NeuroMab™ Anti-CD32b Antibody(NRP-0422-P1802)

Product Overview

Description

The isolated monoclonal antibody binds to human CD32b, which is essential for novel treatments based on therapeutic antibodies, including monoclonal antibody treatment of B-cell lymphoproliferative disorders. Such identification and generation has been hindered by the homology of CD32A to CD32b within the extracellular region. The monoclonal anti-CD32b antibody can be used as an adjuvants, i.e. by boosting an immune response through blocking of the inhibitory effects of CD32b.

Immunogen

Recombinant soluble extracellular domain

Epitope

Fab

Species Reactivity

Human

Clonality

Monoclonal

Host Species

Human

Applications

ELISA; WB; ADCC; Cyt; Block; In Vitro; In Vivo

Relevant Diseases

Systemic Lupus Erythematosus; Malaria

Product Properties

Formulation

PBS only

Preservatives

BSA Free

Concentration

1mg/mL

Purification

Purified recombinant IgG prepared by affinity chromatography on Protein A from a mammalian cell line

Purity

> 95% (SDS-PAGE)

Endotoxin Level

Regular Endotoxin < 5 EU/mg
Low Endotoxin < 1 EU/mg

Shipping

Gel Packs

Storage

Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.

Research Use Only

For research use only

Target

CD32b

Official Name

FCGR2B

Full Name

Fc fragment of IgG receptor IIb

Alternative Names

FCGR2B; CD32; CD32B; FCG2; FCGR2; IGFR2; Fc fragment of IgG receptor IIb; FcRII-c; FCGR2C

Gene ID

2213

Uniprot ID

P31994

Product Pictures

ELISA

Figure 1 shows the binding of anti-CD32b antibodies to (Figure 1A) CD32bECDHis and (Figure 1B) CD32aECDHis measured by ELISA.

FuncS

Figure 10 shows the binding of anti-CD32b antibodies to human peripheral blood leukocytes.

Figure 11 shows the binding of anti-CD32b antibody to CD32bECDHis in Western blot. Under reducing (lanes 1-6) and non-reducing conditions (9-12).

FCM

Figure 2 shows the binding of anti-CD32b antibodies to stably transfected IIA1.6 cells expressing full-length CD32b measured by flow cytometry.

ADCC

Figure 3 shows the ability of anti-CD32b antibody to induce Daudi cell lysis by ADCC compared to HuMab-KLH

FRET

Figure 4 shows CD32b TR-FRET based binding competition data. Maximum TR-FRET fluorescence was determined in samples without unlabeled mAb (which did not compete with labeled mAb). Background fluorescence was measured in samples without CD32bECDHis and CD32aECDHis. The inhibition of a-KLH-AlexaFluor 647 binding to CD32bECDHis and CD32aECDHis was represented by IC50 values (Table 6). The data for antibody 026 illustrate antibodies 020, 022, 024, 028, 053 and 063.

FuncS

Figure 5 shows the in vivo anti-tumor efficacy of anti-CD32b antibodies in a xenograft tumor model in SCID mice. Antibody was administered on day 0 (Figure 5A) or day 6 (Figure 5B) after tumor challenge; shown are mean counts per minute (cpm) values ± SEM for each treatment group.

FuncS

Figure 6 shows the in vivo anti-tumor efficacy of anti-CD32b antibodies in a xenograft tumor model in SCID mice. Antibody was administered on day 6 (Figure 6A and 6B) or 14 days after tumor challenge (Figure 6C); data shown are mean tumor burden ± SEM for each group.

FuncS

Figure 7 shows the ability of anti-CD32b antibodies to induce Daudi cell lysis by ADCC compared to HuMab-KLH. Data shown are mean ± SEM of triplicates.

FuncS

Figure 8 shows the binding of anti-CD32b antibodies to membrane-bound CD32b1 expressed on IIA1.6 cells. Data shown are mean MFI ± stdev of three independent experiments.