Search results for: Anti Acetyl Lysine biotin conjugate
#36167521 2022/09/27 To Up
Site-Selective Lysine Acetylation of Human Immunoglobulin G for Immunoliposomes and Bispecific Antibody Complexes.
Site-selective acetylation of a single lysine residue in a protein that reaches a lysine acetyltransferase's accuracy, precision, and reliability is challenging. Here, we report a peptide-guided, proximity-driven group transfer reaction that acetylates a single lysine residue, Lys 248, of the fragment crystallizable region (Fc region) in the heavy chain of the human Immunoglobulin G (IgG). An Fc-interacting peptide bound with the Fc domain and positioned a phenolic ester close to Lys 248, which induced a nucleophilic reaction and resulted in the transfer of an acetyl group to Lys 248. The acetylation reaction proceeded to a decent yield under the physiological condition without the need for deglycosylation, unnatural amino acids, or catalysts. Along with acetylation, functional moieties such as azide, alkyne, fluorescent molecules, or biotin could also be site-selectively installed on Lys 248, allowing IgG's further derivatization. We then synthesized an antibody-lipid conjugate and constructed antibody-conjugated liposomes (immunoliposomes), targeting HER2-positive (HER2+) cancer cells. We also built a bispecific antibody complex (bsAbC) covalently linking an anti-HER2 antibody and an anti-CD3 antibody. The bsAbC showed effector-cell-mediated cytotoxicity at nanomolar concentrations. Compared with bispecific antibodies (bsAbs), bsAbCs are constructed based on native IgGs and contain two antigen-binding sites to each antigen, twice that of bsAbs. Altogether, this work reports a method of site-selective acetylation of native antibodies, highlights a facile way of site-selective IgG functionalization, and underscores the potential of bsAbCs in cancer immunotherapy.Dingdong Yuan, Yu Zhang, King Hoo Lim, Stephen King Pong Leung, Xizi Yang, Yujie Liang, Wilson Chun Yu Lau, Kwan T Chow, Jiang Xia
2790 related Products with: Site-Selective Lysine Acetylation of Human Immunoglobulin G for Immunoliposomes and Bispecific Antibody Complexes.
100ug Lyophilized100μg 100ul 100ul4 Sample Kit0.1 mg100ug 100ul4 Arrays/Slide 100ul100ug Lyophilized 100ulRelated Pathways
#23718707 2013/06/25 To Up
Histone biotinylation in Candida albicans.
Candida albicans is an opportunistic fungal pathogen in humans. It is a polymorphic fungus: it can live as yeasts, hyphae, or pseudohyphae. Biotin is required for cell growth and fatty acid metabolism because it is used as a cofactor for carboxylases such as acetyl-CoA carboxylase, and pyruvate carboxylase. In addition, we have discovered that biotin is used to modify histones in C. albicans. Biotinylation was detected by Western blots using a monoclonal antibiotin HRP-conjugated antibody as well as with qTOF and LC/MS/MS mass spectrometry. As a precaution, the antibiotin antibody was dialyzed against neutravidin prior to use. During this study, we observed that three histones, H2A, H2B, and H4, were biotinylated at many lysine residues in an apparently nonsite-specific manner. Roughly, equivalent levels of acetylation, methylation, and phosphorylation were found in histones from biotin-replete and biotin-starved cells, but histone biotinylation was only observed for cells grown in excess biotin. The function of histone biotinylation in C. albicans is still unknown but, because C. albicans is a natural biotin auxotroph, a storage reservoir for biotin is attractive. Techniques used to detect histone biotinylation in C. albicans did not detect any histone biotinylation in Saccharomyces cerevisiae.Sahar Hasim, Swetha Tati, Nandakumar Madayiputhiya, Renu Nandakumar, Kenneth W Nickerson
2467 related Products with: Histone biotinylation in Candida albicans.
50mg96 assays 1 mL100 ug10mg48 assays 5mg96 assays 1 mL5mg48 assays 1 mLRelated Pathways
#17566976 2007/06/13 To Up
Synthesis and characterization of PAMAM dendrimer-based multifunctional nanodevices for targeting alphavbeta3 integrins.
We have synthesized a stable and clinically relevant nanodevice (cRGD-BT-ND; ND for short) that exhibits superior binding to the biologic target alphavbeta3 integrins, when either compared to the same free cRGD peptide or to the biotinylated nanodevice without covalently attached peptides (BT-ND). Selective targeting of alphavbeta3 integrins was achieved by coupling cyclic cRGD peptides to the nanodevice (ND) surface, while biotin groups (BT) were used for amplified detection of bound cRGD-BT-ND by anti-biotin antibody or avidin linked to horseradish peroxidase after binding. The synthesis involved the following steps: the amino-terminated ethylenediamine core generation 5 poly(amidoamine) (PAMAM_E5.NH2) dendrimer was first partially acetylated and then biotinylated, and residual primary amine termini were converted to succinamic acid groups (SAH), some of which finally were conjugated with cRGD peptide residues through the amino group of the lysine side chain. The starting material and all derivatives were extensively characterized by polyacrylamide gel electrophoresis (PAGE), size exclusion chromatography (SEC), potentiometric acid-base titration, MALDI-TOF, and NMR. Cytotoxicity of all dendrimer derivatives was examined in B16F10 melanoma cell cultures using the XTT colorimetric assay for cellular viability. Binding of nanodevices to the biological target was determined using plates coated with human alphavbeta3 integrin and alphavbeta3 receptor expressing human dermal microvascular endothelial cells (HDMECs). The PAMAM_E5.(NHAc)72(NHBT)8(NHSAH)35(NHSA-cR GD)4 nanodevice is nontoxic within physiologic concentration ranges and specifically binds to the alphavbeta3 integrins, apparently much stronger than the cyclic cRGD peptide itself.Wojciech G Lesniak, Muhammed S T Kariapper, Bindu M Nair, Wei Tan, Alan Hutson, Lajos P Balogh, Mohamed K Khan
2122 related Products with: Synthesis and characterization of PAMAM dendrimer-based multifunctional nanodevices for targeting alphavbeta3 integrins.
100ug100 Rxns Kit 100ul1,000 tests200ug1.0 mg200 mg500 tests0.1ml (1mg/ml)1 mgRelated Pathways
Contact Us:
Belgium
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45 Fax 0032 16 50 90 45
[email protected]
France
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50 Fax 01 43 25 01 60
[email protected]
Germany
GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Tel 0241 40 08 90 86 Fax 0241 55 91 05 36
[email protected]
United Kingdom
GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
[email protected]
Also in
Luxembourg +35220880274
Schweiz Züri +41435006251
Danmark +4569918806
Österreich +43720880899
Česká republika Praha +420246019719
Ireland Dublin +35316526556
Norge Oslo +4721031366
Finland Helsset +358942419041
Sverige Stockholm +46852503438
Ελλάς Αθήνα +302111768494
Magyarország Budapest +3619980547
Poland
GENTAUR Poland Sp. z o.o.
ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
Tel 058 710 33 44
Fax 058 710 33 48
[email protected]
skype gentaurpoland
Nederland
GENTAUR Nederland BV
Kuiper 1
5521 DG Eersel Nederland
Tel 0208-080893 Fax 0497-517897
[email protected]
Italy
GENTAUR SRL
IVA IT03841300167
Piazza Giacomo Matteotti, 6, 24122 Bergamo
Tel 02 36 00 65 93 Fax 02 36 00 65 94
[email protected]
Spain
GENTAUR Spain
Tel 0911876558
[email protected]
Bulgaria
GENTAUR Bulgaria
53 Iskar Str. 1191 Kokalyane, Sofia
Sofia 1000
Tel 0035924682280
Fax 0035929830072
[email protected]