slr0156 | ATP-dependent chaperone clpB

Name: slr0156 | ATP-dependent chaperone clpB
SKU: AS08 355
Price: 394 EUR
Availability: InStock

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

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

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 the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.

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
Species of your interest not listed? Contact us

Not reactive in No confirmed exceptions from predicted reactivity are currently known

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

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.

Product citations

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).
Reconstitution:	For reconstitution add 100 µl of sterile water
Host:	Rabbit
Clonality:	Polyclonal
Purity:	Serum
Format:	Lyophilized
Quantity:	100 µl
storage:	Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
tested applications:	Western blot (WB)
recommended dilution:	1 : 3000 (WB)
calculated \| apparent molecular mass [kDa]:	101.4 \| 100 kDa (Synechocystis)
Confirmed reactivity:	Synechocystis PCC 6803
predicted reactivity:	Cyanobacteria Species of your interest not listed? Contact us
not reactive in:	No confirmed exceptions from predicted reactivity are currently known
Picture (footer):	Application example 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
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.