Superoxide dismutase copper chaperone antibody

Catalog No. ABIN499056

The Rabbit Polyclonal anti-Superoxide dismutase copper chaperone antibody (ABIN499056) specifically detects Superoxide dismutase copper chaperone in WB. The antibody is reactive with Human samples.

Quick Overview for Superoxide dismutase copper chaperone antibody (ABIN499056)

Target: Superoxide dismutase copper chaperone (CCS) (Copper Chaperone For Superoxide Dismutase (CCS))

Reactivity: Human

Host: Rabbit

Clonality: Polyclonal

Conjugate: This Superoxide dismutase copper chaperone antibody is un-conjugated

Application: Western Blotting (WB)

Product Details anti-Superoxide dismutase copper chaperone Antibody

Specificity: This antibody detects endogenous levels of CCCS protein. (region surrounding Pro271)

Cross-Reactivity (Details): Species reactivity (tested):Human.

Purification: Affinity chromatography

Purity: > 95 % by SDS-PAGE

Application Details

Application Notes: Western Blot: 1/500 - 1/1000.
Other applications not tested.
Optimal dilutions are dependent on conditions and should be determined by the user.

Restrictions: For Research Use only

Handling

Concentration: 1,0 mg/mL

Buffer: Phosphate buffered saline (PBS), pH 7.2., 0.05 % sodium azide

Preservative: Sodium azide

Precaution of Use: This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Handling Advice: Avoid repeated freezing and thawing.

Storage: 4 °C/-20 °C

Storage Comment: Store the antibody undiluted at 2-8 °C for one month or (in aliquots) at -20 °C for longer.

Target Details for Superoxide dismutase copper chaperone

Target: Superoxide dismutase copper chaperone (CCS) (Copper Chaperone For Superoxide Dismutase (CCS))

Alternative Name: CCS

Background: Cu-Zn superoxide dismutase-1 (SOD-1) is a well characterized cytosolic scavenger of oxygen free radicals that requires copper and zinc binding to potentiate its enzymatic activity. Copper chaperone for SOD-1 (CCS) is essential for the incorporation of copper into SOD-1, and therefore is necessary for its enzymatic activity. CCS prevents copper ions from binding to intracellular copper scavengers and provides the SOD-1 enzyme with the necessary copper cofactor. CCS escorts copper only to SOD-1 and fails to deliver copper to proteins in the mitochondria, nucleus or secretory pathway. CCS interacts with both wildtype and mutated forms of SOD-1 through CCS domains that are homologous in SOD-1. CCS exists as a homodimer that may form a heterodimer with SOD-1 during copper loading. While many tissues express CCS, the chaperone is most abundant in the kidney, liver and Purkinje cells in the neuropil of the central nervous system. The gene for CCS maps to human chromosome 11q13.Synonyms: SOD-4, Superoxide Dismutase Copper Chaperone

Molecular Weight: approx. 32 kDa

Gene ID: 9973

NCBI Accession: NP_005116

UniProt: O14618

Pathways: Transition Metal Ion Homeostasis