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Anti-Hsc70 Picoband Antibody

     
  • WB - Anti-Hsc70 Picoband Antibody ABO12327
    Anti- Hsc70 Picoband antibody, ABO12327, Western blottingAll lanes: Anti Hsc70 (ABO12327) at 0.5ug/mlLane 1: Rat Liver Tissue Lysate at 50ugLane 2: Rat Thymus Tissue Lysate at 50ugLane 3: Rat Testis Tissue Lysate at 50ugLane 4: Mouse Liver Tissue Lysate at 50ugLane 5: Mouse Thymus Tissue Lysate at 50ugLane 6: Mouse Testis Tissue Lysate at 50ugLane 7: HELA Whole Cell Lysate at 40ugLane 8: MCF-7 Whole Cell Lysate at 40ugLane 9: 293T Whole Cell Lysate at 40ugPredicted bind size: 71KDObserved bind size: 71KD
  • IHC - Anti-Hsc70 Picoband Antibody ABO12327
    Anti- Hsc70 Picoband antibody, ABO12327,IHC(P)IHC(P): Mouse Kidney Tissue
  • IHC - Anti-Hsc70 Picoband Antibody ABO12327
    Anti- Hsc70 Picoband antibody, ABO12327,IHC(P)IHC(P): Rat Kidney Tissue
  • IHC - Anti-Hsc70 Picoband Antibody ABO12327
    Anti- Hsc70 Picoband antibody, ABO12327,IHC(P)IHC(P): Human Mammary Cancer Tissue
  • SPECIFICATION
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
WB, IHC-P
Primary Accession P11142
Host Rabbit
Reactivity Human, Mouse, Rat
Clonality Polyclonal
Format Lyophilized
Description Rabbit IgG polyclonal antibody for Heat shock cognate 71 kDa protein(HSPA8) detection. Tested with WB, IHC-P in Human;Mouse;Rat.
Reconstitution Add 0.2ml of distilled water will yield a concentration of 500ug/ml.
Additional Information
Gene ID 3312
Other Names Heat shock cognate 71 kDa protein, Heat shock 70 kDa protein 8, Lipopolysaccharide-associated protein 1, LAP-1, LPS-associated protein 1, HSPA8, HSC70, HSP73, HSPA10
Calculated MW 70898 MW KDa
Application Details Immunohistochemistry(Paraffin-embedded Section), 0.5-1 µg/ml, Human, Mouse, Rat, By Heat

Western blot, 0.1-0.5 µg/ml, Human, Mouse, Rat
Subcellular Localization Cytoplasm. Melanosome. Nucleus, nucleolus. Cell membrane. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock.
Tissue Specificity Ubiquitous. .
Protein Name Heat shock cognate 71 kDa protein
Contents Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.
Immunogen E.coli-derived human Hsc70 recombinant protein (Position: Q520-A614). Human Hsc70 shares 98.9% amino acid (aa) sequence identity with both mouse and rat Hsc70.
Purification Immunogen affinity purified.
Cross Reactivity No cross reactivity with other proteins
Storage At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing.
Protein Information
Name HSPA8
Synonyms HSC70, HSP73, HSPA10
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, 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 (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). 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:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). 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:24318877, PubMed:27474739, PubMed:24121476, PubMed:26865365). 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). 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).
Cellular Location Cytoplasm. Melanosome. Nucleus, nucleolus. Cell membrane. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock
Tissue Location Ubiquitous..
Research Areas
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Background

HSPA8 (heat shock 70kDa protein 8) also known as HSC70, HSC71, HSP73, HSPA10, FORMERLY, LAP1 or LPS-ASSOCIATED PROTEIN 1, is a heat shock protein that in humans is encoded by the HSPA8 gene. The HSPA8 gene contains 9 exons and spans 5 kb. The deduced HSPA8 protein has 646 amino acids and a predicted molecular mass of 70,899 Da. And the HSPA8 gene is mapped on 11q24.1. HSPA8 plays an important role in cells by transiently associating with nascent polypeptides to facilitate correct folding. HSP73 also functions as an ATPase in the disassembly of clathrin-coated vesicles during transport of membrane components through the cell. Rapid decay involves AU-rich binding protein AUF1, which complexes with heat-shock proteins HSC70 and HSP70, translation initiation factor EIF4G, and poly (A)-binding protein. In the absence of Il3, Hsc70 formed a complex with Hsp40 and Hip, and this complex, in association with Eif4g and Pabp, formed a high-stability complex with Bim mRNA that protected it from ribonucleases.

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$ 280.00
Cat# ABO12327
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