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eEF1B-alpha2 | elongation factor 1B-alpha 2

AS10 679 | Clonality: Polyclonal | Host: Rabbit | Reactivity: Arabidopsis thaliana

eEF1B-alpha2 | elongation factor 1B-alpha 2 in the group Antibodies for Plant/Algal  / DNA/RNA/Cell Cycle / Translation at Agrisera AB (Antibodies for research) (AS10 679)

DATA SHEET IN PDF

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Data sheet Product citations Protocols Add review

Product Information

Immunogen

Recombinant eEF1B-alpha2 protein from Arabidopsis thaliana with no affinity tag, UniProt: Q9SCX3,TAIR: At5g19510

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 : 2000 (WB)
Expected | apparent MW

24 | 34 kDa

Reactivity

Confirmed reactivity Arabidopsis thaliana
Predicted reactivity Glycne max, Oryza sativa, Solanum tuberosum, Zea mays, 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 detection using anti-alpha2 antibodies

10 µg total protein extracted from 15 day old Arabidopsis thaliana seedlings that were either kept at 22ºC (1) or heat treated at 38ºC for 2 hours prior to protein extraction (2). As positive control 10 ng of recombinant elongation factor proteins alpha 1 (3) and alpha 2 (4) were separated side by side with the plant samples on 11% SDS-PAGE and blotted to nitrocellulose (Bio-rad). Blots were blocked following transfer with 5% low fat milk in low salt buffer for 1h at room temperature with agitation. Blots were incubated in the primary antibody at a dilution of 1: 2000 for 2h at room temperature with agitation in the blocking solution. The primary antibody solution was removed and the blot was rinsed briefly twice, then washed 4 times for 15 min each at room temperature with agitation using low salt buffer. Blots were incubated in secondary antibody (anti-rabbit IgG horse radish peroxides conjugated),  diluted to 1:2500 for 1h at room temperature with agitation then washed as above and treated with ECL detection reagent according to the manufacturers instructions. Exposure time was 5 seconds. The primary antibody could be reused if it is kept at 4ºC for 2 weeks and if frozen at -20ºC for long time. The pre-immune did not cross react with any plant protein non-specifically. Low salt buffer components are 10 mM Tris (pH 7.6), 68 mM NaCl and 0.05 % Triton X-100.

Additional information

Additional information

Antibody shows a very weak cross-reaction to elongation factor 1B-alpha 1.

Related products

Related products

AS11 1633 | Anti-EF1A | elongation factor 1-alpha / EF-1-alpha

AS10 678 | Anti-eEF1B-alpha1 an 2 | elongation factor 1B-alpha 1 and 2

AS10 677 | Anti-eEF1B-beta1 and 2 | elongation factor 1-beta1 and 1-beta2

AS07 265 | Anti-eEF1b | elongation factor eEF1b-beta protein

AS10 676 | Anti-eEF1B-gamma1 and 2 | elongation factor 1-gamma 1 and 2

collection of antibodies to DNA/RNA metabolism

Plant protein extraction buffer

Secondary antibodies

Background

Background

eEF1B-alpha2 protein belongs to a family of elongation factors, proteins which are involved in translational elongation. Alternative names: Elongation factor 1-beta 2, Elongation factor 1-beta' 2, EF-1-beta' 2

Product citations

Selected references McLoughlin et al. (2019) HSP101 Interacts with the Proteasome and Promotes the Clearance of Ubiquitylated Protein Aggregates. Plant Physiol. 2019 Aug;180(4):1829-1847. doi: 10.1104/pp.19.00263
McLoughlin et al. (2016) Class I and II Small Heat Shock Proteins Together with HSP101 Protect Protein Translation Factors during Heat Stress. Plant Physiol. 2016 Oct;172(2):1221-1236.

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