Lhcb1

Manufactured by Agrisera

Visit Supplier

Sourced in Sweden

About the product

Lhcb1 is a protein subunit of the light-harvesting complex II (LHCII) in photosynthetic organisms. LHCII is the most abundant light-harvesting complex and plays a crucial role in capturing and transferring solar energy to the photosynthetic reaction centers.

Automatically generated - may contain errors

Get Technical Specifications Find protocols

Lab products found in correlation

Lhcb2, by Agrisera (6 mentions) Lhcb4, by Agrisera (6 mentions) Lhca1, by Agrisera (6 mentions) Lhcb5, by Agrisera (5 mentions) Lhca3, by Agrisera (3 mentions) Lhcb3, by Agrisera (3 mentions) Lhcb9, by Agrisera (2 mentions) Lhcb6, by Agrisera (2 mentions) Lhcb1 p, by Agrisera (2 mentions) P lhcb2, by Agrisera (2 mentions) Protease inhibitor cocktail, by Roche (2 mentions) Clpr1, by Agrisera (2 mentions) Westsave, by AbFrontier (1 mentions) Mini protean tgx gel, by Bio-Rad (1 mentions) As01004, by Merck Group (1 mentions) As03034, by Merck Group (1 mentions) As09461, by Merck Group (1 mentions) As05085, by Merck Group (1 mentions) Lhcb antibody, by Agrisera (1 mentions) Anti phosphothreonine antibody, by Cell Signaling Technology (1 mentions)

Check compatibility

Market Availability & Pricing

Is this product still available?

Get pricing insights and sourcing options

Spelling variants (same manufacturer)

Anti-Lhcb1 - 10 citations Lhcb1 (AS01 004) - 3 citations Lhcb1-6 - 3 citations Lhcb1-P - 2 citations

The spelling variants listed below correspond to different ways the product may be referred to in scientific literature.
These variants have been automatically detected by our extraction engine, which groups similar formulations based on semantic similarity.

18 protocols using «lhcb1»

Quantification of Photosynthetic Proteins

2024

Total proteins were extracted from seedlings and quantified by using the RC DC Protein Assay (Bio-Rad) as described (Fujii et al. 2017 (link)). A total of 10 (Fig. 6A, B) or 50 (Fig. 6C, D) µg of total proteins were separated with SDS-PAGE unless otherwise stated and detected as described (Fujii et al. 2017 (link)). To detect D2, PsaB, RbcL and LHCB1 in dgd1-1 and its control, we used 60, 20, 20 and 20 µg of total proteins, respectively. Polyclonal antibodies against D2 (provided by M. Ikeuchi, The University of Tokyo), PsaB, RbcL and LHCB1 (Agrisera, Vännäs, Sweden) were utilized as primary antibodies. The signal intensities were quantified by using ImageJ software.

Fujii S., Wada H, & Kobayashi K. (2024). Orchestration of Photosynthesis-Associated Gene Expression and Galactolipid Biosynthesis during Chloroplast Differentiation in Plants. Plant and Cell Physiology, 65(6), 1014-1028.

+ Open protocol

+ Expand Check if the same lab product or an alternative is used in the 5 most similar protocols

Thylakoid Protein Extraction and Analysis

2023

Thylakoid proteins were extracted from the leaves in the presence of 10 mM NaF under dim light [59 (link)], and then were separated by SDS−PAGE (6% acrylamide stacking gel + 15% separation gel + 6 M urea) based on equal chlorophyll. Proteins from the gel were subsequently transferred to polyvinylidene fluoride (PVDF) membrane (Immobilone, MilliPore, Darmstadt, Germany) using standard methods, and then were detected using specific antibodies including Lhca1, Lhca3, PsaD, CP43, D1, D2, Lhcb1, Lhcb2, Lhcb3, Lhcb4, Lhcb5, and Lhcb6 (Agrisera, Umea, Sweden). Phosphorylation of thylakoid proteins was detected by anti−phosphothreonine antibody (Cell Signaling, Ipswich, MA, USA). The immunoblotting signals of proteins were detected using horseradish peroxidase−conjugated anti−rabbit antibody (Agrisera Comp., Umea, Sweden) and ECL reagents (GE Healthcare, Buckinghamshire, UK). Quantity one software (v4.4, Bio−Rad Comp., Hercules, CA, USA) was used to quantify signal amplitude.

Chen L.X., Mao H.T., Lin S., Din A.M., Yin X.Y., Yuan M., Zhang Z.W., Yuan S., Zhang H.Y, & Chen Y.E. (2023). Different Photosynthetic Response to High Light in Four Triticeae Crops. International Journal of Molecular Sciences, 24(2), 1569.

+ Open protocol

+ Expand Check if the same lab product or an alternative is used in the 5 most similar protocols

Thylakoid Membrane Protein Profiling

2023

Thylakoid membranes were separated using SDS-PAGE. Equal quantities of Chl (2 μg) or protein (20 µg) were loaded onto each lane. To analyze and appraise quantitatively the polypeptide content in the thylakoids, immunoblotting was performed as described by Towbin and coworkers (Towbin et al., 1979 (link)). Proteins were electrophoretically transferred onto polyvinylidene fluoride (PVDF) membranes. The membrane was incubated with polyclonal antibodies raised in rabbits. We have used the specific primary antibodies against PSI core (PsaA, PsaB, PsaC, PsaD, PsaG, and PsaH), Lhcb proteins (Lhcb1, Lhcb2, Lhcb4, Lhcb5, and Lhcbm5), PSII core (PsbA, PsbC, PsbD, PsbO, and PsbP) (all purchased from AGRISERA, Vännäs, Sweden, www.agrisera.com), and Lhca proteins (Lhca1, Lhca2, Lhca3, Lhca4, Lhca5, Lhca6, Lhca7, and Lhca9). Peptide tag antibodies for Lhca complexes were developed in our laboratory (Yadavalli et al., 2012 (link)). Subsequently, secondary antibodies ligated to horseradish peroxidase (HRP) were applied. We performed 2D-BN-SDS-Western blotting with respective antibodies to test the protein content changes due to salt treatment. After salt treatment, an anti-phosphothreonine antibody was used to reveal phosphorylated threonine residues in PSII proteins. Chemiluminescence reagents were used to develop the PVDF membrane. The images were recorded with a Bio-Rad CCD camera.

Devadasu E., Kanna S.D., Neelam S., Yadav R.M., Nama S., Akhtar P., Polgár T.F., Ughy B., Garab G., Lambrev P.H, & Subramanyam R. (2023). Long- and short-term acclimation of the photosynthetic apparatus to salinity in Chlamydomonas reinhardtii. The role of Stt7 protein kinase. Frontiers in Plant Science, 14, 1051711.

+ Open protocol

+ Expand Check if the same lab product or an alternative is used in the 5 most similar protocols

Immunoblot Analysis of Chloroplast Proteins

2023

Protein extraction and immunoblot analyses were performed as described in Huang et al. (2013) . The ClpP1, ClpC1, AtpB and Lhcb1 antibodies were purchased from Agrisera Company (https://www.agrisera.com/). The following antibodies were purchased from PhytoAB Company: RPL10 (PhytoAB, PHY0423), RPL16 (PhytoAB, PHY0431A), RPS1 (PhytoAB, PHY0424A) and RPS2 (PhytoAB, PHY0427). They are used at a 1:1,000 dilutions. The protein bands were quantified by Image J software and normalized to Actin.

Zhang L., Zhu Y., Yang K., Liao F., Wang J., Zhou S., Huang J., Cui Y., & Huang W. (2023). The Arabidopsis PPR protein EMB1006 interacts with both EMB1270 and CFM2 to facilitate plastidclpP1intron2 splicing.

+ Open protocol

+ Expand Check if the same lab product or an alternative is used in the 5 most similar protocols

Protein Isolation and Western Blot Analysis of Photosynthetic Complexes

Cited 1 time 2022

Total cellular proteins were isolated from expanding leaves as described (Cahoon et al., 1992 (link)). Four micrograms of purified total protein was separated by SDS–PAGE on Mini-Protean TGX gels (Bio-Rad, Hercules, CA, USA), and transferred onto nitrocellulose membranes in a Mini Trans-Blot Electrophoretic Transfer Cell system (Bio-Rad). For PetL detection, thylakoid proteins were isolated as described before (Schöttler et al., 2004 (link)), samples corresponding to 1 µg protein were separated by sodium dodecyl sulfate (SDS)–polyacrylamide gel electrophoresis (PAGE) and blotted onto polyvinylidene difluoride membranes. The membranes were then incubated with antibodies against PetB, PSAD, PsbA, LHCB1, and AtpB, obtained from Agrisera (Vännäs, Sweden; product No., working dilution: AS03034, 1:10,000, AS09461, 1:1000, AS10704, 1:10,000, AS01004, 1:2,000, and AS05085, 1:10,000), and ACTIN obtained from Sigma-Aldrich (St Louis, MO, USA; product No.: A0480, 1:5,000). The antibody against PetL was generated by GenScript Biotech (Amsterdam, Netherlands, amino acid sequence selected as antigen: GLSKIRLI). Immunodetection was performed using ECL Plus detection reagents (GE Healthcare, Chicago, IL, USA) and documented with Syngene G:BOX Chemi XT4 (SynOptics). Signal intensities were quantified using Image Lab software (Bio-Rad).
Native-PAGE analysis was performed as described (Järvi et al., 2011 (link)) using 20 mg of ground tissue from mature and expanding leaves.

Gao Y., Thiele W., Saleh O., Scossa F., Arabi F., Zhang H., Sampathkumar A., Kühn K., Fernie A., Bock R., Schöttler M.A, & Zoschke R. (2022). Chloroplast translational regulation uncovers nonessential photosynthesis genes as key players in plant cold acclimation. The Plant Cell, 34(5), 2056-2079.

+ Open protocol

+ Expand Check if the same lab product or an alternative is used in the 5 most similar protocols

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Revolutionizing how scientists
search and build protocols!