• Official Full Name

    lymphotoxin beta receptor (TNFR superfamily, member 3)

  • Overview

    The protein encoded by this gene is a member of the tumor necrosis factor (TNF) family of receptors. It is expressed on the surface of most cell types, including cells of epithelial and myeloid lineages, but not on T and B lymphocytes. The protein specifically binds the lymphotoxin membrane form (a complex of lymphotoxin-alpha and lymphtoxin-beta). The encoded protein and its ligand play a role in the development and organization of lymphoid tissue and tranformed cells. Activation of the encoded protein can trigger apoptosis.
  • Synonyms

    LTBR; lymphotoxin beta receptor (TNFR superfamily, member 3); D12S370; tumor necrosis factor receptor superfamily member 3; TNF R III; TNFCR; TNFR RP; TNFR2 RP; TNFRSF3; CD 18; CD18; CD18 antigen; LT beta R; LTBETAR; Lymphotoxin B receptor; Lymphotoxin beta receptor; TNFR superfamily member 3; TNFR2RP; TNFRII; TNFRRP; TNFRSF 3; Tumor necrosis factor C receptor; Tumor necrosis factor receptor 2 related protein; Tumor necrosis factor receptor superfamily member 3 precursor; TNF-RIII; TNFR-III; OTTHUMP00000238625; OTTHUMP00000238626; lymphotoxin-beta receptor; TNFR superfamily, member 3; tumor necrosis factor receptor type II; TNFR-RP; TNFR2-RP; LT-BETA-R; TNF-R-III;

  • Recombinant Proteins
  • Antibody
  • Protein Pre-coupled Magnetic Beads
  • Cell & Tissue Lysates
  • Cynomolgus
  • Cynomolgus Monkey
  • Homo sapiens (Human)
  • Human
  • Mouse
  • Rat
  • Rhesus Macaque
  • CHO
  • E.coli
  • E.coli expression system
  • HEK293
  • HEK293 Cells
  • Human Cell
  • In Vitro Cell Free System
  • Mammalian Cell
  • Mammalian cells
  • Mouse
  • Wheat Germ
  • C
  • Fc
  • hFc
  • Fc Chimera
  • His(C
  • ter)
  • GST
  • His
  • His (Fc)
  • Avi
  • His|GST
  • human|IgG1|Fc
  • N/A
  • N
Species Cat.# Product name Source (Host) Tag Protein Length Price
Human LTBR-745H Active Recombinant Human LTBR, Fc Chimera Mammalian cells Fc Chimera
Human LTBR-633H Active Recombinant Human LTBR, MIgG2a Fc-tagged CHO Fc
Human LTBR-635H Active Recombinant Human LTBR protein, Fc-tagged CHO Fc Gln31-Met225
Human LTBR-746H Active Recombinant Human LTBR, Fc Chimera CHO Fc Chimera
Human LTBR-634H Active Recombinant Human LTBR, HIgG1 Fc-tagged CHO Fc
Human LTBR-636H Active Recombinant Human LTBR, Fc-tagged, Biotinylated Human Cell Fc
Human LTBR-961HB Active Recombinant Human LTBR protein, His-Avi-tagged, Biotinylated HEK293 His-Avi Gln 31 - Met 227
Human LTBR-960H Recombinant Human LTBR Protein, His-tagged HEK293 His
Human LTBR-2683H Recombinant Human LTBR protein, His-tagged E.coli His Thr66~Glu215 (Accession # P36941)
Human LTBR-398H Active Recombinant Human LTBR, Fc-tagged CHO Fc
Human LTBR-2090H Recombinant Human LTBR, FC Chimera HEK293 Fc
Human LTBR-1665H Recombinant Human LTBR, His-tagged Mammalian cells His
Human LTBR-674H Recombinant Human lymphotoxin beta receptor (TNFR superfamily, member 3), His-tagged E.coli His
Human LTBR-4589H Recombinant Human LTBR Protein, GST-tagged Wheat Germ GST
Human LTBR-1752H Recombinant Human LTBR Protein, His&GST-tagged E.coli N-His&GST Thr66-Glu215
Human DMABT-H19157 Mouse Anti-LTBR Monoclonal Antibody Mouse N/A
Human LTBR-190H Recombinant Human LTBR protein, Fc-tagged HEK293 Cells Fc Gln31-Met227
Human LTBR-5243H Recombinant Human LTBR protein, His-tagged E.coli His 31-224aa
Human LTBR-235H Recombinant Human LTBR Protein (ECD), Fc-His-tagged(C-ter) HEK293 Fc-His(C-ter) Gln31-Met227
Human LTBR-200H-B Recombinant Human LTBR Protein Pre-coupled Magnetic Beads HEK293
Human LTBR-200H Recombinant Human LTBR Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
Human LTBR-1840H Recombinant Human LTBR protein, His-tagged, PE Labeled HEK293 His Gln 31 - Met 227
Human LTBR-369H Recombinant Human LTBR Protein, Fc-tagged HEK293 Fc 435
Human LTBR-399H Recombinant Human LTBR protein, Fc-tagged HEK293 human/IgG1/Fc 197
Human LTBR-0360H Active Recombinant Human LTBR protein, Fc-tagged HEK293 Fc Gln31-Met227
Human LTBR-4467H Recombinant Human LTBR Protein (Gln31-Met227), N-His tagged E.coli N-His Gln31-Met227
Human LTBR-4466H Recombinant Human LTBR Protein (Gln31-Met227), C-Fc tagged Mammalian cells C-Fc Gln31-Met227
Human LTBR-8493H Recombinant Human LTBR Protein, Fc-tagged CHO Fc
Human LTBR-6208HF Recombinant Full Length Human LTBR Protein, GST-tagged In Vitro Cell Free System GST 31-435 amino acids
Mouse LTBR-4557M Active Recombinant Mouse LTBR, MIgG2a Fc-tagged CHO Fc
Mouse LTBR-4556M Active Recombinant Mouse LTBR, MIgG2a Fc-tagged, mutant CHO Fc
Mouse Ltbr-1219M Active Recombinant Mouse Ltbr Protein, Fc-tagged HEK293 Fc Ser28-Pro218
Mouse Ltbr-2684M Recombinant Mouse Ltbr protein, His & GST-tagged E.coli His/GST Pro128~Tyr395
Mouse Ltbr-1751M Recombinant Mouse Ltbr Protein, His-tagged E.coli N-His Gln31-Leu223
Rat Ltbr-381R Recombinant Rat Ltbr protein, His-tagged HEK293 His Met 1-Ala 218
Rat LTBR-380R Recombinant Rat Ltbr, Fc tagged Human Cell His
Rat LTBR-1052RCL Recombinant Rat LTBR cell lysate Human Cell N/A
Rat LTBR-1288R Recombinant Rat LTBR protein(Met1-Ala218), hFc-tagged HEK293 C-hFc Met1-Ala218
Cynomolgus LTBR-8827C Recombinant Cynomolgus LTBR protein, hFc-tagged HEK293 hFc Met1-Met225
Cynomolgus Monkey LTBR-1229CCL Recombinant Cynomolgus LTBR cell lysate Human Cell N/A
Homo sapiens (Human) RFL35243HF Recombinant Full Length Human Tumor Necrosis Factor Receptor Superfamily Member 3(Ltbr) Protein, His-Tagged E.coli expression system His Full Length (31-435)
Rhesus Macaque LTBR-2591R Recombinant Rhesus monkey LTBR Protein, His-tagged Mammalian Cell His
Rhesus Macaque LTBR-2411R-B Recombinant Rhesus Macaque LTBR Protein Pre-coupled Magnetic Beads HEK293
Rhesus Macaque LTBR-2411R Recombinant Rhesus Macaque LTBR Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
  • Background
  • Quality Guarantee
  • Case Study
  • Involved Pathway
  • Protein Function
  • Interacting Protein
  • Other Resource
  • LTBR Related Signal Pathway

Fig1. The α–β and β–β' binding sites are essential for signaling. (Jawahar Sudhamsu, 2013)

What is LTBR protein?

LTBR (lymphotoxin beta receptor) gene is a protein coding gene which situated on the short arm of chromosome 12 at locus 12p13. The protein encoded by this gene is a member of the tumor necrosis factor (TNF) family of receptors. It is expressed on the surface of most cell types, including cells of epithelial and myeloid lineages, but not on T and B lymphocytes. The protein specifically binds the lymphotoxin membrane form (a complex of lymphotoxin-alpha and lymphtoxin-beta). The LTBR protein is consisted of 435 amino acids and its molecular mass is approximately 46.7 kDa.

What is the function of LTBR protein?

LTBR plays a role in signalling during the development of lymphoid and other organs, lipid metabolism, immune response, and programmed cell death. Activity of this receptor has also been linked to carcinogenesis. The LTBR activates two different NF-κB pathways that lead to distinct patterns of gene induction, including selected chemokines, and the cytokine BAFF, which is essential for the survival of mature B lymphocytes. LTBR activates the classical NF-κB (relA/p50) pathway, like the type 1 TNF receptor (TNFR1), that regulates proinflammatory genes, like the chemokine MIP1β. However, LTBR, unlike TNFR1, also activates the processing of p100 to form RelB/p52 complexes, which activate genes involved in lymphoid organ formation and lymphocyte survival.

LTBR Related Signaling Pathway

Lβr activates the downstream NF-κB signaling pathway by binding to its ligand. It can also interact with other signal transduction molecules, such as TRAF2, TRAF6, etc., to regulate the activity of a variety of signal pathways. Activation of LβR activates the MAPK pathway by activating MAP3K, MAP2K, and MAPK cascases. The activated MAPK pathway can further activate multiple transcription factors and cytokines, which are involved in cell proliferation, survival and inflammation. Activation of LβR can lead to activation of JAK kinase, which phosphorylates STAT protein, thereby activating the JAK-STAT pathway.

LTBR Related Diseases

Lβr protein is related to the occurrence and development of tumors, and its abnormal expression may participate in the immune escape and angiogenesis of tumors, such as liver cancer, lung cancer, breast cancer, etc. Dysfunctional LTBR is likely to lead to abnormal activation of immune cells and inflammatory response, leading to allergic diseases, infectious diseases and transplant rejection. Deficiencies in the LβR protein can lead to immune dysfunction and susceptibility to infections, such as the two types of inherited immunodeficiency, HIM (hyper IgM syndrome) and CVID (common variable immunodeficiency), and other autoimmune diseases.

Bioapplications of LTBR

The specific uses and effects of LβR protein in these application areas are still being studied, and some applications have not yet been used clinically. For example, it is used as a therapeutic target for immune, anti-inflammatory and anti-tumor research, as well as a marker for new drug screening and disease detection.

High Purity



Fig2. Activity Data. (LTBR-399H)

Case study 1: Małgorzata Maksymowicz, 2020

At the cellular level, upon ligand binding, the receptor activates the pro-inflammatory NF-κB and AP-1 pathways. Yet, the intracellular distribution of LTβR, the routes of its endocytosis and their connection to the signaling activation are not characterized. Here, the researchers investigated the contribution of LTβR internalization to its signaling potential.

Intracellular localization of LTβR in unstimulated and stimulated cells was analyzed by confocal microscopy. Endocytosis impairment was achieved through siRNA- or CRISPR/Cas9-mediated depletion, or chemical inhibition of proteins regulating endocytic routes. The activation of LTβR-induced signaling was examined. A transcriptional response to LTβR stimulation was assessed by qRT-PCR analysis. The results showed that LTβR was predominantly present on endocytic vesicles and the Golgi apparatus. Depletion of regulators of different endocytic routes (clathrin-mediated, dynamin-dependent or clathrin-independent) resulted in the impairment of LTβR internalization, indicating that this receptor uses multiple entry pathways. This work shows that the impairment of clathrin- and dynamin-dependent internalization amplifies a cellular response to LTβR stimulation.


Fig1. A549 cells were stimulated with Ago for the indicated time periods and immunostained for LTβR, trans- (TGN46) and cis-Golgi (GM130).

Fig2. Lysates of A549 cells stimulated with: Ago, LTα1β2 and LIGHT for different time periods were analyzed by Western blotting with antibodies against the indicated proteins to assess activity of the NF-κB pathway.

Case study 2: Magdalena Banach-Orłowska, 2018

The researchers previously demonstrated that depletion of ESCRT components leads to endosomal accumulation of TNFRI and LTβR, and their ligand-independent signaling to NF-κB. Here, they studied if other perturbations of the endolysosomal system could trigger intracellular accumulation and signaling of ligand-free LTβR.

While depletion of CORVET had no effect, knockdown of HOPS or Rab7, or pharmacological inhibition of lysosomal degradation, caused endosomal accumulation of LTβR and its increased interactions with TRAF2/TRAF3 signaling adaptors. And the LTβR sequestration in intraluminal vesicles of endosomes precluded NF-κB signaling. Sequestration of LTβR in intraluminal vesicles of endosomes upon depletion of HOPS components or Rab7 precludes NF-κB signaling, whereas LTβR accumulation on the outer endosomal membrane after ESCRT depletion promotes signaling.


Fig3. Immunofluorescence staining of LTβR, EEA1 and LAMP1 in HeLa cells upon knockdown of Vps16 or Vps18 and in control (Ctrl) siRNA-transfected cells.

Fig4. (Left panel) Western blot analysis of immunoprecipitation (IP) of LTβR in extracts of HeLa cells transfected with non-targeting (Ctrl) or Rab7- and Vps11-targeting siRNA.

Fig1. Model of the different LTβR topology and signaling upon dysfunction of various trafficking regulators. (Magdalena Banach-Orłowska, 2018)


Fig2. LTβR was predominantly present on endocytic vesicles and the Golgi apparatus. (Małgorzata Maksymowicz, 2020)

LTBR involved in several pathways and played different roles in them. We selected most pathways LTBR participated on our site, such as Cytokine-cytokine receptor interaction, NF-kappa B signaling pathway, HIF- signaling pathway, which may be useful for your reference. Also, other proteins which involved in the same pathway with LTBR were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

Pathway Name Pathway Related Protein
Cytokine-cytokine receptor interactionCSF1RA;CSF2RA;IRX1;IL7;TNFRSF13B;IFNG1-2;ACVR1BA;NGFR;CXCL12B
HIF- signaling pathwayARNT;MKNK1;ANGPT4;MAPK3;PFKFB3;PIK3R2;INS2;BCL2;EP300
ne network for IgA productionCCL28;Icosl;CXCR4A;BMA1;IL-15RA;TGFB1;MHC2DCB;HLA-DRB1;ITGB7

LTBR has several biochemical functions, for example, identical protein binding, protein binding, tumor necrosis factor-activated receptor activity. Some of the functions are cooperated with other proteins, some of the functions could acted by LTBR itself. We selected most functions LTBR had, and list some proteins which have the same functions with LTBR. You can find most of the proteins on our site.

Function Related Protein
identical protein bindingCIDEB;MCPH1;SP100;ENTPD2;CLDN7;SOD1;KCNJ10;ZBTB16;GRB7
tumor necrosis factor-activated receptor activityTNFRSF1A;TNFRSF21;RELT;TNFRSF9A;TNFRSFA;TNFRSF25;HDR;NGFRB;TNFRSF6B
ubiquitin protein ligase bindingASB4;TUBB;RIPK1;UBE2A;DNM1L;DERL1;GABARAPL2;BLZF1;FAF1

LTBR has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with LTBR here. Most of them are supplied by our site. Hope this information will be useful for your research of LTBR.

p29846-pro_0000037666; ZMYND11; DEAF1; TRAF2; TRAF3; BALF4 (provisional); HES1; q00653-pro_000003032; Bmpr1a; NFKB2

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        Q&As (7)

        Ask a question
        What therapeutic strategies can be employed to target LTBR? 12/18/2022

        Therapeutic strategies targeting LTBR include inhibition of its signaling pathways, modulation of immune response, and anti-cancer approaches. Inhibitors of the NF-κB pathway, such as small molecule inhibitors or neutralizing antibodies, can be used to block LTBR-mediated signaling and reduce inflammation or tumor growth.

        What is the current research focus regarding the role of LTBR in disease mechanisms? 11/12/2021

        Current research on LTBR aims to further elucidate its role in disease mechanisms, particularly in autoimmune disorders, chronic inflammation, and cancer. Studies are investigating the downstream effects of LTBR activation, its involvement in immune cell function, and the identification of potential therapeutic targets within the LTBR signaling pathway.

        How is the expression of LTBR regulated at the transcriptional level? 06/26/2021

        The expression of LTBR is regulated by transcription factors and signaling pathways. For example, NF-κB and AP-1 transcription factors can bind to the promoter region of LTBR gene and enhance its expression. Additionally, cytokines and growth factors can also influence LTBR expression through downstream signaling cascades.

        How does the LTBR signaling pathway interact with other signaling pathways? 07/18/2020

        The LTBR signaling pathway interacts with various other signaling pathways, including those activated by TNFR1, TNFR2, and CD40. These interactions can lead to crosstalk and amplification of signaling, resulting in enhanced cellular responses. Understanding these interactions is crucial for elucidating the complex network of signaling events involved in disease pathogenesis.

        What is the biological function of LTBR and its involvement in cellular processes? 04/13/2018

        LTBR, a membrane protein belonging to the tumor necrosis factor receptor superfamily, regulates various cellular processes such as inflammation, immune response, and lymphoid organ development. It activates signaling pathways including the NF-κB pathway and non-canonical NF-κB pathway.

        Are there any genetic variants associated with LTBR expression and disease susceptibility? 01/06/2017

        Yes, certain genetic variants have been identified that are associated with altered LTBR expression and disease susceptibility. These variants can affect the binding of transcription factors or alter the stability of LTBR mRNA, leading to dysregulation of LTBR expression and increased risk of certain diseases.

        What are the potential future directions in LTBR research? 11/21/2016

        Future research directions in LTBR include exploring the molecular mechanisms underlying LTBR-mediated signaling, investigating the impact of LTBR genetic variants on disease susceptibility, and developing novel therapeutic strategies targeting LTBR. Additionally, studying the interplay between LTBR and other signaling pathways may uncover new insights into disease pathogenesis and identify new therapeutic avenues.

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