Rabbit Anti-Human ALKBH2 (a.a. 1-259) Polyclonal antibody

Name: Rabbit Anti-Human ALKBH2 (a.a. 1-259) Polyclonal antibody
SKU: DPABH-06375
Rating: 5 (1 reviews)

Rabbit Anti-Human ALKBH2 (a.a. 1-259) Polyclonal antibody for WB, ELISA

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COA

SDS

Datasheet

Key features and details

Target: Human ALKBH2
Host: Rabbit
Application: WB, ELISA
Species Reactivity: Human

Summary

Specifications

Antibody Isotype

IgG

Species Reactivity

Human

Immunogen

Recombinant human ALKBH2 protein; Source: E. coli derived, PGEX-4T; Tag: GST; Domain: 1-259 aa of BC070489

Conjugate

Unconjugated

Applications

Application Notes

WB: 1:500-1:1000

General Notes

This product (Catalog No. DPABH-06375) is a rabbit-derived polyclonal antibody raised against human ALKBH2, targeting the amino acid region 1–259 of the protein. It has been affinity purified by Protein A. Escherichia coli AlkB is a DNA repair enzyme that represents the founding member of the AlkB family of non-heme iron-dependent dioxygenases. The human genome encodes nine AlkB homologs termed AlkB homolog 1 through 8 (ALKBH1 through 8) plus a ninth member termed fat mass and obesity associated (FTO). Bacterial AlkB as well as human ALKBH2 and ALKBH3 catalyze the direct reversal of DNA methylation damage through a distinct oxidative demethylation reaction. Importantly, ALKBH2 has been shown to play a role in DNA alkylation damage repair in human, mouse and plant cells. Full-length ALKBH2 has a molecular weight of about 30kDa and ALKBH2 variant encoded by an alternatively spliced transcript with a frameshift deletion of the C-terminal dioxygenase domain has a molecular weight of about 25kDa (PMID:22079122).
DPABH-06375 is suitable for use in Western blot (WB) (1:500–1:1,000) application.
DPABH-06375 is supplied as a liquid formulation in PBS with 0.02% sodium azide and 50% glycerol, pH 7.3. For long-term storage, keep at −20 °C. For short-term use, store at 2–8 °C. Avoid repeated freeze–thaw cycles to maintain antibody integrity and performance.

Target

Alternative Names

ABH2; ALKBH2; Oxy DC1

Entrez Gene ID

121642

UniProt ID

Q6NS38

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Q & A

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Q: Does DPABH-06375 antibody have Conjugate?

A: Unconjugated

Customer Reviews

References

Duplex interrogation by a direct DNA repair protein in search of base damage

NATURE STRUCTURAL & MOLECULAR BIOLOGY

Authors: Yi, Chengqi; Chen, Baoen; Qi, Bo; Zhang, Wen; Jia, Guifang; Zhang, Liang; Li, Charles J.; Dinner, Aaron R.; Yang, Cai-Guang; He, Chuan

Abstract

ALKBH2 is a direct DNA repair dioxygenase guarding the mammalian genome against N-1-methyladenine, N-3-methylcytosine and 1,N-6-ethenoadenine damage. A prerequisite for repair is to identify these lesions in the genome. Here we present crystal structures of human ALKBH2 bound to different duplex DNAs. Together with computational and biochemical analyses, our results suggest that DNA interrogation by ALKBH2 has two previously unknown features: (i) ALKBH2 probes base-pair stability and detects base pairs with reduced stability, and (ii) ALKBH2 does not have nor need a damage-checking site, which is critical for preventing spurious base cleavage for several glycosylases. The demethylation mechanism of ALKBH2 insures that only cognate lesions are oxidized and reversed to normal bases, and that a flipped, non-substrate base remains intact in the active site. Overall, the combination of duplex interrogation and oxidation chemistry allows ALKBH2 to detect and process diverse lesions efficiently and correctly.

The complex structures of ALKBH2 mutants cross-linked to dsDNA reveal the conformational swing of beta-hairpin

SCIENCE CHINA-CHEMISTRY

Authors: Chen BaoEn; Gan JianHua; Yang CaiGuang

Abstract

Mammalian AlkB homologue 2 (ALKBH2) is the primary housekeeping DNA demethylase, effectively repairing endogenously formed methylated lesions in double-stranded DNA. Our previous studies demonstrated that a hydrophobic beta-hairpin motif of ALKBH2 could play crucial roles in base-pair stability interrogation and damaged base flipping. Using chemical cross-linking strategy, we obtained two crystal structures of human ALKBH2 mutant bound to duplex DNA. The structural analysis suggests that the beta-hairpin motif is flexible in conformation and is likely to slide along the DNA duplex in local regions to search for damaged base. This study provides a new mechanistic insight into DNA damage detection by ALKBH2.