| Weight | 1 lbs |
|---|---|
| Dimensions | 9 × 5 × 2 in |
| host | mouse |
| isotype | Rabbit IgG |
| clonality | monoclonal |
| concentration | concentrate, predilute |
| applications | IHC |
| reactivity | human |
| available size | 0.1 mL, 0.5 mL, 1 mL concentrated, 7 mL prediluted |
rabbit anti-HSP70 monoclonal antibody (ZR152) 6217
Price range: $160.00 through $528.00
Antibody summary
- Rabbit monoclonal to HSP70
- Suitable for: Immunohistochemistry (formalin-fixed, paraffin-embedded tissues)
- Reacts with: Human
- Isotype:Rabbit IgG
- Control: Hepatocellular carcinoma
- Visualization: Nuclear and cytoplasmic
- 0.1, 0.5, 1.0 mL concentrated, 7 mL prediluted
rabbit anti-HSP70 monoclonal antibody ZR152 6217
| target relevance |
|---|
| Homo sapiens HSPA8 Heat shock cognate 71 kDa protein |
| Protein names Heat shock cognate 71 kDa protein |
| Alternative names Heat shock 70 kDa protein 8, Heat shock protein family A member 8, Lipopolysaccharide-associated protein 1 |
| Gene names HSPA8 |
| Protein family Belongs to the heat shock protein 70 family |
| Function Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins, formation and dissociation of protein complexes, and antigen presentation. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation (PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661, PubMed:2799391, PubMed:36586411). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:12526792, PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661). The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation (PubMed:12526792, PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661). The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24121476, PubMed:24318877, PubMed:26865365, PubMed:27474739). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:10722728, PubMed:11276205). Substrate recognition component in chaperone-mediated autophagy (CMA), a selective protein degradation process that mediates degradation of proteins with a -KFERQ motif: HSPA8/HSC70 specifically recognizes and binds cytosolic proteins bearing a -KFERQ motif and promotes their recruitment to the surface of the lysosome where they bind to lysosomal protein LAMP2 (PubMed:11559757, PubMed:2799391, PubMed:36586411). KFERQ motif-containing proteins are eventually transported into the lysosomal lumen where they are degraded (PubMed:11559757, PubMed:2799391, PubMed:36586411). In conjunction with LAMP2, facilitates MHC class II presentation of cytoplasmic antigens by guiding antigens to the lysosomal membrane for interaction with LAMP2 which then elicits MHC class II presentation of peptides to the cell membrane (PubMed:15894275). Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 (PubMed:23990462). It is recruited to clathrin-coated vesicles through its interaction with DNAJC6 leading to activation of HSPA8/HSC70 ATPase activity and therefore uncoating of clathrin-coated vesicles (By similarity) |
| Catalytic activity ATP + H2O = ADP + phosphate + H(+) |
| Subcellular location Cytoplasm, Melanosome, Nucleus, nucleolus, Cell membrane, Lysosome membrane |
| Structure (Microbial infection) Interacts with human herpes virus 1 (HHV-1) transcriptional regulator ICP22; this interaction recruits HSPA8/HSP40 to discrete nuclear foci |
| Post-translational modification Acetylated ISGylated Trimethylation at Lys-561 reduces fibrillar SNCA binding |
| Keywords 3D-structure, Acetylation, Alternative splicing, ATP-binding, Autophagy, Cell membrane, Chaperone, Cytoplasm, Direct protein sequencing, Host-virus interaction, Hydrolase, Isopeptide bond, Lysosome, Membrane, Methylation, mRNA processing, mRNA splicing, Nucleotide-binding, Nucleus, Phosphoprotein, Proteomics identification, Reference proteome, Repressor, Spliceosome, Stress response, Transcription, Transcription regulation, Ubl conjugation |
| Sequence MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVA MNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVS SMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAA IAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNH FIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRA RFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELN KSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTI PTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDI DANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKN SLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELE KVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD |
| UniProt accession: P11142 |
Data
 |
| Formalin-fixed, paraffin-embedded human hepatocellular carcinoma stained with anti-HSP70 using peroxidase-conjugate and DAB chromogen. Note cell cytoplasmic staining of tumor cells |
FAQ & Publications
Frequently Asked Questions
What species does the rabbit anti-HSP70 monoclonal antibody (ZR152) specifically react with?
The rabbit anti-HSP70 monoclonal antibody (ZR152) is reactive with human species.
What are the recommended storage conditions for the rabbit anti-HSP70 monoclonal antibody (ZR152) to maintain its stability?
For short term storage, keep the antibody at 2-8°C. For longer term storage, it should be kept at -20°C, and freeze/thaw cycles should be avoided to preserve antibody integrity.
Publications
| pmid | title | authors | citation |
|---|---|---|---|
| We haven't added any publications to our database yet. | |||
Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from the PubMed database provided by the United States National Library of Medicine at the National Institutes of Health.
Protocols
| relevant to this product |
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| IHC |
Documents
| Batch Number | QC File | SDS |
|---|---|---|
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