Mouse Anti-HSCB Recombinant Antibody (CBFYH-1990) (CBMAB-H3001-FY)

Name: Mouse Anti-HSCB Recombinant Antibody (CBFYH-1990)
SKU: CBMAB-H3001-FY
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

CBFYH-1990

Application

Specificity

Human

Antibody Isotype

IgG2a

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

Buffer

PBS, PH 7.3, 1% BSA, 50% glycerol

Preservative

0.02% Sodium azide

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

Hscb Mitochondrial Iron-Sulfur Cluster Cochaperone

Introduction

This gene encodes a DnaJ-type co-chaperone and member of the heat shock cognate B (HscB) family of proteins. The encoded protein plays a role in the synthesis of iron-sulfur clusters, protein cofactors that are involved in the redox reactions of mitochondrial electron transport and other processes. Cells in which this gene is knocked down exhibit reduced activity of iron-sulfur cluster-dependent enzymes including succinate dehydrogenase and aconitase. The encoded protein may stimulate the ATPase activity of the mitochondrial stress-70 protein. Alternative splicing results in multiple transcript variants.

Entrez Gene ID

150274

UniProt ID

Q8IWL3

Alternative Names

HscB Mitochondrial Iron-Sulfur Cluster Cochaperone; DnaJ (Hsp40) Homolog, Subfamily C, Member 20; DNAJC20; HSC20; Iron-Sulfur Cluster Co-Chaperone Protein HscB, Mitochondrial; HscB Iron-Sulfur Cluster Co-Chaperone Homolog (E. Coli)

Function

Acts as a co-chaperone in iron-sulfur cluster assembly in both mitochondria and the cytoplasm (PubMed:20668094, PubMed:29309586).

Required for incorporation of iron-sulfur clusters into SDHB, the iron-sulfur protein subunit of succinate dehydrogenase that is involved in complex II of the mitochondrial electron transport chain (PubMed:26749241).

Recruited to SDHB by interaction with SDHAF1 which first binds SDHB and then recruits the iron-sulfur transfer complex formed by HSC20, HSPA9 and ISCU through direct binding to HSC20 (PubMed:26749241).

Also mediates complex formation between components of the cytosolic iron-sulfur biogenesis pathway and the CIA targeting complex composed of CIAO1, DIPK1B/FAM69B and MMS19 by binding directly to the scaffold protein ISCU and to CIAO1 (PubMed:29309586).

This facilitates iron-sulfur cluster insertion into a number of cytoplasmic and nuclear proteins including POLD1, ELP3, DPYD and PPAT (PubMed:29309586).

Biological Process

[2Fe-2S] cluster assembly Source: GO_Central
Iron-sulfur cluster assembly Source: UniProtKB
Protein complex oligomerization Source: InterPro
Protein maturation by iron-sulfur cluster transfer Source: InterPro

Cellular Location

Iron-sulfur cluster co-chaperone protein HscB, cytoplasmic: Cytoplasm
Iron-sulfur cluster co-chaperone protein HscB, mitochondrial: Mitochondrion

Pedroletti, L., Moseler, A., & Meyer, A. J. (2023). Assembly, transfer, and fate of mitochondrial iron–sulfur clusters. Journal of Experimental Botany, 74(11), 3328-3344.

López-López, A., Keech, O., & Rouhier, N. (2022). Maturation and assembly of iron-Sulfur cluster-containing subunits in the mitochondrial Complex I from plants. Frontiers in Plant Science, 13, 916948.

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.

Crispin, A., Guo, C., Chen, C., Campagna, D. R., Schmidt, P. J., Lichtenstein, D., ... & Ducamp, S. (2020). Mutations in the iron-sulfur cluster biogenesis protein HSCB cause congenital sideroblastic anemia. The Journal of clinical investigation, 130(10), 5245-5256.

Kleczewska, M., Grabinska, A., Jelen, M., Stolarska, M., Schilke, B., Marszalek, J., ... & Dutkiewicz, R. (2020). Biochemical convergence of mitochondrial Hsp70 system specialized in iron–sulfur cluster biogenesis. International Journal of Molecular Sciences, 21(9), 3326.

Maio, N., Jain, A., & Rouault, T. A. (2020). Mammalian iron–sulfur cluster biogenesis: recent insights into the roles of frataxin, acyl carrier protein and ATPase-mediated transfer to recipient proteins. Current opinion in chemical biology, 55, 34-44.

Dutkiewicz, R., & Nowak, M. (2018). Molecular chaperones involved in mitochondrial iron–sulfur protein biogenesis. JBIC Journal of Biological Inorganic Chemistry, 23, 569-579.

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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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