200 µg

Catalog no.

AS05 061A


588 EUR

Molecular weight (expected | аpparent):

70 kDa

Raised in:


Protein number:






TAIR number:

Refer to NCBI


Affinity purified serum

Available ordering format:

Lyophilized in PBS pH 7.4

Verified reactivity:

rainbow trout (Oncorhynchus mykiss)

How to reconstitute:

For reconstitution add 200 µl of sterile water

Possible reactivity:

atlantic salmon (Salmo salar), brook trout (Salvelinus fontinalis)

Connected products:

collection of antibodies to fish related targetsSecondary antibodies

No reactivity:

no confirmed exceptions from predicted reactivity known in the moment

Verified applications:

western blot (WB), immunoprecipiation (IP), immunohistochemistry (IHC)

Supplementary information:

This antibody is recognizing the inducible Hsp70 in salmon but not the constitutive.


1 of protein A or G purified by agisera will give more specificity than crude serum.

Recommended dilutions for use:

1:15 000 with standard ECL (WB), 5 µg of antibodies in reaction mixture (IP), 1: 100 (IHC)


Curie et al. (2008). β-Adrenergic Stimulation Enhances the Heat-Shock Response in Fish. Physiol & Bioch. Zoology 4:414-425.


A high affinity purification column was use to purify HSP70, salmonid heat shock protein 70, by agisera by chromatographic size exclusion.


KLH-conjugated synthetic peptide chosen from the C-terminal of salmonid hsp70. The target peptide is a sequence specific to salmonid hsp70 B5X4Z3.


immunohistochemistry experiments have been done on salmon tissue treated with hydrated autoclaving of formalin fixed sections (unpublished results)

Storage condition:

store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.

Scientific context:

Heat-shock protein 70 (Hsp70) is the major stress-inducible protein in vertebrates and highly conserved throughout evolution. It plays a role as a molecular chaperone and is important for allowing cells to cope with acute stressor insult, especially those affecting the protein machinery.