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Search results for: Rabbit Anti-ERN2 Polyclonal Antibody

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#38760596   2024/05/17 To Up

Expression of Recombinant Stonustoxin Alpha Subunit and Preparation of polyclonal antiserum for Stonustoxin Neutralization Studies.

Stonustoxin (SNTX) is a lethal protein found in stonefish venom, responsible for many of the symptoms associated with stonefish envenomation. To counter stonefish venom challenges, antivenom is a well-established and effective solution. In this study, we aimed to produce the recombinant alpha subunit protein of Stonustoxin from Synanceia horrida and prepare antibodies against it The SNTXα gene sequence was optimized for E. coli BL21 (DE3) expression and cloned into the pET17b vector. Following purification, the recombinant protein was subcutaneously injected into rabbits, and antibodies were extracted from rabbit´s serum using a G protein column As a result of codon optimization, the codon adaptation index for the SNTXα cassette increased to 0.94. SDS-PAGE analysis validated the expression of SNTXα, with a band observed at 73.5 kDa with a yield of 60 mg/l. ELISA results demonstrated rabbits antibody titers were detectable up to a 1:256,000 dilution. The isolated antibody from rabbit´s serum exhibited a concentration of 1.5 mg/ml, and its sensitivity allowed the detection of a minimum protein concentration of 9.7 ng. In the neutralization assay the purified antibody against SNTXα protected mice challenged with 2 LD50. In conclusion, our study successfully expressed the alpha subunit of Stonustoxin in a prokaryotic host, enabling the production of antibodies for potential use in developing stonefish antivenom.
Amir Sajjad Hojjati-Razgi, Shahram Nazarian, Hossein Samiei-Abianeh, Amir Vazirizadeh, Emad Kordbacheh, Seyed Mojtaba Aghaie

1406 related Products with: Expression of Recombinant Stonustoxin Alpha Subunit and Preparation of polyclonal antiserum for Stonustoxin Neutralization Studies.

310.05 mg50 ug 100100ug Lyophilized1mg100ug100ug100ug Lyophilized100ug Lyophilized

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#38756656   2024/05/02 To Up

Phosphorylation of cell cycle and apoptosis regulatory protein-1 by stress activated protein kinase P38γ is a novel mechanism of apoptosis signaling by genotoxic chemotherapy.

CARP-1, a perinuclear phospho-protein, regulates cell survival and apoptosis signaling induced by genotoxic drugs. However, kinase(s) phosphorylating CARP-1 and down-stream signal transduction events remain unclear. Here we find that CARP-1 Serine (S) and Threonine (T) substitution to Alanines (AA) inhibits genotoxic drug-induced apoptosis. CARP-1 T is followed by a Proline (P), and this TP motif is conserved in vertebrates. Based on these findings, we generated affinity-purified, anti-phospho-CARP-1 T rabbit polyclonal antibodies, and utilized them to elucidate chemotherapy-activated, CARP-1-dependent cell growth signaling mechanisms. Our kinase profiling studies revealed that MAPKs/SAPKs phosphorylated CARP-1 T. We then UV cross-linked protein extracts from Adriamycin-treated HeLa cervical cancer cells with a CARP-1 (614-638) peptide, and conducted liquid chromatography-tandem mass spectrometry (LC-MS/MS) analyses of the peptide-bound protein complexes. This experiment revealed SAPK p38γ interaction with CARP-1 (614-638) peptide. Our studies further established that SAPK p38γ, but not other MAPKs, phosphorylates CARP-1 T in cancer cells treated with genotoxic drugs. Loss of p38γ abrogates CARP-1 T phosphorylation, and results in enhanced survival of breast cancer cells by genotoxic drugs. CARP-1 T phosphorylation was also noted in breast tumors from patients treated with radiation or endocrine therapies. We conclude that genotoxic drugs activate p38γ-dependent CARP-1 T phosphorylation to inhibit cell growth.
Jaganathan Venkatesh, Magesh Muthu, Indulekha Singaravelu, Vino T Cheriyan, Sreeja C Sekhar, Nuwan C P N Acharige, Edi Levi, Hadeel Assad, Mary Kay H Pflum, Arun K Rishi

1632 related Products with: Phosphorylation of cell cycle and apoptosis regulatory protein-1 by stress activated protein kinase P38γ is a novel mechanism of apoptosis signaling by genotoxic chemotherapy.

100ul100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized 100ul100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100μg

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#38716786   // To Up

Induction therapy in heart transplantation: A systematic review and network meta-analysis for developing evidence-based recommendations.

Induction therapy (IT) utility in heart transplantation (HT) remains contested. Commissioned by a clinical-practice guidelines panel to evaluate the effectiveness and safety of IT in adult HT patients, we conducted this systematic review and network meta-analysis (NMA).
Lakshmi Kugathasan, Daniel G Rayner, Sabrina Mianchen Wang, Eduardo Rodenas-Alesina, Ani Orchanian-Cheff, Josef Stehlik, Finn Gustafsson, Douglas Greig, Michael McDonald, Alejandro Mario Bertolotti, Penny Demas-Clarke, Stella Kozuszko, Gordon Guyatt, Farid Foroutan, Ana Carolina Alba

1863 related Products with: Induction therapy in heart transplantation: A systematic review and network meta-analysis for developing evidence-based recommendations.

100 UG100.00 ug100ug Lyophilized20 µl (10 mM)100 μg5mg5 g

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#38668248   2024/03/30 To Up

Identification and Characterization of Heat Shock Protein 70 (HSP70) as Novel Diagnostic Marker of Onchocerciasis in Human Urine.

Despite several decades of mass drug administration and elimination-related activities, human onchocerciasis still represents a major parasitic threat in endemic regions. Among the challenges encountered by the elimination program is the lack of a suitable diagnostic tool that is accurate and non-invasive. Currently used methods are either invasive or not suitable for monitoring large numbers of patients. Herein, we describe the identification and characterization of heat shock protein 70 (HSP70) as a novel diagnostic biomarker for human onchocerciasis, which can directly be detected in urine samples of infected patients. This nematode-specific antigen was identified through LC-MS after differential SDS-PAGE using urine-derived protein extracts from -infected patients in Cameroon. Polyclonal antibodies generated in rabbits after cloning and expression of HSP70 in reliably differentiated between urine samples from infected- and uninfected patients in a hypoendemic area of human onchocerciasis. These results provide an excellent basis for further development of a non-invasive and scalable diagnostic assay for human onchocerciasis using urine samples. Such a urine-based diagnostic assay will be of major importance for the elimination program of human onchcerciasis in endemic countries.
Lum Abienwi Ambe, Elisabeth Limunga, Clarisse Engowei Mbah, Ngwewondo Adela, Ndumu Eric, Martha Ngoe, Bertrand Sone, Günter Lochnit, Julius Babila Tachu, Samuel Wanji, Anja Taubert, Carlos Hermosilla, Faustin Kamena

2153 related Products with: Identification and Characterization of Heat Shock Protein 70 (HSP70) as Novel Diagnostic Marker of Onchocerciasis in Human Urine.

0.1 mg1 mg10 ug 0.2 mg 100 μg1 kit(96 Wells)25 μg10 ìg 50 µg 10 0.2 mg 25 μg

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#38664356   2024/04/26 To Up

Human and camel cystic echinococcosis - a polyclonal antibody-based sandwich ELISA for its serodiagnosis with molecular identification.

Cystic echinococcosis (CE) is an emergent neglected disease affecting human and animals in Egypt with a wide distribution and incidence. This study aimed to evaluate the use of a polyclonal antibody-based sandwich ELISA in the detection of Echinococcus granulosus antigen in human and camel sera. Hydatid cyst protoscoleces antigen (PsAg) was isolated from hydatid cysts collected from naturally infected camel livers and lungs. PsAg was used for immunization of rabbits to raise IgG polyclonal antibodies (IgG PsAb). IgG PsAb were then precipitated, purified using Protein-A Sepharose gel and labeled with horseradish peroxidase enzyme. We assayed the purity of the IgG PsAb, and the two prepared E. granulosus antigens CPsAg from camel cysts and HPsAg from human cysts by Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The resulted protein bands of the prepared CPsAg appeared at different molecular weights: 180, 90, 68, 54, 42 and 22 kDa while, HPsAg shared with it in 4 common bands at 68, 54, 42, and 22 kDa. The purified IgG PsAb had been resolved at two bands at 52 kDa and at 32 kDa. Sandwich ELISA were performed for the detection of circulating E. granulosus antigens in sera of human (n = 183) and camels (n = 190). The purified IgG PsAb showed strong reactivity against E. granulosus infected human and camel samples and no cross reactivity neither with free-healthy negative sera nor with others parasitic diseases (Schistosomiasis, Fascioliasis, Toxoplasmosis, Ancylostomiasis for human samples and Fascioliasis, ticks' infestation, Eimeriosis, Cryptosporidiosis, Nasal myiasis, Toxoplasmosis for camel samples). The sensitivity of the assay was 98.25% (56/57) and 96.9% (31/32) against human and camel samples, respectively. Specificity was 100% in both human and camel samples. Sandwich ELISA detected CE in 33.3% (24/72) and 55.6% (50/90) random human and camel samples, respectively. Indirect ELISA, using CPsAg, was used for detection of antibodies in positive human and camels' sera and detected 96.5% (55/57) and 93.8% (30/32) of human and camel samples, respectively. In our study, Genomic DNA was extracted from protoscoleces fluid of human liver hydatid cysts to identify the Echinococcus sp. isolate based on NADH dehydrogenase subunit 1 (NAD1) gene by Polymerase Chain Reaction (PCR) and the isolate (GenBank: OP785689.1) were identified as E. granulosus sensu lato genotype. In conclusion, Sandwich ELISA technique was found to be a potent and sensitive assay for detection of hydatid antigen in both human and camel samples.
A Maher, N I Toaleb, R M Shaapan, D Aboelsoued, M B Salman, S Zaky

2953 related Products with: Human and camel cystic echinococcosis - a polyclonal antibody-based sandwich ELISA for its serodiagnosis with molecular identification.

1 kit100ug Lyophilized 100 UG0.1 mg100ug100ug Lyophilized100ug Lyophilized100ug0.1 mg100ug Lyophilized100ug100ug

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#38663138   2024/04/19 To Up

Cooling rate modifies the location of aquaporin 3 in spermatozoa of sheep and goat.

The freeze-thawing process induces osmotic changes that may affect the membrane domain location of aquaporins' (AQP) in spermatozoa. Recent studies suggest that changes in AQP3 localization allows better sperm osmo-adaptation, improving the cryoresistance. Ultra-rapid freezing is an alternative cryopreservation technique that requires less equipment than conventional freezing, and it is faster, simpler and can be used in the field. This study aimed to determine the influence of freezing-thawing rates (slow (control) vs. ultra-rapid) on AQP3 expression and location in the spermatozoa from small ruminants (sheep and goats) and its relationship with sperm cryo-damage. Spermatozoa were collected from 10 Merino rams and 10 Murciano-Granadina bucks. The presence and distribution of AQP3 were assessed by Western blotting and immunocytochemistry (ICC), employing a commercial rabbit polyclonal antibody. Sperm motility was CASA system-analyzed, and membrane and acrosome integrity assessed by fluorescence (PI/PNA-FITC). Western blotting did not detect a significant effect of freezing-thawing rate on the amount of AQP3 while ICC found freezing-thawing rate affecting AQP3 location (P < 0.05). In both species, the percentages of spermatozoa showing AQP3 in the post-acrosome region, mid-piece, and principal piece of the tail were greater in samples cryopreserved by slow freezing-thawing (control) than ultra-rapid freezing-thawing rates (P < 0.05). Spermatozoa cryopreserved using ultra-rapid freezing-thawing showed decrease motility, plasma membrane, and acrosome integrity (P < 0.05), which might be related, at least in part, to a lower expression of AQP3. In conclusion, the cooling rate modifies the location of AQP3 in spermatozoa of sheep and goat, which might be associated with sperm cryosurvival.
Belén Pequeño, María Gemma Millán de la Blanca, Cristina Castaño, Adolfo Toledano-Díaz, Milagros Cristina Esteso, Esther Alba, Francisco A Arrebola, Rodolfo Ungerfeld, Belén Martínez-Madrid, Manuel Alvarez-Rodriguez, Heriberto Rodriguez-Martinez, Julián Santiago-Moreno

2233 related Products with: Cooling rate modifies the location of aquaporin 3 in spermatozoa of sheep and goat.

1100 μg100 μg100 μg100 μg100 μg100 μg100 μg100 μg100 μg100 μg100 μg

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#38659451   2024/04/10 To Up

Recombinant expression and characterization of Canine circovirus capsid protein for diagnosis.

Canine circovirus (CanineCV) is a contagious virus that causes severe gastroenteritis, diarrhea, respiratory disease, and vasculitis, often resulting in fatality among infected dogs. In this study, a recombinant Capsid protein (rCap) of CanineCV was expressed in the () Rosetta (DE3) pLysS host cell, followed by affinity purification, and then analyzed by SDS-PAGE, revealing a molecular weight of approximately 31 kDa. The antigenicity of the CanineCV rCap protein was confirmed through recognition by a rabbit anti-CanineCV rCap protein polyclonal antibody (PoAb). Additionally, the reactivity and specificity of this PoAb were assessed using indirect enzyme-linked immunosorbent assay (ELISA) and Western blot analysis before applying in an immunohistochemistry (IHC), namely, immunoperoxidase detection. The immunoperoxidase assay using rabbit anti-CanineCV rCap protein PoAb demonstrated that the CanineCV Cap protein was predominantly located in immune cells, especially lymphocytes and macrophages, within the spleen, lung, tracheobronchial lymph nodes, small intestine, and kidney. Similarly, the Cap protein was also found in pneumocytes in the lung and renal tubular epithelial cells in the kidney. These findings reflected the biological activity and cell tropism of the virus. Therefore, the recombinant Cap protein and its PoAb could be used for the development of a valuable diagnostic tool for CanineCV detection.
Wichan Dankaona, Pornpiroon Nooroong, Napassorn Poolsawat, Chutchai Piewbang, Somporn Techangamsuwan, Panat Anuracpreeda

1523 related Products with: Recombinant expression and characterization of Canine circovirus capsid protein for diagnosis.

1021 mg1mg10ìg100ul102x 100ug21mg100010

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#38634336   2024/04/18 To Up

Central Chirality and Axial Chirality Recognition of the Enantioselective Antibodies to Herbicide Metolachlor.

Enantioselective antibodies have emerged as efficient tools in the field of chiral chemical detection and separation. However, it is complicated to obtain a highly stereoselective antibody due to the unclear recognition mechanism. In this study, the hapten of metolachlor was synthesized and enantio-separated. The absolute configuration of the four haptens obtained was identified by the computed and experimental electronic circular dichroism comparison. Five polyclonal antibodies against the Rac-metolachlor and its enantiomers were generated by immunization. The cross-activity of all the 5 antibodies with 44 structural analogues, including metolachlor enantiomers, was tested. It demonstrated that antibodies have higher specificity to recognize central chirality than axial chirality. Especially, αRR-MET-Ab exhibited excellent specificity and stereoselectivity. Accordingly, 3D-QSAR models were constructed and revealed that paired stereoisomers exhibited opposite interactions with the antibodies. It is the first time that the antibodies against four stereoisomers were prepared and analyzed, which will be conducive to the rational design of the stereoselective antibodies.
Xing Shen, Yan Zhang, JingJing Xu, XiaoTing Yu, WenMing Bai, Xinan Huang, HongTao Lei

1631 related Products with: Central Chirality and Axial Chirality Recognition of the Enantioselective Antibodies to Herbicide Metolachlor.

100 μg0.1 mg50 200 ug1 mg100 1 mg100 100 μg1000 TESTS/0.65ml

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#38633244   2024/04/03 To Up

Dry and liquid formulations of IBT-V02, a novel multi-component toxoid vaccine, are effective against isolates from low-to-middle income countries.

is the leading cause of skin and soft tissue infections (SSTIs) in the U.S. as well as more serious invasive diseases, including bacteremia, sepsis, endocarditis, surgical site infections, osteomyelitis, and pneumonia. These infections are exacerbated by the emergence of antibiotic-resistant clinical isolates such as methicillin-resistant (MRSA), highlighting the need for alternatives to antibiotics to treat bacterial infections. We have previously developed a multi-component toxoid vaccine (IBT-V02) in a liquid formulation with efficacy against multiple strains of prevalent in the industrialized world. However, liquid vaccine formulations are not compatible with the paucity of cold chain storage infrastructure in many low-to-middle income countries (LMICs). Furthermore, whether our IBT-V02 vaccine formulations are protective against isolates from LMICs is unknown. To overcome these limitations, we developed lyophilized and spray freeze-dried formulations of IBT-V02 vaccine and demonstrated that both formulations had comparable biophysical attributes as the liquid formulation, including similar levels of toxin neutralizing antibodies and protective efficacy against MRSA infections in murine and rabbit models. To enhance the relevancy of our findings, we then performed a multi-dimensional screen of 83 clinical isolates from LMICs (e.g., Democratic Republic of Congo, Palestine, and Cambodia) to rationally down-select strains to test in our models based on broad expression of IBT-V02 targets (i.e., pore-forming toxins and superantigens). IBT-V02 polyclonal antisera effectively neutralized toxins produced by the clinical isolates from LMICs. Notably, the lyophilized IBT-V02 formulation exhibited significant efficacy in various preclinical infection models against the clinical isolates from LMICs, which was comparable to our liquid formulation. Collectively, our findings suggested that lyophilization is an effective alternative to liquid vaccine formulations of our IBT-V02 vaccine against infections, which has important implications for protection from isolates from LMICs.
Yu Wang, Ipsita Mukherjee, Arundhathi Venkatasubramaniam, Dustin Dikeman, Nicholas Orlando, Jing Zhang, Roger Ortines, Mark Mednikov, Shardulendra P Sherchand, Tulasikumari Kanipakala, Thao Le, Sanjay Shukla, Mark Ketner, Rajan P Adhikari, Hatice Karauzum, M Javad Aman, Nathan K Archer

2183 related Products with: Dry and liquid formulations of IBT-V02, a novel multi-component toxoid vaccine, are effective against isolates from low-to-middle income countries.

200 assays50 ug50 ug100 ul50 ug50 ug 25 G200 assays50 ug25 mg20

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#38574703   2024/04/03 To Up

Development and validation of streptavidin-biotin-based double antibody sandwich ELISA for ricin diagnosis.

Ricin is a potential biowarfare agent. It is a phytotoxin isolated from castor seeds. At present there is no antidote available for ricin poisoning, patients only get supportive treatment based on their symptoms. This highlights the importance of early detection to avoid severity of accidents and reduce the risk factor. Considering this, our study aimed to develop a highly sensitive and specific sandwich ELISA for the detection of ricin.
Shivani Dixit, Jagrati Parashar, Ram Kumar Dhaked, Abdhesh Kumar, Nandita Saxena

1170 related Products with: Development and validation of streptavidin-biotin-based double antibody sandwich ELISA for ricin diagnosis.

1 kit100ug Lyophilized100ug Lyophilized100ug100ug Lyophilized100ug100ug100 ul100ug Lyophilized100ug100ug100ug

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