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
Restrictions
For Research Use only
Buffer
0.5 mg/mL if reconstituted with 0.2 mL sterile DI water
Stock
-20 °C
Stockage commentaire
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.
Antigène
Hsc70 (HSPA8)
(Heat Shock 70kDa Protein 8 (HSPA8))
anticorps hsc54, anticorps hsc70, anticorps hsc71, anticorps hsp71, anticorps hsp73, anticorps hspa10, anticorps lap1, anticorps nip71, anticorps HSC54, anticorps HSC70, anticorps HSC71, anticorps HSP71, anticorps HSP73, anticorps HSPA10, anticorps LAP1, anticorps NIP71, anticorps Hsc70, anticorps 2410008N15Rik, anticorps Hsc71, anticorps Hsc73, anticorps Hsp73, anticorps Hspa10, anticorps wu:fb01g06, anticorps wu:fi48b06, anticorps heat shock protein family A (Hsp70) member 8 L homeolog, anticorps heat shock protein family A (Hsp70) member 8, anticorps heat shock 70kDa protein 8, anticorps heat shock protein 8, anticorps hspa8.L, anticorps HSPA8, anticorps Hspa8, anticorps hspa8
Sujet
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.