Human SOD1/Cu‑Zn SOD Alexa Fluor™ Plus 594‑conjugated Antibody

R&D Systems | Catalog # FAB3418AFP594

R&D Systems

Key Product Details

Species Reactivity

Human

Applications

Knockout Validated, Western Blot, Immunocytochemistry

Label

Alexa Fluor Plus 594 (Excitation = 590 nm, Emission = 618 nm)

Antibody Source

Monoclonal Mouse IgG2A Clone # 348808
View all SOD1/Cu-Zn SOD Primary Antibodies »

Product Specifications

Specificity

Detects human SOD1/Cu‑Zn SOD in Western blots. In Western blots, no cross-reactivity with recombinant human (rh) SOD2 or rhSOD3 is observed.

Clonality

Monoclonal

Host

Mouse

Isotype

IgG2A

Applications for Human SOD1/Cu‑Zn SOD Alexa Fluor™ Plus 594‑conjugated Antibody

Application
Recommended Usage

Immunocytochemistry

Optimal dilution of this antibody should be experimentally determined.

Knockout Validated

Optimal dilution of this antibody should be experimentally determined.

Western Blot

Optimal dilution of this antibody should be experimentally determined.

Formulation, Preparation, and Storage

Formulation

Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.

Shipping

The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

Stability & Storage

Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied

Background: SOD1/Cu-Zn SOD

Superoxide Dismutases (SODs), originally identified as Indophenoloxidase (IPO), are enzymes that catalyze the conversion of naturally-occuring but harmful superoxide radicals into molecular oxygen and hydrogen peroxide. Superoxide Dismutases 1, SOD1, also known as Cu/Zn SOD, soluble SOD and IPO-A, is a soluble, cytoplasmic 16 kDa homodimer. Each SOD1 monomer binds one Cu2+ and one Zn2+ ion. Three isozymes of SOD have been identified and are functionally related but have very modest sequence homology. SOD1 shares 23% and 27% sequence identity with SOD2 and SOD3, respectively. Mutations in SOD1 have been implicated as causes of familial amyotrophic lateral sclerosis (ALS). The ALS-causing mutations of SOD1 are scattered throughout the protein and provide no clear functional or structural clues to the underlying disease mechanism. The oligomerization hypothesis suggests that mutant SOD1 proteins become misfolded and consequently oligomerize into high molecular weight aggregates that result in the death of motor neurons. The oxidative damage hypothesis suggests that loss of function mutation in SOD1 protein results in the accumulation of cellular superoxide radical, leading to free radical-mediated damage, the release of cytochrome c, and apoptosis.

Long Name

Superoxide Dismutase-1

Alternate Names

Cu-Zn SOD, CuZn SOD, Ipo1, IPOA, SOD, cytosolic, SOD, Soluble

Entrez Gene IDs

6647 (Human); 20655 (Mouse); 24786 (Rat)

Gene Symbol

SOD1

UniProt

P00441

Additional SOD1/Cu-Zn SOD Products

Product Documents for Human SOD1/Cu‑Zn SOD Alexa Fluor™ Plus 594‑conjugated Antibody

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot or batch number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Human SOD1/Cu‑Zn SOD Alexa Fluor™ Plus 594‑conjugated Antibody


This product is provided under an intellectual property license from Life Technologies Corporation. The transfer of this product is conditioned on the buyer using the purchased product solely in research conducted by the buyer, excluding contract research or any fee for service research, and the buyer must not (1) use this product or its components for (a) diagnostic, therapeutic or prophylactic purposes; (b) testing, analysis or screening services, or information in return for compensation on a per-test basis; or (c) manufacturing or quality assurance or quality control, and/or (2) sell or transfer this product or its components for resale, whether or not resold for use in research. For information on purchasing a license to this product for purposes other than as described above, contact Life Technologies Corporation, 5781 Van Allen Way, Carlsbad, CA 92008 USA or outlicensing@thermofisher.com.

For research use only

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Protocols

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FAQs

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