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Mouse Anti-LEPR Recombinant Antibody (CBXS-4566) (CBMAB-S1806-CQ)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBXS-4566
Antibody Isotype
IgG1
Application
FC, IA, IHC-P

Basic Information

Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.1% BSA
Preservative
0.02% sodium azide
Concentration
0.1 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Introduction
The protein encoded by this gene belongs to the gp130 family of cytokine receptors that are known to stimulate gene transcription via activation of cytosolic STAT proteins. This protein is a receptor for leptin (an adipocyte-specific hormone that regulates body weight), and is involved in the regulation of fat metabolism, as well as in a novel hematopoietic pathway that is required for normal lymphopoiesis. Mutations in this gene have been associated with obesity and pituitary dysfunction. Alternatively spliced transcript variants encoding different isoforms have been described for this gene. It is noteworthy that this gene and LEPROT gene (GeneID:54741) share the same promoter and the first 2 exons, however, encode distinct proteins (PMID:9207021).
Entrez Gene ID
3953
UniProt ID
P48357
Alternative Names
CD295; LEP-R; LEPRD; OB-R; OBR
Function
Receptor for hormone LEP/leptin (Probable) (PubMed:22405007).
On ligand binding, mediates LEP central and peripheral effects through the activation of different signaling pathways such as JAK2/STAT3 and MAPK cascade/FOS. In the hypothalamus, LEP acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones (By similarity) (PubMed:9537324).
In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic and affects innate and adaptive immunity (PubMed:25060689, PubMed:12504075, PubMed:8805376).
Control of energy homeostasis and melanocortin production (stimulation of POMC and full repression of AgRP transcription) is mediated by STAT3 signaling, whereas distinct signals regulate NPY and the control of fertility, growth and glucose homeostasis. Involved in the regulation of counter-regulatory response to hypoglycemia by inhibiting neurons of the parabrachial nucleus. Has a specific effect on T lymphocyte responses, differentially regulating the proliferation of naive and memory T -ells. Leptin increases Th1 and suppresses Th2 cytokine production (By similarity).
Isoform A
May transport LEP across the blood-brain barrier. Binds LEP and mediates LEP endocytosis. Does not induce phosphorylation of and activate STAT3.
Isoform E
Antagonizes Isoform A and isoform B-mediated LEP binding and endocytosis.
Biological Process
AngiogenesisManual Assertion Based On ExperimentIMP:UniProtKB
Bone growthISS:UniProtKB
Cell surface receptor signaling pathwayManual Assertion Based On ExperimentTAS:ProtInc
Cholesterol metabolic processIEA:Ensembl
Cytokine-mediated signaling pathwayManual Assertion Based On ExperimentIBA:GO_Central
Energy homeostasisISS:UniProtKB
Energy reserve metabolic processManual Assertion Based On ExperimentTAS:ProtInc
Glial cell proliferationIEA:Ensembl
Glucose homeostasisISS:UniProtKB
Glycogen metabolic processIEA:Ensembl
Leptin-mediated signaling pathwayManual Assertion Based On ExperimentIDA:ARUK-UCL
Multicellular organism developmentManual Assertion Based On ExperimentTAS:ProtInc
Negative regulation of autophagyManual Assertion Based On ExperimentIDA:UniProtKB
Negative regulation of gluconeogenesisIEA:Ensembl
Negative regulation of hydrolase activityIEA:Ensembl
PhagocytosisIEA:Ensembl
Positive regulation of cold-induced thermogenesisBy SimilarityISS:YuBioLab
Positive regulation of protein phosphorylationManual Assertion Based On ExperimentIDA:ARUK-UCL
Regulation of bone remodelingISS:UniProtKB
Regulation of feeding behaviorISS:UniProtKB
Regulation of transportManual Assertion Based On ExperimentIDA:ARUK-UCL
Response to leptinISS:UniProtKB
Sexual reproductionISS:UniProtKB
T cell differentiationISS:UniProtKB
Transport across blood-brain barrier2 PublicationsNAS:ARUK-UCL
Cellular Location
Cell membrane
Basolateral cell membrane
Isoform E:
Secreted
Involvement in disease
Leptin receptor deficiency (LEPRD):
A rare disease characterized by normal levels of serum leptin, hyperphagia and severe obesity from an early age. Additional features include alterations in immune function, and delayed puberty due to hypogonadotropic hypogonadism.
Topology
Extracellular: 22-839
Helical: 840-862
Cytoplasmic: 863-1165
PTM
On ligand binding, phosphorylated on two conserved C-terminal tyrosine residues (isoform B only) by JAK2. Tyr-986 is required for complete binding and activation of PTPN11, ERK/FOS activation,for interaction with SOCS3 and SOCS3 mediated inhibition of leptin signaling. Phosphorylation on Tyr-1141 is required for STAT3 binding/activation. Phosphorylation of Tyr-1079 has a more accessory role.
More Infomation

Saxton, R. A., Caveney, N. A., Moya-Garzon, M. D., Householder, K. D., Rodriguez, G. E., Burdsall, K. A., ... & Garcia, K. C. (2023). Structural insights into the mechanism of leptin receptor activation. Nature Communications, 14(1), 1797.

Perge, K., Pons, L., Protsenko, N., Collin-Chavagnac, D., & Nicolino, M. (2023). A Novel Leptin Receptor LEPR Variant in a Toddler With Early-Onset Fatal Obesity. Pediatrics, 152(1), e2022059569.

Atawia, R. T., Faulkner, J. L., Mehta, V., Austin, A., Jordan, C. R., Kennard, S., & De Chantemele, E. J. B. (2022). Endothelial leptin receptor is dispensable for leptin-induced sympatho-activation and hypertension in male mice. Vascular Pharmacology, 146, 107093.

Butiaeva, L. I., Slutzki, T., Swick, H. E., Bourguignon, C., Robins, S. C., Liu, X., ... & Kokoeva, M. V. (2021). Leptin receptor-expressing pericytes mediate access of hypothalamic feeding centers to circulating leptin. Cell Metabolism, 33(7), 1433-1448.

Trinh, T., & Broxmeyer, H. E. (2021). Role for leptin and leptin receptors in stem cells during health and diseases. Stem Cell Reviews and Reports, 17, 511-522.

Voigtmann, F., Wolf, P., Landgraf, K., Stein, R., Kratzsch, J., Schmitz, S., ... & Körner, A. (2021). Identification of a novel leptin receptor (LEPR) variant and proof of functional relevance directing treatment decisions in patients with morbid obesity. Metabolism, 116, 154438.

Kleinendorst, L., Abawi, O., van der Kamp, H. J., Alders, M., Meijers-Heijboer, H. E., van Rossum, E. F., ... & van Haelst, M. M. (2020). Leptin receptor deficiency: a systematic literature review and prevalence estimation based on population genetics. European journal of endocrinology, 182(1), 47-56.

Nunziata, A., Funcke, J. B., Borck, G., von Schnurbein, J., Brandt, S., Lennerz, B., ... & Wabitsch, M. (2019). Functional and phenotypic characteristics of human leptin receptor mutations. Journal of the Endocrine Society, 3(1), 27-41.

Al-Shibli, S. M., Harun, N., Ashour, A. E., Kasmuri, M. H. B. M., & Mizan, S. (2019). Expression of leptin and leptin receptors in colorectal cancer—an immunohistochemical study. PeerJ, 7, e7624.

Nowzari, Z., Masoumi, M., Nazari-Robati, M., Akbari, H., Shahrokhi, N., & Asadikaram, G. (2018). Association of polymorphisms of leptin, leptin receptor and apelin receptor genes with susceptibility to coronary artery disease and hypertension. Life sciences, 207, 166-171.

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For research use only. Not intended for any clinical use.

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