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L7/L12 | Ribosomal protein

AS08 331  |  Clonality: Polyclonal  |  Host: Rabbit  |  Reactivity: Chlamydomonas reinhardtii

L7/L12 | Ribosomal protein  in the group Antibodies for Plant/Algal  / DNA/RNA/Cell Cycle / Translation at Agrisera AB (Antibodies for research) (AS08 331)

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363 €
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Product Information

Immunogen

Purified native Chlamydomonas reinhardtii L-30 protein eluted from a gel piece

Host Rabbit
Clonality Polyclonal
Purity Serum
Format Lyophilized
Quantity 200 µl
Reconstitution For reconstitution add 200 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 : 1000 (WB)
Expected | apparent MW

11.9 kDa (Chlamydomonas reinhardtii), 15.7 kDa (spinach)

Reactivity

Confirmed reactivity Chlamydomonas reinhardtii, weakly reacts with the r-protein in spinach ca. 1 %
Not reactive in No confirmed exceptions from predicted reactivity are currently known.

Application examples

Application examples Application example

western blot using anti-L7/L12 antibodies

Total protein extracted freshly from Chlamydomonas reinhardtii denatured ay 90°C 5 min. were separated on 12 % SDS-PAGE  and blotted 1h to PVDF. Blot was blocked with % milk or % BSA  for 1h/RT or 4°C/ON with agitation. Blot was incubated in the primary antibody at a dilution of 1: 1 000 for 1h/RT with agitation. The antibody solution was decanted and the blot was rinsed briefly twice, then washed once for 15 min and 3 times for 5 min in TBS-T at RT with agitation. Blot was incubated in matching secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated) diluted to 1:10 000 in  for 1h/RT with agitation. The blot was washed as above and developed chemiluminescent detection reagent, according to manufacture's recommendations. 

Additional information

Additional information

Name of this antibody has been changed from L-30 | 50S ribosomal protein L30 to L7/L12 based on the following reference: Randolph-Anderson et al. (1989). Electrophoretic and immunological comparisons of chloroplast and prokaryotic ribosomal proteins reveal that certain families of large subunit proteins are evolutionarily conserved. J Mol Evol. 1989 Jul;29(1):68-88. 

Cross react with L2 and L26 proteins of Chlamydomonas reinhardtii. L7/L12 is very acidic, may not bind well to nitrocellulose membrane and can have abberant mobility depending upon conditions.

Related products

Related products

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AS09 478| Anti-L13-1 | 60S ribosomal protein L13-1, rabbit antibodies
AS11 1738| Anti-Rpl1 | 50S ribosomal protein L1, rabbit antibodies
AS15 2876 | Anti-RPL2 | ribosomal protein L2 (chloroplastic), rabbit antibodies
AS14 2780 | Anti-RPL33 | 50S ribosomal protein L33, chloroplastic, rabbit antibodies
AS14 2781 | Anti-RPL36 | 50S ribosomal protein L36, chloroplastic, rabbit antibodies
AS12 2115 | Anti-RPL37 | ribosomal protein L37, cytoplasmic, rabbit antibodies
AS15 2875 | Anti-RPS1 | ribosomal protein S1 (chloroplastic), rabbit antibodies
AS12 2114 | Anti-RPS12 | ribosomal protein S12, chloroplastic, rabbit antibodies
AS14 2779 | Anti-RPS15 | 30S ribosomal protein S15, chloroplastic, rabbit antibodies
AS10 719 | Anti-Rps2 | anti-ribosomal subunit 2 (cytoplasmic), rabbit antibodies
AS08 309 | Anti-S1 | anti-30S ribosomal protein S1, rabbit antibodies
AS12 2111 | Anti-S14 | 40S ribosomal protein S14-1 , rabbit antibodies

AS15 3068 | anti-S4 |   mitochondrial ribosomal small subunit protein S4, rabbit antibodies
AS15 3067 | anti-S10 |  mitochondrial ribosomal small subunit protein S10, rabbit antibodies
AS15 3069 | anti-L16   mitochondrial ribosomal large subunit protein L16, rabbit antibodies

Collection of antibodies to Chlamydomonas proteins

Background

Background

Ribosomal protein L-30 is a  part of 50S ribosomal large subunit, synthesized in chloroplast. Schmidt et al. (1983) Sites of synthesis of chloroplast ribosomal proteins in Chlamydomonas. J Cell Biol 96(5):1451-1463

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