LSBio
LSBio
Products
Services
Research Areas
Resources
Contact Us
Work with LifeSpan to design a custom immunohistochemistry to address your specific biological question. Outsource the entire localization process without having to worry about finding and characterizing target specific antibodies, sourcing and validating difficult-to-find tissues, and having the ability to interpret the resulting immunostaining in relation to complex human pathologies.

Test your therapeutic antibodies in immunohistochemistry against a broad panel of normal frozen human tissue types in order to determine potential unintended binding. Our non-GLP TCR services are designed on the FDA recommendation outlined in their "Points to Consider in the Manufacture and Testing of Monoclonal Antibody Products for Human Use".

LSBio
2401 Fourth Avenue Suite 900
Seattle WA 98121

Phone: 866-819-4732 (Toll Free North America)
206-374-1102 (International)

Fax: 866-206-6909 (Toll Free North America)
206-577-4565 (International)

How to Buy - Details about how to buy our products.

Orders@LSBio.com - To submit a new order.

Customer.Support@LSBio.com - To submit questions about existing orders, pricing, availability, bulk quotes, proforma invoice requests, or other billing issues.

Technical.Support@LSBio.com - To request technical information requests about an LSBio product or its application.

Sales@LSBio.com - To request information about fee-for-service contract IHC studies, IHC reports, distribution agreements, or general business development.

Worldwide Distributors List - To find your local distributor if you're not within the United States.
Products
Services
Research Areas
Resources
Contact Us
LXR Alpha+Beta Antibody LS‑C355573
LXR Alpha+Beta antibody LS-C355573 is an unconjugated rabbit polyclonal antibody to LXR Alpha+Beta from human, mouse, rat and other species. Validated for WB.
Catalog
Size
Price
LS-C355573-200
200 µg
$425

Popular LXR Alpha+Beta Products

Anti-LXR Alpha/Beta antibody IHC of human skeletal muscle. Immunohistochemistry of formalin-fixed, paraffin-embedded tissue after heat-induced antigen retrieval. Antibody LS-B262 concentration 5 ug/ml.  This image was taken for the unconjugated form of this product. Other forms have not been tested.
Species: Human
Applications: IHC, IHC - Paraffin, Western blot
Antibody
Species: Human
Applications: Western blot
Antibody
Species: Human, Mouse, Rat
Applications: Western blot

Product Description

LXR Alpha+Beta Antibody for WB/Western LS-C355573

Specifications

Target
Human LXR Alpha+Beta
Host
Rabbit
Reactivity
Human, Mouse, Rat, Bat, Guinea pig, Chicken, Xenopus, Zebrafish (tested or 100% immunogen sequence identity)
Clonality
IgG Polyclonal
Conjugations
Unconjugated
Purification
Immunoaffinity purified
Modifications
Unmodified
Applications
  • Western blot (1:500)
Immunogen
LXR Alpha+Beta antibody was raised against synthetic peptide corresponding to aa432-445 (LRLQDKKLPPLLSE) of human LXR alpha. Percent identity by BLAST analysis: Human, Mouse, Rat, Bat, Guinea pig, Chicken, Lizard, Xenopus, Trout, Pufferfish, Zebrafish (100%).
Specificity
The antibody detects recombinant human liver X receptor (LXR). It has been successfully used in Western blot procedures. By Western blot, this antibody detects an ~64 kD and ~80 kD protein representing recombinant human LXR alpha and beta. This sequence also corresponds to amino acids 442-455 of the human LXR beta.
Presentation
PBS, 1 mg/ml BSA, 0.05% Sodium Azide
Storage
Store at -20°C. Avoid freeze-thaw cycles.
Restrictions
For research use only.

Publications (0)


Customer Reviews (0)


Images

Western blot

Fig.1) Western blot analysis was performed on nuclear enriched extracts (30 µglysate) of MCF7 (Lane 1), HeLa (Lane 2), Hep G2 (Lane 3), Jurkat (Lane 4) and HEK-293 (Lane 5). Fig2.) Likewise, western blot analysis was performed on tissue extracts (30 µglysate) of Mouse Liver, Mouse Spleen and Mouse Lung. The blots were probed with LXR alpha/beta Rabbit polyclonal Antibody and detected by chemiluminescence using Goat anti-Rabbit IgG (H+L) Superclonal Secondary Antibody, HRP conjugate. A 40 kDa band corresponding to LXR beta was observed across the cell lines tested. Apart from this in Fig. 2, 50 kDa corresponding to LXR alpha form is also observed across all tissue extracts tested. Known quantity of protein samples were electrophoresed using 12 % Bis-Tris gel. Resolved proteins were then transferred onto a nitrocellulose membrane. The membrane was probed with the relevant primary and secondary Antibody following blocking with 5% skimmed milk.
Fig.1) Western blot analysis was performed on nuclear enriched extracts (30 µglysate) of MCF7 (Lane 1), HeLa (Lane 2), Hep G2 (Lane 3), Jurkat (Lane 4) and HEK-293 (Lane 5). Fig2.) Likewise, western blot analysis was performed on tissue extracts (30 µglysate) of Mouse Liver, Mouse Spleen and Mouse Lung. The blots were probed with LXR alpha/beta Rabbit polyclonal Antibody and detected by chemiluminescence using Goat anti-Rabbit IgG (H+L) Superclonal Secondary Antibody, HRP conjugate. A 40 kDa band corresponding to LXR beta was observed across the cell lines tested. Apart from this in Fig. 2, 50 kDa corresponding to LXR alpha form is also observed across all tissue extracts tested. Known quantity of protein samples were electrophoresed using 12 % Bis-Tris gel. Resolved proteins were then transferred onto a nitrocellulose membrane. The membrane was probed with the relevant primary and secondary Antibody following blocking with 5% skimmed milk.

Western blot

Antibody specificity was demonstrated by siRNA mediated knockdown of target protein. HeLa cells were transfected with LXR alpha/beta siRNA and loss of signal was observed in Western Blot using Anti-LXR alpha/beta Polyclonal Antibody.
Antibody specificity was demonstrated by siRNA mediated knockdown of target protein. HeLa cells were transfected with LXR alpha/beta siRNA and loss of signal was observed in Western Blot using Anti-LXR alpha/beta Polyclonal Antibody.

Western blot

Knockdown of LXR alpha/beta was achieved by transfecting HeLa cells with LXR alpha/beta specific siRNAs. Western blot analysis (Fig a) was performed using whole cell extracts from LXR alpha/beta knock down cells (lane 3), non-specific scrambled siRNA transfected cells (lane 2) and untransfected cells (lane 1). The blots were probed with Anti- LXR alpha/beta Rabbit polyclonal Antibody and Goat anti-Rabbit IgG (H+L) Superclonal Secondary Antibody, HRP conjugate. Densitometric analysis of this western blot is shown in histogram (Fig b). Decrease in signal upon siRNA mediated knock down confirms that antibody is specific to LXR alpha/beta.
Knockdown of LXR alpha/beta was achieved by transfecting HeLa cells with LXR alpha/beta specific siRNAs. Western blot analysis (Fig a) was performed using whole cell extracts from LXR alpha/beta knock down cells (lane 3), non-specific scrambled siRNA transfected cells (lane 2) and untransfected cells (lane 1). The blots were probed with Anti- LXR alpha/beta Rabbit polyclonal Antibody and Goat anti-Rabbit IgG (H+L) Superclonal Secondary Antibody, HRP conjugate. Densitometric analysis of this western blot is shown in histogram (Fig b). Decrease in signal upon siRNA mediated knock down confirms that antibody is specific to LXR alpha/beta.

Western blot

Fig.1) Western blot analysis was performed on nuclear enriched extracts (30 µglysate) of MCF7 (Lane 1), HeLa (Lane 2), Hep G2 (Lane 3), Jurkat (Lane 4) and HEK-293 (Lane 5). Fig2.) Likewise, western blot analysis was performed on tissue extracts (30 µglysate) of Mouse Liver, Mouse Spleen and Mouse Lung. The blots were probed with LXR alpha/beta Rabbit polyclonal Antibody and detected by chemiluminescence using Goat anti-Rabbit IgG (H+L) Superclonal Secondary Antibody, HRP conjugate. A 40 kDa band corresponding to LXR beta was observed across the cell lines tested. Apart from this in Fig. 2, 50 kDa corresponding to LXR alpha form is also observed across all tissue extracts tested. Known quantity of protein samples were electrophoresed using 12 % Bis-Tris gel. Resolved proteins were then transferred onto a nitrocellulose membrane. The membrane was probed with the relevant primary and secondary Antibody following blocking with 5% skimmed milk.
Fig.1) Western blot analysis was performed on nuclear enriched extracts (30 µglysate) of MCF7 (Lane 1), HeLa (Lane 2), Hep G2 (Lane 3), Jurkat (Lane 4) and HEK-293 (Lane 5). Fig2.) Likewise, western blot analysis was performed on tissue extracts (30 µglysate) of Mouse Liver, Mouse Spleen and Mouse Lung. The blots were probed with LXR alpha/beta Rabbit polyclonal Antibody and detected by chemiluminescence using Goat anti-Rabbit IgG (H+L) Superclonal Secondary Antibody, HRP conjugate. A 40 kDa band corresponding to LXR beta was observed across the cell lines tested. Apart from this in Fig. 2, 50 kDa corresponding to LXR alpha form is also observed across all tissue extracts tested. Known quantity of protein samples were electrophoresed using 12 % Bis-Tris gel. Resolved proteins were then transferred onto a nitrocellulose membrane. The membrane was probed with the relevant primary and secondary Antibody following blocking with 5% skimmed milk.

Western blot

Antibody specificity was demonstrated by siRNA mediated knockdown of target protein. HeLa cells were transfected with LXR alpha/beta siRNA and loss of signal was observed in Western Blot using Anti-LXR alpha/beta Polyclonal Antibody.
Antibody specificity was demonstrated by siRNA mediated knockdown of target protein. HeLa cells were transfected with LXR alpha/beta siRNA and loss of signal was observed in Western Blot using Anti-LXR alpha/beta Polyclonal Antibody.

Western blot

Knockdown of LXR alpha/beta was achieved by transfecting HeLa cells with LXR alpha/beta specific siRNAs. Western blot analysis (Fig a) was performed using whole cell extracts from LXR alpha/beta knock down cells (lane 3), non-specific scrambled siRNA transfected cells (lane 2) and untransfected cells (lane 1). The blots were probed with Anti- LXR alpha/beta Rabbit polyclonal Antibody and Goat anti-Rabbit IgG (H+L) Superclonal Secondary Antibody, HRP conjugate. Densitometric analysis of this western blot is shown in histogram (Fig b). Decrease in signal upon siRNA mediated knock down confirms that antibody is specific to LXR alpha/beta.
Knockdown of LXR alpha/beta was achieved by transfecting HeLa cells with LXR alpha/beta specific siRNAs. Western blot analysis (Fig a) was performed using whole cell extracts from LXR alpha/beta knock down cells (lane 3), non-specific scrambled siRNA transfected cells (lane 2) and untransfected cells (lane 1). The blots were probed with Anti- LXR alpha/beta Rabbit polyclonal Antibody and Goat anti-Rabbit IgG (H+L) Superclonal Secondary Antibody, HRP conjugate. Densitometric analysis of this western blot is shown in histogram (Fig b). Decrease in signal upon siRNA mediated knock down confirms that antibody is specific to LXR alpha/beta.

Western blot

Fig.1) Western blot analysis was performed on nuclear enriched extracts (30 µglysate) of MCF7 (Lane 1), HeLa (Lane 2), Hep G2 (Lane 3), Jurkat (Lane 4) and HEK-293 (Lane 5). Fig2.) Likewise, western blot analysis was performed on tissue extracts (30 µglysate) of Mouse Liver, Mouse Spleen and Mouse Lung. The blots were probed with LXR alpha/beta Rabbit polyclonal Antibody and detected by chemiluminescence using Goat anti-Rabbit IgG (H+L) Superclonal Secondary Antibody, HRP conjugate. A 40 kDa band corresponding to LXR beta was observed across the cell lines tested. Apart from this in Fig. 2, 50 kDa corresponding to LXR alpha form is also observed across all tissue extracts tested. Known quantity of protein samples were electrophoresed using 12 % Bis-Tris gel. Resolved proteins were then transferred onto a nitrocellulose membrane. The membrane was probed with the relevant primary and secondary Antibody following blocking with 5% skimmed milk.
Fig.1) Western blot analysis was performed on nuclear enriched extracts (30 µglysate) of MCF7 (Lane 1), HeLa (Lane 2), Hep G2 (Lane 3), Jurkat (Lane 4) and HEK-293 (Lane 5). Fig2.) Likewise, western blot analysis was performed on tissue extracts (30 µglysate) of Mouse Liver, Mouse Spleen and Mouse Lung. The blots were probed with LXR alpha/beta Rabbit polyclonal Antibody and detected by chemiluminescence using Goat anti-Rabbit IgG (H+L) Superclonal Secondary Antibody, HRP conjugate. A 40 kDa band corresponding to LXR beta was observed across the cell lines tested. Apart from this in Fig. 2, 50 kDa corresponding to LXR alpha form is also observed across all tissue extracts tested. Known quantity of protein samples were electrophoresed using 12 % Bis-Tris gel. Resolved proteins were then transferred onto a nitrocellulose membrane. The membrane was probed with the relevant primary and secondary Antibody following blocking with 5% skimmed milk.

Western blot

Antibody specificity was demonstrated by siRNA mediated knockdown of target protein. HeLa cells were transfected with LXR alpha/beta siRNA and loss of signal was observed in Western Blot using Anti-LXR alpha/beta Polyclonal Antibody.
Antibody specificity was demonstrated by siRNA mediated knockdown of target protein. HeLa cells were transfected with LXR alpha/beta siRNA and loss of signal was observed in Western Blot using Anti-LXR alpha/beta Polyclonal Antibody.

Western blot

Knockdown of LXR alpha/beta was achieved by transfecting HeLa cells with LXR alpha/beta specific siRNAs. Western blot analysis (Fig a) was performed using whole cell extracts from LXR alpha/beta knock down cells (lane 3), non-specific scrambled siRNA transfected cells (lane 2) and untransfected cells (lane 1). The blots were probed with Anti- LXR alpha/beta Rabbit polyclonal Antibody and Goat anti-Rabbit IgG (H+L) Superclonal Secondary Antibody, HRP conjugate. Densitometric analysis of this western blot is shown in histogram (Fig b). Decrease in signal upon siRNA mediated knock down confirms that antibody is specific to LXR alpha/beta.
Knockdown of LXR alpha/beta was achieved by transfecting HeLa cells with LXR alpha/beta specific siRNAs. Western blot analysis (Fig a) was performed using whole cell extracts from LXR alpha/beta knock down cells (lane 3), non-specific scrambled siRNA transfected cells (lane 2) and untransfected cells (lane 1). The blots were probed with Anti- LXR alpha/beta Rabbit polyclonal Antibody and Goat anti-Rabbit IgG (H+L) Superclonal Secondary Antibody, HRP conjugate. Densitometric analysis of this western blot is shown in histogram (Fig b). Decrease in signal upon siRNA mediated knock down confirms that antibody is specific to LXR alpha/beta.

Western blot

Fig.1) Western blot analysis was performed on nuclear enriched extracts (30 µglysate) of MCF7 (Lane 1), HeLa (Lane 2), Hep G2 (Lane 3), Jurkat (Lane 4) and HEK-293 (Lane 5). Fig2.) Likewise, western blot analysis was performed on tissue extracts (30 µglysate) of Mouse Liver, Mouse Spleen and Mouse Lung. The blots were probed with LXR alpha/beta Rabbit polyclonal Antibody and detected by chemiluminescence using Goat anti-Rabbit IgG (H+L) Superclonal Secondary Antibody, HRP conjugate. A 40 kDa band corresponding to LXR beta was observed across the cell lines tested. Apart from this in Fig. 2, 50 kDa corresponding to LXR alpha form is also observed across all tissue extracts tested. Known quantity of protein samples were electrophoresed using 12 % Bis-Tris gel. Resolved proteins were then transferred onto a nitrocellulose membrane. The membrane was probed with the relevant primary and secondary Antibody following blocking with 5% skimmed milk.
Fig.1) Western blot analysis was performed on nuclear enriched extracts (30 µglysate) of MCF7 (Lane 1), HeLa (Lane 2), Hep G2 (Lane 3), Jurkat (Lane 4) and HEK-293 (Lane 5). Fig2.) Likewise, western blot analysis was performed on tissue extracts (30 µglysate) of Mouse Liver, Mouse Spleen and Mouse Lung. The blots were probed with LXR alpha/beta Rabbit polyclonal Antibody and detected by chemiluminescence using Goat anti-Rabbit IgG (H+L) Superclonal Secondary Antibody, HRP conjugate. A 40 kDa band corresponding to LXR beta was observed across the cell lines tested. Apart from this in Fig. 2, 50 kDa corresponding to LXR alpha form is also observed across all tissue extracts tested. Known quantity of protein samples were electrophoresed using 12 % Bis-Tris gel. Resolved proteins were then transferred onto a nitrocellulose membrane. The membrane was probed with the relevant primary and secondary Antibody following blocking with 5% skimmed milk.

Western blot

Antibody specificity was demonstrated by siRNA mediated knockdown of target protein. HeLa cells were transfected with LXR alpha/beta siRNA and loss of signal was observed in Western Blot using Anti-LXR alpha/beta Polyclonal Antibody.
Antibody specificity was demonstrated by siRNA mediated knockdown of target protein. HeLa cells were transfected with LXR alpha/beta siRNA and loss of signal was observed in Western Blot using Anti-LXR alpha/beta Polyclonal Antibody.

Western blot

Knockdown of LXR alpha/beta was achieved by transfecting HeLa cells with LXR alpha/beta specific siRNAs. Western blot analysis (Fig a) was performed using whole cell extracts from LXR alpha/beta knock down cells (lane 3), non-specific scrambled siRNA transfected cells (lane 2) and untransfected cells (lane 1). The blots were probed with Anti- LXR alpha/beta Rabbit polyclonal Antibody and Goat anti-Rabbit IgG (H+L) Superclonal Secondary Antibody, HRP conjugate. Densitometric analysis of this western blot is shown in histogram (Fig b). Decrease in signal upon siRNA mediated knock down confirms that antibody is specific to LXR alpha/beta.
Knockdown of LXR alpha/beta was achieved by transfecting HeLa cells with LXR alpha/beta specific siRNAs. Western blot analysis (Fig a) was performed using whole cell extracts from LXR alpha/beta knock down cells (lane 3), non-specific scrambled siRNA transfected cells (lane 2) and untransfected cells (lane 1). The blots were probed with Anti- LXR alpha/beta Rabbit polyclonal Antibody and Goat anti-Rabbit IgG (H+L) Superclonal Secondary Antibody, HRP conjugate. Densitometric analysis of this western blot is shown in histogram (Fig b). Decrease in signal upon siRNA mediated knock down confirms that antibody is specific to LXR alpha/beta.

Requested From: United States
Date Requested: 10/19/2018

Get Social With Us!
Follow us on Facebook Follow us on Google+ Follow us on LinkedIn PSL Alliance Member
Copyright © 2018 LifeSpan BioSciences, Inc. All Rights Reserved Privacy Policy