• Western blot analysis of extracts of various cell lines, using Hsc70/HSPA8 Rabbit monoclonal antibody (STJ11101237) at 1:1000 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (STJS000856) at 1:10000 dilution. Lysates/proteins: 25 Mu g per lane. Blocking buffer: 3% nonfat dry milk in TBST. Detection: ECL Basic Kit. Exposure time: 30s.

Anti-HSPA8 antibody (547-646) [S7MR] (STJ11101237)

SKU:
STJ11101237

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Host: Rabbit
Applications: WB
Reactivity: Human/Mouse/Rat
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Rabbit monoclonal antibody anti-Hsc70 (547-646) is suitable for use in Western Blot research applications.
Clonality: Monoclonal
Clone ID: S7MR
Conjugation: Unconjugated
Isotype: IgG
Formulation: PBS with 0.02% Sodium Azide, 0.05% BSA, 50% Glycerol, pH7.3.
Purification: Affinity purification
Dilution Range: WB 1:500-1:2000
Storage Instruction: Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles.
Gene Symbol: HSPA8
Gene ID: 3312
Uniprot ID: HSP7C_HUMAN
Immunogen Region: 547-646
Immunogen: A synthetic peptide corresponding to a sequence within amino acids 547-646 of human Hsc70/HSPA8 (P11142).
Immunogen Sequence: FNMKATVEDEKLQGKINDED KQKILDKCNEIINWLDKNQT AEKEEFEHQQKELEKVCNPI ITKLYQSAGGMPGGMPGGFP GGGAPPSGGASSGPTIEEVD
Tissue Specificity Ubiquitous.
Post Translational Modifications Acetylated. ISGylated. Trimethylation at Lys-561 reduces fibrillar SNCA binding.
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 and the formation and dissociation of protein complexes. 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. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. 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. 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. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. 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. 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. KFERQ motif-containing proteins are eventually transported into the lysosomal lumen where they are degraded. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1. Interacts with VGF-derived peptide TLQP-21.
Protein Name Heat Shock Cognate 71 Kda Protein
Heat Shock 70 Kda Protein 8
Lipopolysaccharide-Associated Protein 1
Lap-1
Lps-Associated Protein 1
Database Links Reactome: R-HSA-3371453
Reactome: R-HSA-3371497
Reactome: R-HSA-3371568
Reactome: R-HSA-3371571
Reactome: R-HSA-432720
Reactome: R-HSA-432722
Reactome: R-HSA-447041
Reactome: R-HSA-450408
Reactome: R-HSA-6785807
Reactome: R-HSA-6798695
Reactome: R-HSA-72163
Reactome: R-HSA-8856828
Reactome: R-HSA-8876725
Reactome: R-HSA-888590
Reactome: R-HSA-9613354
Reactome: R-HSA-9613829
Reactome: R-HSA-9615710
Cellular Localisation Cytoplasm
Melanosome
Nucleus
Nucleolus
Cell Membrane
Lysosome Membrane
Peripheral Membrane Protein
Cytoplasmic Side
Localized In Cytoplasmic Mrnp Granules Containing Untranslated Mrnas
Translocates Rapidly From The Cytoplasm To The Nuclei
And Especially To The Nucleoli
Upon Heat Shock
Alternative Antibody Names Anti-Heat Shock Cognate 71 Kda Protein antibody
Anti-Heat Shock 70 Kda Protein 8 antibody
Anti-Lipopolysaccharide-Associated Protein 1 antibody
Anti-Lap-1 antibody
Anti-Lps-Associated Protein 1 antibody
Anti-HSPA8 antibody
Anti-HSC70 antibody
Anti-HSP73 antibody
Anti-HSPA10 antibody

Information sourced from Uniprot.org

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