InVivoMAb polyclonal human IgG

Catalog #BE0092

$164.00 - $4,280.00

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  • 100 mg - $4,280.00
  • 50 mg - $3,024.00
  • 25 mg - $2,009.00
  • 5 mg - $600.00
  • 1 mg - $164.00
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Product Details

The polyclonal human IgG is purified from human serum. It is ideal for use as a non-reactive control IgG for human IgG antibodies in most in vivo and in vitro applications.


Isotype Human IgG
Recommended Dilution Buffer InVivoPure pH 7.0 Dilution Buffer
Conjugation This product is unconjugated. Conjugation is available via our Antibody Conjugation Services.
Formulation PBS, pH 7.0
Contains no stabilizers or preservatives
Endotoxin <2EU/mg (<0.002EU/μg)
Determined by LAL gel clotting assay
Purity >95%
Determined by SDS-PAGE
Sterility 0.2 µm filtration
Purification Protein A
RRID AB_1107779
Molecular Weight 150 kDa
Human Pathogen Test Results Hepatitis B Surface Antigen: Negative
Hepatitis B Core Antigen antibodies: Negative
Human Immunodeficiency Virus 1: Negative
Human Immunodeficiency Virus 2: Negative
Hepatitis C Virus antibodies: Negative
* These tests cannot guarantee the absence of infective agents
Storage The antibody solution should be stored at the stock concentration at 4°C. Do not freeze.
Thura, M., et al. (2016). "PRL3-zumab, a first-in-class humanized antibody for cancer therapy" JCI Insight 1(9): e87607. PubMed

Novel, tumor-specific drugs are urgently needed for a breakthrough in cancer therapy. Herein, we generated a first-in-class humanized antibody (PRL3-zumab) against PRL-3, an intracellular tumor-associated phosphatase upregulated in multiple human cancers, for unconventional cancer immunotherapies. We focused on gastric cancer (GC), wherein elevated PRL-3 mRNA levels significantly correlated with shortened overall survival of GC patients. PRL-3 protein was overexpressed in 85% of fresh-frozen clinical gastric tumor samples examined but not in patient-matched normal gastric tissues. Using human GC cell lines, we demonstrated that PRL3-zumab specifically blocked PRL-3(+), but not PRL-3(-), orthotopic gastric tumors. In this setting, PRL3-zumab had better therapeutic efficacy as a monotherapy, rather than simultaneous combination with 5-fluorouracil or 5-fluorouracil alone. PRL3-zumab could also prevent PRL-3(+) tumor recurrence. Mechanistically, we found that intracellular PRL-3 antigens could be externalized to become “extracellular oncotargets” that serve as bait for PRL3-zumab binding to potentially bridge and recruit immunocytes into tumor microenvironments for killing effects on cancer cells. In summary, our results document a comprehensive cancer therapeutic approach to specific antibody-targeted therapy against the PRL-3 oncotarget as a case study for developing antibodies against other intracellular targets in drug discovery.

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