Mouse Anti-CCS Recombinant Antibody (CBFYC-1093) (CBMAB-C1150-FY)

Name: Mouse Anti-CCS Recombinant Antibody (CBFYC-1093)
SKU: CBMAB-C1150-FY
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Published Data

Mouse Anti-CCS Recombinant Antibody (CBFYC-1093) (CBMAB-C1150-FY) in WB

Western blot analysis of the CCS protein in lysates of HepG2 cells in the presence and absence of the flavonoids 3-HF or QT and Cu(II). HepG2 cells were stimulated with 20 μM flavonoid with and without 50 μM CuSO4 and incubated for 24 h. Cell lysates were collected, and Western blot analysis was performed using antibodies specific for CCS with α-tubulin as a control. ...View More

Lee, V. J., & Heffern, M. C. (2022). Structure-activity assessment of flavonoids as modulators of copper transport. Frontiers in Chemistry, 10, 972198. Distributed under Open Access license CC BY 4.0, without modification.

Mouse Anti-CCS Recombinant Antibody (CBFYC-1093) (CBMAB-C1150-FY) in WB

Effects of liquid fructose supplementation and/or stress on the level of copper chaperone CCS and antioxidant enzymes. Protein level of CCS in renal whole cell extracts, was measured by Western blot. Scatter plot with bar graphs represent the means ± SEMs for each protein normalized to β-actin and expressed relative to controls (n = 6 animals/group). Two-way ANOVA was used to evaluate the effects of fructose and stress, and their interaction. Asterisk denotes statistically significant main effect of fructose. p < 0.05. ...View More

Tasić, D., Opačić, M., Kovačević, S., Nikolić Kokić, A., Dimitrijević, M., Nikolić, D., ... & Brkljačić, J. (2022). Effects of fructose and stress on rat renal copper metabolism and antioxidant enzymes function. International Journal of Molecular Sciences, 23(16), 9023. Distributed under Open Access license CC BY 4.0, without modification.

Mouse Anti-CCS Recombinant Antibody (CBFYC-1093) (CBMAB-C1150-FY) in WB

PA induces changes in proteins associated with copper export and induces a subcellular localization of ATP7B that resembles cytosolic copper overload in liver cells. Representative western blot images, densitometry, and gene expression analysis of CCS (n = 9) and COMMD1 (n = 10) from lysates collected at different stimulation times with PA. ...View More

Harder, N. H., Lee, H. P., Flood, V. J., San Juan, J. A., Gillette, S. K., & Heffern, M. C. (2022). Fatty acid uptake in liver hepatocytes induces relocalization and sequestration of intracellular copper. Frontiers in Molecular Biosciences, 9, 863296. Distributed under Open Access license CC BY 4.0, without modification.

Mouse Anti-CCS Recombinant Antibody (CBFYC-1093) (CBMAB-C1150-FY) in Immunoblot

Immunoblot detection of biotinylated MEK1, ATP7A, SOD1, MYC-BirA, MYC-BirA-ATOX1, or MYC-BirA-CCS from strepavadin pulldowns and whole cell extracts from HEK-HT cells stably expressing MYC-BirA, MYC-BirA-ATOX1, or MYC-BirA-CCS treated with media with (+) or without (−) biotin for 48 h. n = 2 biologically independent experiments. ...View More

Grasso, M., Bond, G. J., Kim, Y. J., Boyd, S., Dzebo, M. M., Valenzuela, S., ... & Brady, D. C. (2021). The copper chaperone CCS facilitates copper binding to MEK1/2 to promote kinase activation. Journal of Biological Chemistry, 297(6). Distributed under Open Access license CC BY 4.0, without modification.

Mouse Anti-CCS Recombinant Antibody (CBFYC-1093) (CBMAB-C1150-FY) in WB

Representative immunoblots of copper chaperone for superoxide dismutase (CCS) protein levels. ...View More

Greco, M., Spinelli, C. C., De Riccardis, L., Buccolieri, A., Di Giulio, S., Musarò, D., ... & Maffia, M. (2021). Copper dependent modulation of α-synuclein phosphorylation in differentiated Shsy5y neuroblastoma cells. International Journal of Molecular Sciences, 22(4), 2038. Distributed under Open Access license CC BY 4.0, without modification.

Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

CBFYC-1093

Application

ELISA, IF, IP, WB, IHC-P

Immunogen

Amino acids 1-274 representing full length CCS of human origin.

Host Species

Mouse

Specificity

Human, Mouse, Rat

Antibody Isotype

IgG1, κ

Clonality

Monoclonal Antibody

Application Notes

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Application	Note
WB	1:100-1:1,000
IP	1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)	1:50-1:500
ELISA	1:100-1:1,000
IHC-P	1:50-1:500

Formulations & Storage [For reference only, actual COA shall prevail!]

Format

Liquid

Buffer

PBS, 0.1% gelatin

Preservative

< 0.1% sodium azide

Concentration

0.2 mg/ml

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at-20°C long term. Avoid repeated freeze/thaw cycles.

More Infomation

Target

Full Name

Copper Chaperone For Superoxide Dismutase

Introduction

CCS (Copper Chaperone For Superoxide Dismutase) is a Protein Coding gene. Diseases associated with CCS include Entropion and Amyotrophic Lateral Sclerosis 1. Among its related pathways are Detoxification of Reactive Oxygen Species and Amyotrophic lateral sclerosis (ALS). Gene Ontology (GO) annotations related to this gene include copper ion binding and copper ion transmembrane transporter activity. An important paralog of this gene is SOD1.

Entrez Gene ID

9973

UniProt ID

O14618

Function

Delivers copper to copper zinc superoxide dismutase (SOD1).

Biological Process

Cellular response to oxidative stress Source: Reactome
Positive regulation of oxidoreductase activity Source: Ensembl
Protein maturation by copper ion transfer Source: ProtInc
Removal of superoxide radicals Source: GO_Central
Superoxide metabolic process Source: ProtInc

Cellular Location

Cytoplasm

PTM

Ubiquitinion by XIAP/BIRC4 leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. XIAP/BIRC4 preferentially ubiquitinates at Lys-241.

Wen, C. Y., Shan, C. L., Sun, W. J., Wan, Y., Lin, R., Chen, B., ... & Yonghui, H. (2021). Copper chaperone for superoxide dismutase expression is down-regulated and correlated with more malignant tumoral features and poor prognosis in human hepatocellular carcinoma.

Boyd, S. D., Ullrich, M. S., Calvo, J. S., Behnia, F., Meloni, G., & Winkler, D. D. (2020). Mutations in superoxide dismutase 1 (Sod1) linked to familial amyotrophic lateral sclerosis can disrupt high-affinity zinc-binding promoted by the copper chaperone for Sod1 (Ccs). Molecules, 25(5), 1086.

Li, Y., Liang, R., Zhang, X., Wang, J., Shan, C., Liu, S., ... & Zhang, S. (2019). Copper chaperone for superoxide dismutase promotes breast cancer cell proliferation and migration via ROS-mediated MAPK/ERK signaling. Frontiers in pharmacology, 10, 356.

Skopp, A., Boyd, S. D., Ullrich, M. S., Liu, L., & Winkler, D. D. (2019). Copper–zinc superoxide dismutase (Sod1) activation terminates interaction between its copper chaperone (Ccs) and the cytosolic metal-binding domain of the copper importer Ctr1. Biometals, 32(4), 695-705.

Ge, Y., Wang, L., Li, D., Zhao, C., Li, J., & Liu, T. (2019). Exploring the extended biological functions of the human copper chaperone of superoxide dismutase 1. The protein journal, 38(4), 463-471.

Fukuoka, M., Tokuda, E., Nakagome, K., Wu, Z., Nagano, I., & Furukawa, Y. (2017). An essential role of N-terminal domain of copper chaperone in the enzymatic activation of Cu/Zn-superoxide dismutase. Journal of inorganic biochemistry, 175, 208-216.

Luchinat, E., Barbieri, L., & Banci, L. (2017). A molecular chaperone activity of CCS restores the maturation of SOD1 fALS mutants. Scientific reports, 7(1), 1-8.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme-Linked Immunospot (ELISpot)
Proteogenomics
Other Protocols

Antibody Pairs

CCS Matched Antibody Pair (202) (CAT#: APMAB-202LY)

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Isotype control

For research use only. Not intended for any clinical use.

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We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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