An amino acid sequence from the N-terminus of human Hsc70 (TTYSCVGVFQHGKVEIIAN) was used as the immunogen for this Hsc70 antibody (100% homologous in human, mouse and rat).
The stated application concentrations are suggested starting amounts. Titration of the Hsc70 antibody may be required due to differences in protocols and secondary/substrate sensitivity.\. Western blot: 0.5-1 μg/mL,IHC (Paraffin): 0.5-1 μg/mL,IHC (Frozen): 0.5-1 μg/mL,Immunocytochemistry: 0.5-1 μg/mL
Beschränkungen
Nur für Forschungszwecke einsetzbar
Buffer
0.5 mg/mL if reconstituted with 0.2 mL sterile DI water
Lagerung
-20 °C
Informationen zur Lagerung
After reconstitution, the Hsc70 antibody can be stored for up to one month at 4°C. For long-term, aliquot and store at -20°C. Avoid repeated freezing and thawing.
Target
Hsc70 (HSPA8)
(Heat Shock 70kDa Protein 8 (HSPA8))
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
The 70 kilodalton heat shock proteins(Hsp70s) are a family of ubiquitously expressed heat shock proteins. The Hsp70s are an important part of the cell's machinery for protein folding, and help to protect cells from stress. All of the Hsp70 proteins have three major functional domains: An N-terminal ATPase domain binds ATP(Adenosine triphosphate) and hydrolyzes it to ADP(Adenosine diphosphate), A substrate binding domain contains a groove with an affinity for neutral, hydrophobic amino acid residues, A C-terminal domain rich in alpha helical structure acts as a 'lid' for the substrate binding domain. By binding tightly to partially-synthesized peptide sequences(incomplete proteins), Hsp70 prevents them from aggregating and being rendered nonfunctional. And it also can act to protect cells from thermal or oxidative stress. Finally, Hsp70 seems to be able to participate in disposal of damaged or defective proteins. Interaction with CHIP(Carboxyl-terminus of Hsp70 Interacting Protein)-an E3 ubiquitin ligase-allows Hsp70 to pass proteins to the cell's ubiquitination and proteolysis pathways.