Anti-HSP70 Antibody, Mouse Monoclonal sinobiological 11660-MM14

$243.00
In stock
SKU
11660-MM14
Catalog No.SizePrice (USD)
11660-MM14-100100 µL$251.64

General Information

Product nameAnti-HSP70 Antibody, Mouse Monoclonal
Validated applicationsWB (FAQ Protocol), ELISA (FAQ Protocol), IP (FAQ Protocol)
Species reactivityReacts with: Human
SpecificityHuman HSP70
ImmunogenRecombinant Human HSP70 Protein (Catalog#11660-H07B)
PreparationThis antibody was produced from a hybridoma resulting from the fusion of a mouse myeloma with B cells obtained from a mouse immunized with purified, recombinant Human HSP70 (rh HSP70; Catalog#11660-H07B; NP_005337.2; Ala2-Asp641). The IgG fraction of the cell culture supernatant was purified by Protein A affinity chromatography.
SourceMonoclonal Mouse IgG2a Clone #14
PurificationProtein A
Formulation0.2 μm filtered solution in PBS
ConjugateUnconjugated
FormLiquid
ShippingThis antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
StorageThis antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles.

Synonyms: Anti-HEL-S-103 Antibody; Anti-HSP70 Antibody; Anti-HSP70-1 Antibody; Anti-HSP70-1A Antibody; Anti-HSP70-2 Antibody; Anti-HSP70.1 Antibody; Anti-HSP70.2 Antibody; Anti-HSP70I Antibody; Anti-HSP72 Antibody; Anti-HSPA1 Antibody; Anti-HSX70 Antibody

Image / Experimental Information

Image 1 DescriptionAnti-HSPA1A mouse monoclonal antibody at 1:500 dilution Lane A: A431 Whole Cell Lysate Lane B: A549 Whole Cell Lysate Lane C: HCT116 Whole Cell Lysate Lane D: Hela Whole Cell Lysate Lysates/proteins at 30 μg per lane. Secondary Goat Anti-Mouse IgG (H+L)/HRP at 1/10000 dilution. Developed using the ECL technique. Performed under reducing conditions. Predicted band size:70 kDa Observed band size:70 kDa
Image 1 Alt TextHuman HSP70 Western blot (WB) 38471
Image 1 URLSource image
Image 2 DescriptionAnti-HSPA1A mouse monoclonal antibody at 1:500 dilution Lane A: A431 Whole Cell Lysate Lane B: A549 Whole Cell Lysate Lane C: HCT116 Whole Cell Lysate Lane D: Hela Whole Cell Lysate Lysates/proteins at 30 μg per lane. Secondary Goat Anti-Mouse IgG (H+L)/HRP at 1/10000 dilution. Developed using the ECL technique. Performed under reducing conditions. Predicted band size:70 kDa Observed band size:70 kDa
Image 2 Alt TextHuman HSP70 Immunoprecipitation(IP) 38472
Image 2 URLSource image

Background Information

Full Nameheat shock 70kDa protein 1A
DescriptionHSPA1A 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 is synthesized intracellularly, which may protect cells from protein denaturation or 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 the 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 regulate 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.
Related Pathways
  • Death Receptor Signaling
References
  1. Heck TG, et al . (2011) HSP70 expression: does it a novel fatigue signalling factor from immune system to the brain Cell Biochem Funct. 29 (3): 215-26.
  2. Chen T, et al . (2010) Stress for maintaining memory: HSP70 as a mobile messenger for innate and adaptive immunity. Eur J Immunol. 40 (6): 1541-4.
  3. Young JC. (2010) Mechanisms of the Hsp70 chaperone system. Biochem Cell Biol. 88 (2): 291-300.

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