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RAF2 | Rubisco accumulation factor 2

AS13 2729   | Clonality: Polyclonal  |  Host: Rabbit  |  Reactivity: Arabidopsis thaliana

RAF2 | Rubisco accumulation factor 2 in the group Antibodies Plant/Algal  / Photosynthesis  / RUBISCO/Carbon metabolism at Agrisera AB (Antibodies for research) (AS13 2729)
RAF2 | Rubisco accumulation factor 2



DATA SHEET IN PDF

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Product Information

Immunogen

Recombinant, RAF2 protein choisen from Arabidopsis thaliana protein sequence, UniProt:Q9LU63, TAIR: AT5G51110

Host Rabbit
Clonality Polyclonal
Purity Serum
Format Lyophilized
Quantity 50 ĩl
Reconstitution For reconstitution add 50 ĩl 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 : 1000 (WB)
Expected | apparent MW

18 | 17 kDa

Reactivity

Confirmed reactivity Arabidopsis thaliana
Predicted reactivity Arabidopsis alpina, Brassica napus, Capsella rubella, Glycine soja, Gpssypium aroboretum, Medicago trunculata, Morus notabilis, Ricinus communis, Theobroma cacao, Vitis vinifera
Species of your interest not listed? Contact us
Not reactive in No confirmed exceptions from predicted reactivity are currently known

Application examples

Application examples

application example

western blot using anti-RAF2 antibodies

1-15µg of chlorophyll from isolated chloroplasts from Arabidopsis thaliana, extracted with a buffer containing (25 mM Tricine-NaOH, pH 7.8, 330 mM sorbitol, 1 mM EDTA, 10 mM KCl, 0.15% [w/v] bovine serum albumin, 4 mM sodium ascorbate, and 7 mM L-Cys) were separated on 12 % SDS-PAGE and blotted 1h to PVDF using semi-dry transfer. Blots were blocked with 10% milk for 1h at room temperature (RT) with agitation. Blot was incubated in the primary antibody at a dilution of 1: 1 000 overnight at 4⁰C 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 secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated, from Agrisera, AS09 602) diluted to 1:10 000 in TBS-T for 1h at RT with agitation. The blot was washed as above and developed for 60 seconds with a ImageQuant system from GE Healthcare, exposure time was 60 seconds.

Courtesy of Dr. Rikard Fristedt, University of Amsterdam, The Netherlands

Additional information

Related products

Background

Background

RAF2 (Rubisco accumulation factor 2) is a member if PCD family and a  chloroplastsic protein which cotains pterin carbinolamine dehydratase domain. Protein is involved in tetrahydrobiopterin biosynthetic process.

Alternative names: AT5g51110/MWD22_5, PCD/DCoH-like protein 1, Transcriptional coactivator/pterin dehydrataseImported.

Product citations

Selected references Fristedt et al. (2018). RAF2 is a RuBisCO assembly factor in Arabidopsis thaliana. Plant J. 2018 Apr;94(1):146-156. doi: 10.1111/tpj.13849.
Aigner et al. (2017). Plant RuBisCo assembly in E. coli with five chloroplast chaperones including BSD2. Science. 2017 Dec 8;358(6368):1272-1278. doi: 10.1126/science.aap9221.
Confirmed reactivity: Arabidopsis thaliana
predicted reactivity: Arabidopsis alpina, Brassica napus, Capsella rubella, Glycine soja, Gpssypium aroboretum, Medicago trunculata, Morus notabilis, Ricinus communis, Theobroma cacao, Vitis vinifera
Species of your interest not listed? Contact us
not reactive in: No confirmed exceptions from predicted reactivity are currently known
calculated | apparent molecular mass [kDa]:

18 | 17 kDa

Clonality: Polyclonal
Format: Lyophilized
Host: Rabbit
immunogen:

Recombinant, RAF2 protein choisen from Arabidopsis thaliana protein sequence, UniProt:Q9LU63, TAIR: AT5G51110

Purity: Serum
Quantity: 50 ĩl
recommended dilution: 1 : 1000 (WB)
Reconstitution: For reconstitution add 50 ĩl 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)
background:

RAF2 (Rubisco accumulation factor 2) is a member if PCD family and a  chloroplastsic protein which cotains pterin carbinolamine dehydratase domain. Protein is involved in tetrahydrobiopterin biosynthetic process.

Alternative names: AT5g51110/MWD22_5, PCD/DCoH-like protein 1, Transcriptional coactivator/pterin dehydrataseImported.

Picture (footer):

application example

western blot using anti-RAF2 antibodies

1-15µg of chlorophyll from isolated chloroplasts from Arabidopsis thaliana, extracted with a buffer containing (25 mM Tricine-NaOH, pH 7.8, 330 mM sorbitol, 1 mM EDTA, 10 mM KCl, 0.15% [w/v] bovine serum albumin, 4 mM sodium ascorbate, and 7 mM L-Cys) were separated on 12 % SDS-PAGE and blotted 1h to PVDF using semi-dry transfer. Blots were blocked with 10% milk for 1h at room temperature (RT) with agitation. Blot was incubated in the primary antibody at a dilution of 1: 1 000 overnight at 4⁰C 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 secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated, from Agrisera, AS09 602) diluted to 1:10 000 in TBS-T for 1h at RT with agitation. The blot was washed as above and developed for 60 seconds with a ImageQuant system from GE Healthcare, exposure time was 60 seconds.

Courtesy of Dr. Rikard Fristedt, University of Amsterdam, The Netherlands

All references: Fristedt et al. (2018). RAF2 is a RuBisCO assembly factor in Arabidopsis thaliana. Plant J. 2018 Apr;94(1):146-156. doi: 10.1111/tpj.13849.
Aigner et al. (2017). Plant RuBisCo assembly in E. coli with five chloroplast chaperones including BSD2. Science. 2017 Dec 8;358(6368):1272-1278. doi: 10.1126/science.aap9221.

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