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Creative Biolabs
Product

Human Anti-DJ-1 (CBP1952)

[CAT#: NAB2007FY442]

Human Monoclonal [W0042] to DJ-1 (Oxidized At C106)

Host Species:
Human
Species Reactivity:
Human
Applications:
ELISA; WB

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Product Overview

Description

The human anti-human DJ-1 antibody, clone AbD03055, recognizes the human DJ-1 oncogene only when it is oxidized on cysteine C106. DJ-1 plays a role in transcriptional regulation and anti-oxidative stress response. The oxidation state of DJ-1, especially at C106, can adjust the function of DJ-1 (Canet-Avilés et al., 2004). DJ-1 oxidative disorder seems to be related to the onset of diseases such as Parkinson's disease.

Immunogen

The DJ-1 peptide is oxidized at C106 (sequence LIAAIC(SO3)AGPTA).

Species Reactivity

Human

Clonality

Monoclonal

Host Species

Human

Isotype

HuCAL Fab bivalent

Clone Number

CBP1952

Applications

ELISA; WB

Relevant Diseases

Parkinson's Disease

Research Areas

Neuroregeneration

Conjugation

Unconjugated
Product Properties

Form

Liquid

Formulation

PBS; 0.01% Thiomersal

Preservatives

Yes

Concentration

0.5 mg/ml

Shipping

The product is shipped at 4°C. Upon receipt, store it immediately at the temperature recommended below.

Storage

Store at +4°C or at -20°C if preferred.
Storage in frost-free freezers is not recommended.
This product should be stored undiluted. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend microcentrifugation before use.

Research Use Only

For research use only, not for diagnostic or therapeutic use.
Target

Target

PARK7

Official Name

PARK7

Full Name

Protein deglycase DJ-1

Alternative Names

PARK7; DJ-1; DJ1; HEL-S-67p; Parkinsonism associated deglycase; GATD2

Gene ID

11315(Human); 57320(Mouse); 117287(Rat)

Uniprot ID

Q99497(Human); Q99LX0(Mouse); O88767(Rat)
References

1. Andres-Mateos, E. et al. (2007) DJ-1 gene deletion reveals that DJ-1 is an atypical peroxiredoxin-like peroxidase.
2. Bitar, M.S. et al. (2012) Decline in DJ-1 and decreased nuclear translocation of Nrf2 in Fuchs endothelial corneal dystrophy.
3. Zhang C et al. (2008) Role of NonO-histone interaction in TNFalpha-suppressed prolyl-4-hydroxylase alpha1.
Publications

Publications (0)

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