Hsc70 Antikörper
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- Target Alle Hsc70 (HSPA8) Antikörper anzeigen
- Hsc70 (HSPA8) (Heat Shock 70kDa Protein 8 (HSPA8))
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Reaktivität
- Human
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Wirt
- Maus
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Klonalität
- Monoklonal
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Konjugat
- Dieser Hsc70 Antikörper ist unkonjugiert
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Applikation
- Western Blotting (WB), Immunohistochemistry (IHC), ELISA, Immunoprecipitation (IP), Immunocytochemistry (ICC), Immunofluorescence (IF), Binding Studies (Bind), Proximity Ligation Assay (PLA), Antibody Array (AA)
- Spezifität
- Detects ~73 kDa. Does not cross react with HSP70.
- Kreuzreaktivität
- Human, Maus, Ratte
- Aufreinigung
- Protein G Purified
- Immunogen
- Full length human HSC70
- Klon
- 1F2-H5
- Isotyp
- IgG2a kappa
- Top Product
- Discover our top product HSPA8 Primärantikörper
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- Applikationshinweise
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- WB (1:1000)
- ICC/IF (1:100)
- optimal dilutions for assays should be determined by the user.
- Kommentare
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1 μg/ml of ABIN361800 was sufficient for detection of HSC70 in 10 μg of HeLa lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
- Beschränkungen
- Nur für Forschungszwecke einsetzbar
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- Format
- Liquid
- Konzentration
- 1 mg/mL
- Buffer
- PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide, Storage buffer may change when conjugated
- Konservierungsmittel
- Sodium azide
- Vorsichtsmaßnahmen
- This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
- Lagerung
- -20 °C
- Informationen zur Lagerung
- -20°C
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Heat shock protein 70 regulates degradation of the mumps virus phosphoprotein via the ubiquitin-proteasome pathway." in: Journal of virology, Vol. 89, Issue 6, pp. 3188-99, (2015) (PubMed).
: "Characterization of cysteine string protein in rat parotid acinar cells." in: Archives of biochemistry and biophysics, Vol. 538, Issue 1, pp. 1-5, (2013) (PubMed).
: "The DNAJA2 substrate release mechanism is essential for chaperone-mediated folding." in: The Journal of biological chemistry, Vol. 287, Issue 50, pp. 41939-54, (2012) (PubMed).
: "Responses of HSC70 expression in diencephalon to iron deficiency anemia in rats." in: The journal of physiological sciences : JPS, Vol. 61, Issue 6, pp. 445-56, (2011) (PubMed).
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Heat shock protein 70 regulates degradation of the mumps virus phosphoprotein via the ubiquitin-proteasome pathway." in: Journal of virology, Vol. 89, Issue 6, pp. 3188-99, (2015) (PubMed).
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- Target
- Hsc70 (HSPA8) (Heat Shock 70kDa Protein 8 (HSPA8))
- Andere Bezeichnung
- HSC70 (HSP73) (HSPA8 Produkte)
- Synonyme
- hsc54 antikoerper, hsc70 antikoerper, hsc71 antikoerper, hsp71 antikoerper, hsp73 antikoerper, hspa10 antikoerper, lap1 antikoerper, nip71 antikoerper, HSC54 antikoerper, HSC70 antikoerper, HSC71 antikoerper, HSP71 antikoerper, HSP73 antikoerper, HSPA10 antikoerper, LAP1 antikoerper, NIP71 antikoerper, Hsc70 antikoerper, 2410008N15Rik antikoerper, Hsc71 antikoerper, Hsc73 antikoerper, Hsp73 antikoerper, Hspa10 antikoerper, wu:fb01g06 antikoerper, wu:fi48b06 antikoerper, heat shock protein family A (Hsp70) member 8 L homeolog antikoerper, heat shock protein family A (Hsp70) member 8 antikoerper, heat shock 70kDa protein 8 antikoerper, heat shock protein 8 antikoerper, hspa8.L antikoerper, HSPA8 antikoerper, Hspa8 antikoerper, hspa8 antikoerper
- Hintergrund
- HSP70 genes encode abundant heat-inducible 70- kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50 % identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). When cells are subjected to metabolic stress (e.g., heat shock) a member of the HSP 70 family, HSP 70 (HSP72), is expressed, HSP 70 is highly related to HSC70 (>90 % sequence identity). Constitutively expressed HSC70 rapidly forms a stable complex with the highly inducible HSP70 in cells following heat shock. The interaction of HSC70 with HSP 70 is regulated by ATP. These two heat shock proteins move together in the cell experiencing stress. Furthermore, research on HSC70 has implicates it with a role in facilitating the recovery of centrosomal structure and function after heat shock (6).
- Gen-ID
- 3312
- NCBI Accession
- NP_006588
- UniProt
- P11142
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