Recombinant Human Iron-sulfur cluster co-chaperone protein HscB, mitochondrial (HSCB)

Code CSB-YP816893HU
MSDS
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Source Yeast
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Code CSB-EP816893HU
MSDS
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Source E.coli
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Code CSB-EP816893HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP816893HU
MSDS
Size Pls inquire
Source Baculovirus
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Code CSB-MP816893HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
HSCB
Uniprot No.
Alternative Names
AI325508; AW049829; dJ366L4.2; DnaJ (Hsp40) homolog, subfamily C member 20; DnaJ homolog subfamily C member 20; DNAJC20; Hsc20; HSC20_HUMAN; hscB; HscB iron sulfur cluster co chaperone homolog; Iron sulfur cluster co chaperone protein HscB mitochondrial; Iron-sulfur cluster co-chaperone protein HscB; J type co chaperone HSC20; JAC1; mitochondrial; RGD1311005; RP3-366L4.2
Species
Homo sapiens (Human)
Expression Region
30-235
Target Protein Sequence
A ASQAGSNYPR CWNCGGPWGP GREDRFFCPQ CRALQAPDPT RDYFSLMDCN RSFRVDTAKL QHRYQQLQRL VHPDFFSQRS QTEKDFSEKH STLVNDAYKT LLAPLSRGLY LLKLHGIEIP ERTDYEMDRQ FLIEIMEINE KLAEAESEAA MKEIESIVKA KQKEFTDNVS SAFEQDDFEE AKEILTKMRY FSNIEEKIKL KKIPL
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Acts as a co-chaperone in iron-sulfur cluster assembly in both mitochondria and the cytoplasm. 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. 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. 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. This facilitates iron-sulfur cluster insertion into a number of cytoplasmic and nuclear proteins including POLD1, ELP3, DPYD and PPAT.
Gene References into Functions
  1. Nfu is shown to bind to both chaperone proteins with binding affinities similar to those observed for IscU binding to the homologous HSPA9 and Hsc20, while Nfu can also stimulate the ATPase activity of HSPA9 PMID: 29211945
  2. The delivery of assembled Fe-S clusters to recipient proteins is a crucial step in the biogenesis of Fe-S proteins; review focuses on recent insights into the molecular mechanism of amino acid motif recognition and discrimination by the co-chaperone HSC20 and finds co-chaperone HSC20 binds to LYR motifs present in Fe-S recipient proteins or their binding partners. [Review] PMID: 27714045
  3. the crucial role of HSC20 in the assembly of the mitochondrial respiratory chain, is reported. PMID: 28380382
  4. NFS1 binds preferentially to the D-state of ISCU while mtHSP70 binds preferentially to the D-state of ISCU and HSC20 binds preferentially to the S-state of ISCU. PMID: 23940031
  5. A cysteine-rich N-terminal domain, which clearly distinguishes hHSC20 from the specialized DnaJ type III proteins of fungi and most bacteria, was found to be important for the integrity and function of the human co-chaperone. PMID: 20668094
  6. structural analysis of human J-type co-chaperone HscB reveals a tetracysteine metal-binding domain PMID: 18713742

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Subcellular Location
[Iron-sulfur cluster co-chaperone protein HscB, cytoplasmic]: Cytoplasm.; [Iron-sulfur cluster co-chaperone protein HscB, mitochondrial]: Mitochondrion.
Protein Families
HscB family
Tissue Specificity
Expressed in lung, brain, stomach, spleen, ovary, testis, liver, muscle and heart.
Database Links

HGNC: 28913

OMIM: 608142

KEGG: hsa:150274

STRING: 9606.ENSP00000216027

UniGene: Hs.632780

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