Recombinant human Hsc70 protein (ab78431)
Key features and details
- Expression system: Escherichia coli
- Purity: > 90% Affinity purified
- Active: Yes
- Tags: His tag N-Terminus
- Suitable for: WB, ELISA, Functional Studies, Competitive Binding Assays, SDS-PAGE
Description
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Product name
Recombinant human Hsc70 protein
See all Hsc70 proteins and peptides -
Biological activity
ab78431 has ATPase activity at the time of manufacture of 3.2 µM phosphate liberated/hr/µg protein in a 200 µl reaction at 37°C (pH 8) in the presence of 20 µl of 1 mM ATP using a Malachite Green assay.
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Purity
> 90 % Affinity purified.
ab78431 is affinity purified. -
Expression system
Escherichia coli -
Accession
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Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Predicted molecular weight
73 kDa including tags -
Amino acids
1 to 646 -
Tags
His tag N-Terminus -
Additional sequence information
His tag
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab78431 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
Western blot
ELISA
Functional Studies
Competitive Binding Assays
SDS-PAGE
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Form
Liquid -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Store at -20°C. Stable for 12 months at -20°C.
pH: 8
Constituents: 1.753% Sodium chloride, 0.788% Tris HClThis product is an active protein and may elicit a biological response in vivo, handle with caution.
General Info
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Alternative names
- 2410008N15Rik
- Constitutive heat shock protein 70
- Epididymis luminal protein 33
see all -
Function
Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Isoform 2 may function as an endogenous inhibitory regulator of HSC70 by competing the co-chaperones. -
Tissue specificity
Ubiquitous. -
Sequence similarities
Belongs to the heat shock protein 70 family. -
Domain
The N-terminal 1-386 residues constitute the ATPase domain, while residues 387-646 form the peptide-binding domain. -
Post-translational
modificationsPhosphorylated upon DNA damage, probably by ATM or ATR.
ISGylated. -
Cellular localization
Cytoplasm. Melanosome. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. - Information by UniProt
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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SDS download
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Datasheet download
References (5)
ab78431 has been referenced in 5 publications.
- Endicott SJ et al. Long-lived mice with reduced growth hormone signaling have a constitutive upregulation of hepatic chaperone-mediated autophagy. Autophagy 17:612-625 (2021). PubMed: 32013718
- Xu X et al. Metformin activates chaperone-mediated autophagy and improves disease pathologies in an Alzheimer disease mouse model. Protein Cell 12:769-787 (2021). PubMed: 34291435
- Fan Y et al. Acetylation-dependent regulation of TPD52 isoform 1 modulates chaperone-mediated autophagy in prostate cancer. Autophagy 17:4386-4400 (2021). PubMed: 34034634
- Endicott SJ et al. Inhibition of class I PI3K enhances chaperone-mediated autophagy. J Cell Biol 219:N/A (2020). PubMed: 33048163
- Labrador-Garrido A et al. Chaperome screening leads to identification of Grp94/Gp96 and FKBP4/52 as modulators of the a-synuclein-elicited immune response. FASEB J 30:564-77 (2016). PubMed: 26443817