|IP||1-4 μL/mg of lysate|
**********Please Note: Optimal concentrations/dilutions should be determined by the end user.**********
Anti-HSPA1A rabbit monoclonal antibody at 1:500 dilution
Lane A: A549 Whole Cell Lysate
Lane B: HCT116 Whole Cell Lysate
Lane C: Hela Whole Cell LysateLysates/proteins at 30 μg per lane.
Goat Anti-Rabbit IgG H&L (Dylight800) at 1/10000 dilution.Developed using the Odyssey technique.
Performed under reducing conditions.Predicted band size:70 kDa
Observed band size:70 kDa
(We are unsure as to the identity of these extra bands.)
HSPA1A was immunoprecipitated using:
Lane A:0.5 mg Hela Whole Cell Lysate2 µL anti-HSPA1A rabbit monoclonal antibody and 15 μl of 50 % Protein G agarose.Primary antibody:
Anti-HSPA1A rabbit monoclonal antibody,at 1:200 dilutionSecondary antibody:
Dylight 800-labeled antibody to rabbit IgG (H+L), at 1:5000 dilutionDeveloped using the odssey technique.
Performed under reducing conditions.Predicted band size: 70 kDa
Observed band size: 70 kDa
HSPA1A is a member of the Hsp70 protein family. The 70 kilodalton heat shock proteins (Hsp70s) are a family of ubiquitously expressed heat shock proteins. HSP are abundant and conserved proteins present in all cells. Upon temperature shock or other stress stimuli, HSP are synthesized intracellularly, which may protect cells from protein denaturation or from death. Extracellularly, HSP can serve a cytokine function to initiate both innate and adaptive immunity through activation of APC. HSP serves also a chaperone function and facilitates presentation of antigen peptide to T cells. Molecular chaperones of the Hsp70 family have diverse functions in cells. They assist the folding of newly synthesized and stress-denatured proteins, as well as the import of proteins into organelles, and the dissociation of aggregated proteins. The well-conserved Hsp70 chaperones are ATP dependent: binding and hydrolysis of ATP regulates their interactions with unfolded polypeptide substrates, and ATPase cycling is necessary for their function. All cellular functions of Hsp70 chaperones use the same mechanism of ATP-driven polypeptide binding and release.
|Product Description||Host||Clonality||Application||Catalog# (PDF)|
|Anti-HSP70 Antibody (FITC)||Rabbit||Monoclonal||FCM||11660-R001-F|