Human IgG1 Kappa Isotype Control Antibody (Low Endotoxin, Azide-Free) (DAG-IC61) Functional Grade

Human IgG1 Kappa Isotype Control Antibody (Low Endotoxin, Azide-Free) for ELISA, FLISA, FC, IP, Control, Blocking, SPR


Host Species
Antibody Isotype
IgG1, κ
Species Reactivity
Functional Grade


Application Notes
ELISA, FLISA, FC, IP, Control, Blocking, SPR
*Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own experiment using appropriate negative and positive controls.


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A chimeric antibody to varicella-zoster virus glycoprotein E


Authors: Shankar, V; Kools, JJ; Armour, KL; Clark, MR

Varicella-Zoster virus (VZV) immune globulin (VZIG) derived from pooled human serum is currently used in immunotherapy of VZV-associated complications of chickenpox and shingles. We developed a mouse-human chimeric antibody against a VZV glycoprotein E (gE) epitope as a safer replacement for VZIG. Variable (V) heavy- and V kappa light-chain exons, derived from an anti-VZV gE antibody secreting mouse hybridoma cell line, were cloned into expression vectors containing an immunoglobulin promoter and enhancer, and human IgG1 or kappa constant (C) region genes. The expression vectors were cotransfected into mouse myeloma cell line (NSO), generating transformants that secreted chimeric human-mouse IgGs. The chimeric and the parent mouse antibody were indistinguishable in their antigen binding specificity. VZV gE chimeric antibody may prove to be a prophylactic antibody that could provide significant advantages over VZIG in having defined specificity, lessened possibility of contamination with viral pathogens, and consistent availability.

Biological activities on T lymphocytes of a baculovirus-expressed chimeric recombinant IgG(1) antibody with specificity for the CDR3-like loop on the D1 domain of the CD4 molecule


Authors: Troadec, S; Bes, C; Chentouf, M; Nguyen, B; Briant, L; Jacquet, C; Chebli, K; Pugniere, M; Roquet, F; Cerutti, M; Chardes, T

A bacutovirus-expressed chimeric recombinant IgG(1) (rlgG(1)) antibody, with C gamma(1) and C kappa human constant domains, was derived from the murine monoclonal antibody (mAb) 13B8.2, which is specific for the CDR3-like loop of the CID4 molecule and which inhibits HIV-1 replication. Chimeric rlgG1 antibody 13B8.2 blocked, in a dose-dependent manner, antigen presentation through inhibition of subsequent IL-2 secretion by stimulated T cells. The one-way mixed lymphocyte reaction was abrogated by previous addition of baculovirus-produced rlgG1 13B8.2 in the T-cell culture. Anti-proliferative activity of rlgG1 was demonstrated on CD3-activated CD4* T lymphocytes from healthy donors, such effect being associated with reduced IL-2 secretion of activated T cells. On the other hand, no proliferation inhibition was observed on CD4(+) T lymphocytes activated with phorbol ester plus ionomycin, suggesting that rlgG, 13B8.2 preferentially acts on a proximal TCR-induced signaling pathway. Treatment of DBA1/J human CD4-transgenic mice with 100 mu g of recombinant antibody for three consecutive days led to in vivo recovery of rlgG1 antibody 13B8.2 both coated on murine T lymphocytes and free in mouse serum, without CD4 depletion or down-modulation. These findings predict that the bacutovirusexpressed chimeric rlgG1 anti-CD4 antibody 13B8.2 is a promising candidate for immunotherapy. (c) 2005 Elsevier Inc. Alt rights reserved.

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