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Search results for: Mouse Anti-Human MBP (pThr98) Antibodies

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#31714958   // To Up

Blockade of TIM-1 on the donor graft ameliorates graft-versus-host disease following hematopoietic cell transplantation.

Acute graft-versus-host disease (GVHD) is a leading cause of mortality after allogeneic hematopoietic cell transplantation (HCT) mediated by dysregulated T-cell immune reconstitution. Given the role of the T-cell immunoglobulin and mucin 1 (TIM-1) surface protein in many immune processes, including organ transplantation tolerance, we asked if TIM-1 might drive post-transplant inflammation and acute GVHD. TIM-1 binds to phosphatidylserine (PtdSer), and agonism of TIM1 on immune cells is proinflammatory. HCT conditioning results in a significant supply of PtdSer from apoptosis and cellular debris. Using murine models, treatment with an antagonistic anti-TIM-1 monoclonal antibody (mAb) protects against acute GVHD while maintaining graft-versus-tumor effects. In contrast, the addition of exogenous free PtdSer worsened GVHD in a TIM-1-dependent manner. Importantly, TIM-1 blockade did not alter the expansion of donor T cells in vitro or in vivo. Instead, TIM-1 blockade reduces proinflammatory cytokines and promotes anti-inflammatory factors like carbonic anhydrase 1 and serum amyloid A1 in the gut tissue. This is mediated by TIM-1 on donor cells, as HCT of wild-type (WT) bone marrow (BM) and conventional T (Tcon) cells into TIM-1-/- knockout (KO) recipient mice showed little survival advantage compared with WT recipients, whereas WT recipients of TIM-1-/- KO Tcon cells or TIM1-/- KO BM had improved survival, in part due to the expression of TIM-1 on donor invariant natural killer T cells, which drives inflammation. Finally, in a humanized mouse xenograft GVHD model, treatment with anti-human TIM-1 antagonist mAb reduced GVHD disease burden and mortality. This supports TIM-1 as important for GVHD pathogenesis and as a target for the prevention of GVHD.
Bettina P Iliopoulou, Katie Hsu, Magdiel Pérez-Cruz, Sai-Wen Tang, Wendy W Pang, Tom Erkers, Neeraja Kambham, Gordon J Freeman, Rosemarie H Dekruyff, Everett H Meyer

2583 related Products with: Blockade of TIM-1 on the donor graft ameliorates graft-versus-host disease following hematopoietic cell transplantation.

100ul50 ug 100ul0.1ml (1mg/ml)0.1ml (1mg/ml)100ul1x10e7 cells50 ug 100ml100ug100ug Lyophilized

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#23424669   2013/02/12 To Up

Tailor-making a protein a-derived domain for efficient site-specific photocoupling to Fc of mouse IgG₁.

Affinity proteins binding to antibody constant regions have proved to be invaluable tools in biotechnology. Here, protein engineering was used to expand the repertoire of available immunoglobulin binding proteins via improvement of the binding strength between the widely used staphylococcal protein A-derived Z domain and the important immunoglobulin isotype mouse IgG₁ (mIgG₁). Addressing seven positions in the 58-residue three-helix bundle Z domain by single or double amino acid substitutions, a total of 170 variants were individually constructed, produced in E. coli and tested for binding to a set of mouse IgG₁ monoclonal antibodies (mAbs). The best variant, denoted Z(F5I) corresponding to a Phe to Ile substitution at position 5, showed a typical ten-fold higher affinity than the wild-type as determined by biosensor technology. Eight amino acid positions in the Z(F5I) variant were separately mutated to cysteine for incorporation of a photoactivable maleimide-benzophenone (MBP) group as a probe for site-specific photoconjugation to Fc of mIgG₁, The best photocoupling efficiency to mIgG₁ Fc was seen when the MBP group was coupled to Cys at position 32, resulting in adduct formation to more than 60% of all heavy chains, with no observable non-selective conjugation to the light chains. A similar coupling yield was obtained for a panel of 19 different mIgG₁ mAbs, indicating a general characteristic. To exemplify functionalization of a mIgG₁ antibody via site-specific biotinylation, the Z(F5I-Q32C-MBP) protein was first biotinylated using an amine reactive reagent and subsequently photoconjugated to an anti-human interferon-gamma mIgG₁ mAb. When comparing the specific antigen binding ability of the probe-biotinylated mAb to that of the directly biotinylated mAb, a significantly higher bioactivity was observed for the sample biotinylated using the Z(F5I-Q32C-MBP) probe. This result indicates that the use of a site-specific and affinity probe-mediated conjugation strategy can result in antibody reagents with increased assay sensitivity.
Feifan Yu, Peter Järver, Per-Åke Nygren

1091 related Products with: Tailor-making a protein a-derived domain for efficient site-specific photocoupling to Fc of mouse IgG₁.

0.1 mg100μg0.2 mg0.2 mg0.1 mg100.00 ug100μg25 µg1 mg25 µg100 TESTS100.00 ug

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#15862139   // To Up

[Expression and purification of two kinds of alternative splicing mouse Era].

To express and purify two alternative splicing mouse Era proteins and detect whether anti-human Era antibody can be used in the study of mouse Era proteins.
Ke Dong, Su-min Chen, Zong-ling Ji, Yu Zheng, Nan-chun Chen

2755 related Products with: [Expression and purification of two kinds of alternative splicing mouse Era].

10ml425ml 5ml10ml25ml 5 G100ug10ml100ug5ml

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#6083464   // To Up

Detection of various forms of brain myelin basic protein in vertebrates by electroimmunoblotting.

An electroimmunoblot technique was used to detect various forms of myelin basic protein (MBP) in brain homogenates of 14 vertebrate species. Three antibodies were used to probe the immunoblots: a monoclonal anti-human MPB reacting with an antigenic determinant located at amino acid residues 131 to 136; a polyclonal anti-human MBP and a polyclonal anti-chicken MBP. Because no processing of the tissue is required prior to electrophoresis, in vitro artifacts are minimized. The 18.5 K form of MBP was present in all species except the shark. A 21.5 K MBP was observed in ovine, bovine, pig, rabbit, mouse, rat, monkey, but not in human, guinea pig, shark, toad and marsupial brains. A variant with a molecular weight between 17 K and 18 K was found in mouse, rat, bovine, human, monkey, pig, and chicken brains, and was the sole component in the shark brain. Marsupial brains had five or six forms of MBP between 14.5 K and 18.5 K.
N Kerlero De Rosbo, P R Carnegie, C C Bernard, D S Linthicum

1959 related Products with: Detection of various forms of brain myelin basic protein in vertebrates by electroimmunoblotting.

1 mg 100 μg50ul100ug2 mL1 Set1 Set1 Set5ug 100ul1 Set1 Set

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