Product Datasheet  
HSPA1A Antibody  
Catalog Number: 32062  
Technical:tech@swbio.com  
Information:info@swbio.com  
Description  
  • host_species：  
  • Rabbit
  • Amount：  
  • 100μgμg
  • Swiss-Prot No.：  
  • Swiss-Prot:P08107
    NCBI Gene ID:3303
  • Form of Antibody：  
  • Supplied at 1.0mg/mL in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
  • Storage：  
  • Store at -20˚C
  • Immunogen：  
  • A synthetic peptide of human HSPA1A .
  • reactivity：  
  • Human,Mouse,Rat
  • appl_detail：  
  • WB 1:1000 - 1:3000
    IHC 1:50 - 1:200
    IF 1:50 - 1:200
  • other_names：  
  • HSP72; HSPA1; HSP70I; HSP70-1; HSP70-1A
  • Purification：  
  • Antibodies were purified by affinity purification using immunogen.
  • Specificity：  
  • The antibody detects endogenous level of total HSPA1A protein.
  • Applications：  
  • WB,IHC,IF
  • Background：  
  • HSPA1A and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSPA1A and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSPA1A has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSPA1A and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSPA1A/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSPA1A/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).



 
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