HSPA8/HSC71/Hsc70 Antibody (3377C) [Unconjugated] Summary
| Additional Information |
Recombinant Monoclonal Antibody. |
| Immunogen |
E. coli-derived recombinant human HSPA8 Asp534-Gly615 Accession # P11142 |
| Specificity |
Detects recombinant human HSPA8 in Direct ELISA. |
| Source |
N/A |
| Isotype |
IgG |
| Clonality |
Monoclonal |
| Host |
Rabbit |
| Purity Statement |
Protein A or G purified from hybridoma culture supernatant |
| Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Packaging, Storage & Formulations
| Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. - 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
|
| Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| Reconstitution Instructions |
Reconstitute lyophilized material at 0.2 mg/ml in sterile PBS. For liquid material, refer to CoA for concentration. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for HSPA8/HSC71/Hsc70 Antibody (3377C) [Unconjugated]
Background
Heat
shock cognate 71-kDa protein (HSPA8), also referred to as HSC70, is a member of
the heat shock protein 70 (HSP70) family, with a molecular weight of
approximately 71 kDa. HSPA8 is an ATP-dependent molecular chaperone
ubiquitously expressed in eukaryotic cells and plays a critical role in protein
homeostasis. It facilitates the folding of nascent polypeptides, the assembly
and disassembly of protein complexes, and the translocation of proteins across
membranes. Additionally, HSPA8 is involved in the targeting and degradation of
misfolded or damaged proteins via the ubiquitin-proteasome pathway and
lysosomal-associated degradation. Beyond its canonical chaperone functions,
HSPA8 participates in cellular processes such as autophagy, stress response,
and clathrin-mediated endocytosis. Dysregulation of HSPA8 expression or
activity has been implicated in various pathological conditions, including
neurodegenerative disorders such as Alzheimer's and Parkinson's diseases, where
aberrant protein aggregation is a hallmark feature. The multifunctionality and
essential cellular roles of HSPA8 underscore its utility as both a biomarker
and a potential therapeutic target in a range of diseases.
- Hartl FU, Hayer-Hartl M. Molecular chaperones in the cytosol: from
nascent chain to folded protein. Science. 2002 Mar 8;295(5561):1852-8. doi:
10.1126/science.1068408. PMID: 11884745.
- Kampinga HH, Craig EA. The
HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat
Rev Mol Cell Biol. 2010 Aug;11(8):579-92. doi: 10.1038/nrm2941. Erratum in: Nat
Rev Mol Cell Biol. 2010 Oct;11(10):750. PMID: 20651708; PMCID: PMC3003299.
- Pustovaya K, Venediktov A,
Soldatov V, Kuzmin E, Pokidova K, Gartzeva V, Payushina O, Tsytsarev V,
Meglinski I and Piavchenko G (2026) Recent insights into HSP70: proteostasis
and beyond. Front. Mol. Biosci. 13:1791536. doi: 10.3389/fmolb.2026.1791536.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are
guaranteed for 1 year from date of receipt.
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