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>   home   >   Products   >   Primary Antibodies   >   Signal Transduction   >   Hsc70 Antibody   

Hsc70 Antibody

Rabbit Polyclonal Antibody

     
  • WB - Hsc70 Antibody ABV10072-30
    Western blot analysis of Hsc70 expression in Jurkat cell lysate (Lane 1) and mouse small intestine tissue lysate (Lane 2).
  • SPECIFICATION
  • CITATIONS
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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
Primary Accession P11142
Reactivity Human, Mouse, Rat, Rabbit, Hamster, Monkey, Bovine
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 70898 Da
Additional Information
Gene ID 3312
Application & Usage Western blot analysis (0.5-4 µg/ml) and in Immunohistochemistry. However, the optimal conditions should be determined individually. The antibody detects a 71 kDa Hsc70. A ~40 kDa band can also be detected in human samples. Jurkat cell lysate and mouse small intestine lysate can be used as positive controls.
Other Names HSPA8, LAP1, HSC54, HSC70, HSC71, HSP71, HSP73, HSPA10, MGC131511, MGC29929, NIP71
Target/Specificity Hsp70
Antibody Form Liquid
Appearance Colorless liquid
Formulation 100 µg (0.5 mg/ml) affinity purified rabbit anti-Hsc70 polyclonal antibody in phosphate buffered saline (PBS), pH 7.2, containing 30% glycerol, 0.5% BSA, 0.01% thimerosal.
Handling The antibody solution should be gently mixed before use.
Reconstitution & Storage -20 °C
Background Descriptions
PrecautionsHsc70 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
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
Citations (0)

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Background

The 70 kDa heat shock cognate protein, Hsc70, is part of the Hsp70 family. The family includes both cognate members and highly inducible isoforms. Members of the Hsp70 family are molecular chaperones which are involved in many cellular functions such as protein folding, transport, maturation and degradation.

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$ 89.00
$ 265.00
Cat# ABV10072-30
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