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HSC70 is a molecular chaperone protein that plays a crucial role in protein folding and homeostasis. It is a member of the heat shock protein 70 (Hsp70) family and is involved in the proper folding, assembly, and transport of a wide range of client proteins within the cell.

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Lab products found in correlation

Pierce bca protein assay kit, by Thermo Fisher Scientific (4 mentions) Anti tubulin, by Cell Signaling Technology (2 mentions) Anti sirt1, by Cell Signaling Technology (2 mentions) Minute total protein extraction kit for adipose tissues, by Invent Biotechnologies (2 mentions) Anti translin, by Thermo Fisher Scientific (2 mentions) Anti trax, by Thermo Fisher Scientific (2 mentions) Ripa buffer, by Cell Signaling Technology (2 mentions) Protease and phosphatase inhibitor, by Merck Group (2 mentions) Anti lc3 clone 2g6, by Nanotools (2 mentions) Anti gm130, by BD (2 mentions) Anti β actin mab, by Merck Group (2 mentions) Nucleoporin p62, by BD (2 mentions) Bcl 2, by Cell Signaling Technology (2 mentions) Anti cd9, by Abcam (2 mentions) Rapamycin rapa, by LC Laboratories (1 mentions) Anti tsg101, by Santa Cruz Biotechnology (1 mentions) Anti flotillin 1, by BD (1 mentions) Atg5 clone 7c6, by Nanotools (1 mentions) Lipofectamine ltx transfection reagent, by Thermo Fisher Scientific (1 mentions) Pefabloc inhibitor, by Roche (1 mentions)

4 protocols using hsc70

1

Liver Protein Extraction and Immunoblotting

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Liver samples were rinsed with PBS and homogenized with RIPA buffer (Cell Signaling Technology, Danvers, MA) containing protease and phosphatase inhibitors (MilliporeSigma, Burlington, MA). Total protein was extracted from eWAT using the Minute Total Protein Extraction Kit for Adipose Tissues (Invent Biotechnologies, Plymouth, MN). Protein concentration was determined using the Pierce BCA Protein Assay Kit (Thermo Fisher Scientific, Waltham, MA). Equal amounts of total protein were separated by an SDS-PAGE gel, transferred to a PVDF membrane and immunoblotted with antibodies: Anti-SIRT1, anti-tubulin (#9475T and #2148, Cell Signaling Technology), anti-translin and anti-trax (generated in our laboratory, [13 (link)]) and HSC70 (#PA529221, Thermo Fisher Scientific). Blots were developed with the ECL system. Band intensities were quantified from digital images, by densitometry, using ImageJ.
Shah A.P., Johnson M.D., Fu X., Boersma G.J., Shah M., Wolfgang M.J., Tamashiro K.L, & Baraban J.M. (2019). Deletion of translin (Tsn) induces robust adiposity and hepatic steatosis without impairing glucose tolerance. International journal of obesity (2005), 44(1), 254-266.
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2

Liver Protein Extraction and Immunoblotting

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Liver samples were rinsed with PBS and homogenized with RIPA buffer (Cell Signaling Technology, Danvers, MA) containing protease and phosphatase inhibitors (MilliporeSigma, Burlington, MA). Total protein was extracted from eWAT using the Minute Total Protein Extraction Kit for Adipose Tissues (Invent Biotechnologies, Plymouth, MN). Protein concentration was determined using the Pierce BCA Protein Assay Kit (Thermo Fisher Scientific, Waltham, MA). Equal amounts of total protein were separated by an SDS-PAGE gel, transferred to a PVDF membrane and immunoblotted with antibodies: Anti-SIRT1, anti-tubulin (#9475T and #2148, Cell Signaling Technology), anti-translin and anti-trax (generated in our laboratory, [13 (link)]) and HSC70 (#PA529221, Thermo Fisher Scientific). Blots were developed with the ECL system. Band intensities were quantified from digital images, by densitometry, using ImageJ.
Shah A.P., Johnson M.D., Fu X., Boersma G.J., Shah M., Wolfgang M.J., Tamashiro K.L, & Baraban J.M. (2019). Deletion of translin (Tsn) induces robust adiposity and hepatic steatosis without impairing glucose tolerance. International journal of obesity (2005), 44(1), 254-266.
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3

Subcellular Protein Profiling Protocol

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All the reagents and chemicals were obtained from Sigma–Aldrich, unless otherwise indicated. Lipo-polysaccharide (LPS) (L2800), chloroquine diphosphate (CQ) (C6628) & Rapamycin (RAPA) was obtained from LC laboratories (R-5000). Sources of the antibodies were as follows: HSC70 (Thermo Scientific, PA5-27,337), anti-CD9 (Abcam, ab92726), Bcl2 (Cell Signaling, D17C4), nucleoporin P62 (BD Transduction Laboratories, 610,497), anti-GM130 (BD Transduction Laboratories, 610,822), anti-β-actin mAb (Sigma–Aldrich, A5441), anti-LC3 (clone 2G6) (NanoTools, 0260-100).
Atya H.B., Sharaf N.M., Abdelghany R.M., El-Helaly S.N, & Taha H. (2024). Autophagy and exosomes; inter-connected maestros in Alzheimer’s disease. Inflammopharmacology, 32(3), 2061-2073.
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4

Exosome Isolation and Characterization

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Unless otherwise indicated, all the reagents and chemical were obtained from Sigma–Aldrich. Proteinase K (PK; 03115879001) and Pefabloc inhibitor (11286700) were from Roche. Lipofectamine 2000 (Invitrogen, 1166807), Lipofectamine LTX transfection reagents (Invitrogen, 15338100), and On Target plus mouse Atg5 (11793) siRNA Smart Pool (GE Health Care, L-064838-00-0005) were acquired from the manufacturers indicated in parentheses.
Sources of the antibodies were as follows: anti-flotillin-1 (BD Transduction Laboratories, 610820), anti-Tsg101 (Santa Cruz Biotechnology, sc-7964), HSC70 (Thermo Scientific, PA5-27337), CD63 (Santa Cruz Biotechnology, SC-15363), Alix (Cell Signaling, 2171), anti-CD9 (Abcam, ab92726), Bcl2 (Cell Signaling, D17C4), Atg-5 (clone 7C6) (NanoTools, 0262-100), nucleoporin P62 (BD Transduction Laboratories, 610497), anti-GM130 (BD Transduction Laboratories, 610822), anti-β-actin mAb (Sigma–Aldrich, A5441), anti-LC3 (clone 2G6) (NanoTools, 0260-100), anti-PrP mAb 4H11 has been previously described (52 (link)). Peroxidase-conjugated Igs were from Jackson Immunoresearch Lab (goat anti-mouse HRP, 115-035-003; and goat anti-rabbit HRP, 111-035-45).
Abdulrahman B.A., Abdelaziz D.H, & Schatzl H.M. (2018). Autophagy regulates exosomal release of prions in neuronal cells. The Journal of Biological Chemistry, 293(23), 8956-8968.
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