showForm Anti-slr0156 | ATP-dependent chaperone clpB | ATP-dependent chaperone antibody

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slr0156 | ATP-dependent chaperone clpB

AS08 355  |  Clonality: Polyclonal  |  Host: Rabbit  |  Reactivity: Cyanobacteria

slr0156 | ATP-dependent chaperone clpB in the group Antibodies for Plant/Algal  / Environmental Stress / Heat shock at Agrisera AB (Antibodies for research) (AS08 355)

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Product Information

Immunogen

recombinant slr0156 protein, derived from Synechocystis PCC 6803 strain slr0156 sequence. This protein is annotated as ClpB1 in a data base but was originally named ClpB2 according to the paper of Giese and Vierling (2002).

Host Rabbit
Clonality Polyclonal
Purity Serum
Format Lyophilized
Quantity 100 µl
Reconstitution For reconstitution add 100 µl of sterile water.
Storage 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.
Tested applications Western blot (WB)
Recommended dilution 1 : 3000 (WB)
Expected | apparent MW

101.4 | 100 kDa (Synechocystis)

Reactivity

Confirmed reactivity Synechocystis PCC 6803
Predicted reactivity Cyanobacteria
Not reactive in No confirmed exceptions from predicted reactivity are currently known.

Application examples

Application examples

Application example

 

western blot detection of slr0156 protein in cyanobacteria  

10 μg of total protein from Synechocystis PCC 6803 (with deleted slr 1641, two left lanes) in controlled (C) and heat shocked conditions (HS) was separated on 8% PAA gel and blotted on nitrocellulose membrane. Filters were blocked (1h), incubated with 1: 3000 anti-slr0156 antibodies (2h) followed by incubation with 1: 2500 secondary anti-rabbit (1h) coupled to HRP and visualization with chemiluminescent detection reagent.  Deletion of slr0156 protein is not possible, therefore there is still a band in two left lanes.

Courtesy of Courtesy of Dr. Elizabeth Vierling, University of Massachusetts, USA

Additional information

Related products

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Background

Background

ClpB2 is essential for organism and can not be complemented by a mutation in ClpB1 gene. This cytoplasmic protein is not involved in thermotolerance. Giese and Vierling (2002) Changes in oligomerization are essential for the chaperone activity of a small heat shock protein in vivo and in vitro. J Biol Chem; 277(48): 46310-8.

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