membrane permeability. BID contains only the BH3 domain, which is required for its interaction with the Bcl-2 family proteins and for its pro-death activity. BID is susceptible to proteolytic cleavage by caspases, calpains, Granzyme B and cathepsins. It is an integrating key regulator of the intrinsic death pathway that amplifies caspase-dependent and caspase-independent execution of neuronal apoptosis. Therefore pharmacological inhibition of BID provides a promising therapeutic strategy in neurological diseases where programmed cell death is prominent, and also offer a new strategy for the treatment of acute renal failure associated with ischemia-reperfusion. BID receives direct inputs from a key regulator of the cell cycle arrest/DNA repair machinery (ATM), and therefore is an excellent candidate to coordinate genotoxic stress responses and apoptotic cell death. BID is a novel pro-apoptosis Bcl-2 family protein that is activated by caspase 8 in response to Fas/TNF-R1 death receptor signals. Deletion of BID inhibits carcinogenesis in the liver, although this genetic alteration promotes tumorigenesis in the myeloid cells. This is likely related to the function of BID to promote cell cycle progression into S phase. BID could be also involved in the maintenance of genomic stability by engaging at mitosis checkpoint.
Description: A polyclonal antibody for detection of BID from Human. This BID antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human BID at AA range: 20-100
Description: A polyclonal antibody for detection of BID from Human. This BID antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human BID at AA range: 20-100
Description: A polyclonal antibody for detection of BID from Human. This BID antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the Internal region of human BID at AA range: 20-100
Description: A polyclonal antibody for detection of BID from Human, Mouse. This BID antibody is for WB , IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human BID around the non-phosphorylation site of S78
Description: A polyclonal antibody for detection of BID from Human, Mouse. This BID antibody is for WB , IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human BID around the non-phosphorylation site of S78
Description: A polyclonal antibody for detection of BID from Human, Mouse. This BID antibody is for WB , IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human BID around the non-phosphorylation site of S78
Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human Bid . This antibody is tested and proven to work in the following applications:
Description: A polyclonal antibody against BID. Recognizes BID from Human. This antibody is FITC conjugated. Tested in the following application: ELISA
Description: A polyclonal antibody against BID. Recognizes BID from Human. This antibody is Biotin conjugated. Tested in the following application: ELISA
Description: Description of target: Induces caspases and apoptosis. Counters the protective effect of Bcl-2. The major proteolytic product p15 BID allows the release of cytochrome c.;Species reactivity: Rat;Application: ;Assay info: Assay Methodology: Quantitative Sandwich ELISA;Sensitivity: 0.157 ng/mL
Description: Description of target: This gene encodes a death agonist that heterodimerizes with either agonist BAX or antagonist BCL2. The encoded protein is a member of the BCL-2 family of cell death regulators. It is a mediator of mitochondrial damage induced by caspase-8 (CASP8); CASP8 cleaves this encoded protein, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release. Multiple alternatively spliced transcript variants have been found, but the full-length nature of some variants has not been defined.;Species reactivity: Human;Application: ELISA;Assay info: ;Sensitivity: < 0.58ng/mL
Description: Description of target: Induces caspases and apoptosis. Counters the protective effect of Bcl-2. The major proteolytic product p15 BID allows the release of cytochrome c.;Species reactivity: Mouse;Application: ;Assay info: Assay Methodology: Quantitative Sandwich ELISA;Sensitivity: 0.443 ng/mL
Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human mouse BID (S61). This antibody is tested and proven to work in the following applications:
Description: A polyclonal antibody for detection of BID phospho Ser78) from Human, Mouse. This BID phospho Ser78) antibody is for IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human BID around the phosphorylation site of S78
Description: A polyclonal antibody for detection of BID phospho Ser78) from Human, Mouse. This BID phospho Ser78) antibody is for IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human BID around the phosphorylation site of S78
Description: A polyclonal antibody for detection of BID phospho Ser78) from Human, Mouse. This BID phospho Ser78) antibody is for IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from human BID around the phosphorylation site of S78
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Results. Analysis of the results showed that a complete cure ulcer was achieved in 35% of patients treated with radial shockwave, 26% of patients with focused shock waves used
