AdipoGen Life Sciences

anti-Isocitrate Dehydrogenase 1 [IDH1] (R132H Mutant) (human), mAb (AG-IHC132)

CHF 200.00
In stock
AG-20B-6024-R100100 µlCHF 200.00
More Information
Product Details
Product Type Monoclonal Antibody
Properties
Clone AG-IHC132
Isotype Mouse IgG1
Source/Host Purified from concentrated hybridoma tissue culture supernatant.
Immunogen/Antigen Synthetic IDH1 peptide.
Application

Immunohistochemistry: 1:100 - 1:400 for formalin-fixed, paraffin-embedded tissue sections (frozen sections not validated).
ELISA
Optimal conditions must be determined individually for each application.

Recommended Positive Control: Astrocytoma

Crossreactivity Human
Specificity

Recognizes human IDH1 mutated at R132H.

Purity Protein A/G purified.
Formulation Liquid. In Tris Buffer, pH 7.3 - 7.7, containing 1% BSA and <0.1% sodium azide.
Isotype Negative Control

Mouse IgG1 Isotype Control

Other Product Data

UniProt Link O75874: IDH1 (human)

Accession Number O75874
Shipping and Handling
Shipping BLUE ICE
Short Term Storage +4°C
Long Term Storage +4°C
Handling Advice Do not freeze.
Use/Stability Stable for at least 1 year after receipt when stored at +4°C.
Documents
Protocols Download PDF
MSDS Download PDF
Product Specification Sheet
Datasheet Download PDF
Description

Isocitrate Dehydrogenase 1 (IDH1) is a soluble, cytosolic enzyme involved in the TCA metabolic cycle. The most notable mutation in this enzyme, R132H, is clinically indicated in the majority of astrocytomas and oligodendroglial tumors, with the mutation being associated with more favourable prognosis and increased survival in those patients. IDH1 R132H is also useful in the differential diagnosis between anaplastic glioma and glioblastoma.

This antibody is intended to qualitatively identify by light microscopy the presence of associated antigens in sections of formalin-fixed, paraffin-embedded tissue sections using IHC test methods. It has been optimized and validated using the BOND-MAX fully automated IHC&ISH stainer (see Protocol).

Product References
  1. Consequences of IDH1/2 Mutations in Gliomas and an Assessment of Inhibitors Targeting Mutated IDH Proteins: B. Kaminska, et al., Molecules 24, E968 (2019) (Review)
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