Mouse Anti-ISCU Recombinant Antibody (3B8-1C4) (CBMAB-A5977-LY)

Name: Mouse Anti-ISCU Recombinant Antibody (3B8-1C4)
SKU: CBMAB-A5977-LY
Rating: 5 (1 reviews)

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Datasheet

SDS

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

Basic Information

Host Animal

Mouse

Clone

3B8-1C4

Application

WB, ELISA

Immunogen

NIFUN (AAH11906, 26 a.a. ~ 167 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Specificity

Human

Antibody Isotype

IgG1, κ

Clonality

Monoclonal

Application Notes

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

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

Format

Liquid

Purity

> 95% Purity determined by SDS-PAGE.

Storage

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

More Infomation

Target

Full Name

iron-sulfur cluster scaffold homolog (E. coli)

Introduction

Iron-sulfur (Fe-S) clusters are necessary for several mitochondrial enzymes and other subcellular compartment proteins. They contain sulfur and iron, and are created via several steps that include cysteine desulfurases, iron donors, chaperones, and scaffold proteins. This gene encodes the two isomeric forms, ISCU1 and ISCU2, of the Fe-S cluster scaffold protein. Mutations in this gene have been found in patients with myopathy with severe exercise intolerance and myoglobinuria. [provided by RefSeq]

Entrez Gene ID

23479

UniProt ID

Q9H1K1

Alternative Names

2310020H20Rik; HML; ISU2; MGC74517; NIFU; NIFUN; hnifU

Function

Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins (PubMed:11060020).
First, a [2Fe-2S] cluster is transiently assembled on the scaffold protein ISCU. In a second step, the cluster is released from ISCU, transferred to a glutaredoxin GLRX5, followed by the formation of mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and their target-specific insertion into the recipient apoproteins. Cluster assembly on ISCU depends on the function of the cysteine desulfurase complex NFS1-LYRM4/ISD11, which serves as the sulfur donor for cluster synthesis, the iron-binding protein frataxin as the putative iron donor, and the electron transfer chain comprised of ferredoxin reductase and ferredoxin, which receive their electrons from NADH (By similarity).
Isoform 2
Functions as a cytoplasmic scaffold protein for the de novo synthesis of iron-sulfur clusters in the cytoplasm.

Biological Process

Cellular iron ion homeostasisManual Assertion Based On ExperimentIBA:GO_Central
Iron-sulfur cluster assemblyManual Assertion Based On ExperimentTAS:UniProtKB
Negative regulation of iron ion import across plasma membraneManual Assertion Based On ExperimentIMP:ARUK-UCL
Positive regulation of aconitate hydratase activityManual Assertion Based On ExperimentIMP:ARUK-UCL
Positive regulation of mitochondrial electron transport, NADH to ubiquinoneManual Assertion Based On ExperimentIMP:ARUK-UCL

Cellular Location

Isoform 1: Mitochondrion
Isoform 2: Cytoplasm; Nucleus

Involvement in disease

Myopathy with exercise intolerance Swedish type (MEIS):
Autosomal recessive metabolic disease characterized by lifelong severe exercise intolerance, in which minor exertion causes fatigue of active muscles, shortness of breath, and cardiac palpitations in association with lactic acidosis. The biochemical phenotype is characterized by a deficiency in mitochondrial iron-sulfur proteins and impaired muscle oxidative metabolism.

Du, J., Huang, Z., Li, Y., Ren, X., Zhou, C., Liu, R., ... & Tan, G. (2023). Copper exerts cytotoxicity through inhibition of iron-sulfur cluster biogenesis on ISCA1/ISCA2/ISCU assembly proteins. Free Radical Biology and Medicine, 204, 359-373.

Bonomi, F., Iametti, S., & Barbiroli, A. (2022). Protein interactions in the biological assembly of iron–sulfur clusters in Escherichia coli: Molecular and mechanistic aspects of the earliest assembly steps. IUBMB life, 74(7), 723-732.

Perfitt, T. L., & Martelli, A. (2022). Mitochondrial De Novo Assembly of Iron–Sulfur Clusters in Mammals: Complex Matters in a Complex That Matters. Inorganics, 10(3), 31.

Lin, C. W., McCabe, J. W., Russell, D. H., & Barondeau, D. P. (2020). Molecular mechanism of ISC iron–sulfur cluster biogenesis revealed by high-resolution native mass spectrometry. Journal of the American Chemical Society, 142(13), 6018-6029.

Srour, B., Gervason, S., Monfort, B., & D’Autréaux, B. (2020). Mechanism of iron–sulfur cluster assembly: In the intimacy of iron and sulfur encounter. Inorganics, 8(10), 55.

Tanaka, N., Yuda, E., Fujishiro, T., Hirabayashi, K., Wada, K., & Takahashi, Y. (2019). Identification of IscU residues critical for de novo iron–sulfur cluster assembly. Molecular Microbiology, 112(6), 1769-1783.

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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

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

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