NK1R Antibody [J8D24] | Primary Antibodies

Application: Reactivity: Human

Usage Information

Dilution
WB1:500

Application
WB

Reactivity
Human

Source
Mouse Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
46 kDa ~80 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
NK1R Antibody [J8D24] detects endogenous levels of total NK1R protein.

Clone
J8D24

Synonym(s)
SPR, TAC1R, TACR1

Background
NK1R (neurokinin‑1 receptor; TACR1) is a class A G protein‑coupled receptor that serves as the high‑affinity receptor for the tachykinin neuropeptide substance P and functions as a central node linking neurogenic signaling to pain, stress responses, inflammation, and tumor biology across the nervous, immune, and cardiovascular systems. The receptor is a seven‑transmembrane glycoprotein with an extracellular N‑terminus that contributes to peptide recognition, three extracellular and three intracellular loops, and an intracellular C‑terminal tail enriched in serine/threonine residues and multiple regulatory motifs for G protein coupling, GRK phosphorylation, β‑arrestin binding, and internalization; high‑resolution cryo‑EM structures of substance P–bound NK1R in complex with Gq and Gs reveal that the peptide lies deep in the orthosteric pocket formed by transmembrane segments 2, 3, 6, and 7, with its C‑terminal hydrophobic motif engaging conserved aromatic residues and its N‑terminus interacting with extracellular loops, thereby stabilizing an active‑state conformation that accommodates distinct G‑protein coupling geometries. Ligand‑occupied NK1R primarily couples to Gq/11 to activate phospholipase Cβ, generating inositol 1,4,5‑trisphosphate and diacylglycerol, mobilizing intracellular and extracellular Ca²⁺ and activating PKC, while simultaneous or context‑dependent coupling to Gs stimulates adenylyl cyclase and cAMP–PKA signaling, and coupling to Gi/o, G12, and G13 engages additional second‑messenger pathways including PI3K–Akt, Rho/ROCK, phospholipase A2–arachidonic acid, and MAPK cascades, which together regulate transcription factors such as NF‑κB, AP‑1, and CREB and control cell survival, proliferation, migration, and cytokine production. NK1R is widely expressed on neurons of the central and peripheral nervous systems, where substance P binding drives nociceptive transmission, central sensitization, neurogenic inflammation, and activation of brainstem emetic centers in the nucleus tractus solitarius and area postrema, providing the mechanistic basis for the antiemetic efficacy of clinically used NK1R antagonists aprepitant and fosaprepitant in chemotherapy‑induced nausea and vomiting. The receptor is also constitutively or inducibly expressed on monocytes, macrophages, dendritic cells, T lymphocytes, neutrophils, mast cells, endothelial cells, and fibroblasts, where SP–NK1R signaling enhances chemotaxis, respiratory burst, degranulation, cytokine and chemokine release, and expression of adhesion molecules, establishing a neuro–immune axis that amplifies acute and chronic inflammation in disorders such as rheumatoid arthritis, inflammatory bowel disease, asthma, and neuroinflammatory conditions. NK1R undergoes rapid agonist‑dependent desensitization mediated by GRKs that phosphorylate the C‑terminal tail and promote β‑arrestin recruitment, which uncouples G proteins, drives receptor internalization, and initiates β‑arrestin–scaffolded signaling endosomes; biased ligands and non‑peptide antagonists can alter this balance by stabilizing inactive conformations that display “insurmountable antagonism” and long‑lasting blockade of SP responses, a property that contributes to their clinical antiemetic and potential antidepressant and analgesic actions. Overexpression and hyperactivation of NK1R are reported in numerous solid tumors and hematologic malignancies, where SP–NK1R signaling promotes tumor cell proliferation, survival, migration, angiogenesis, and metabolic reprogramming via sustained MAPK, PI3K–Akt, and NF‑κB activity and induction of pro‑angiogenic factors, placing NK1R as both a prognostic marker and a druggable driver in cancer; NK1R antagonists in preclinical models inhibit tumor growth and metastasis and induce apoptosis, supporting ongoing exploration of repurposed or next‑generation NK1R blockers as anticancer agents.

Background

NK1R (neurokinin‑1 receptor; TACR1) is a class A G protein‑coupled receptor that serves as the high‑affinity receptor for the tachykinin neuropeptide substance P and functions as a central node linking neurogenic signaling to pain, stress responses, inflammation, and tumor biology across the nervous, immune, and cardiovascular systems. The receptor is a seven‑transmembrane glycoprotein with an extracellular N‑terminus that contributes to peptide recognition, three extracellular and three intracellular loops, and an intracellular C‑terminal tail enriched in serine/threonine residues and multiple regulatory motifs for G protein coupling, GRK phosphorylation, β‑arrestin binding, and internalization; high‑resolution cryo‑EM structures of substance P–bound NK1R in complex with Gq and Gs reveal that the peptide lies deep in the orthosteric pocket formed by transmembrane segments 2, 3, 6, and 7, with its C‑terminal hydrophobic motif engaging conserved aromatic residues and its N‑terminus interacting with extracellular loops, thereby stabilizing an active‑state conformation that accommodates distinct G‑protein coupling geometries. Ligand‑occupied NK1R primarily couples to Gq/11 to activate phospholipase Cβ, generating inositol 1,4,5‑trisphosphate and diacylglycerol, mobilizing intracellular and extracellular Ca²⁺ and activating PKC, while simultaneous or context‑dependent coupling to Gs stimulates adenylyl cyclase and cAMP–PKA signaling, and coupling to Gi/o, G12, and G13 engages additional second‑messenger pathways including PI3K–Akt, Rho/ROCK, phospholipase A2–arachidonic acid, and MAPK cascades, which together regulate transcription factors such as NF‑κB, AP‑1, and CREB and control cell survival, proliferation, migration, and cytokine production. NK1R is widely expressed on neurons of the central and peripheral nervous systems, where substance P binding drives nociceptive transmission, central sensitization, neurogenic inflammation, and activation of brainstem emetic centers in the nucleus tractus solitarius and area postrema, providing the mechanistic basis for the antiemetic efficacy of clinically used NK1R antagonists aprepitant and fosaprepitant in chemotherapy‑induced nausea and vomiting. The receptor is also constitutively or inducibly expressed on monocytes, macrophages, dendritic cells, T lymphocytes, neutrophils, mast cells, endothelial cells, and fibroblasts, where SP–NK1R signaling enhances chemotaxis, respiratory burst, degranulation, cytokine and chemokine release, and expression of adhesion molecules, establishing a neuro–immune axis that amplifies acute and chronic inflammation in disorders such as rheumatoid arthritis, inflammatory bowel disease, asthma, and neuroinflammatory conditions. NK1R undergoes rapid agonist‑dependent desensitization mediated by GRKs that phosphorylate the C‑terminal tail and promote β‑arrestin recruitment, which uncouples G proteins, drives receptor internalization, and initiates β‑arrestin–scaffolded signaling endosomes; biased ligands and non‑peptide antagonists can alter this balance by stabilizing inactive conformations that display “insurmountable antagonism” and long‑lasting blockade of SP responses, a property that contributes to their clinical antiemetic and potential antidepressant and analgesic actions. Overexpression and hyperactivation of NK1R are reported in numerous solid tumors and hematologic malignancies, where SP–NK1R signaling promotes tumor cell proliferation, survival, migration, angiogenesis, and metabolic reprogramming via sustained MAPK, PI3K–Akt, and NF‑κB activity and induction of pro‑angiogenic factors, placing NK1R as both a prognostic marker and a druggable driver in cancer; NK1R antagonists in preclinical models inhibit tumor growth and metastasis and induce apoptosis, supporting ongoing exploration of repurposed or next‑generation NK1R blockers as anticancer agents.

References
https://pubmed.ncbi.nlm.nih.gov/34878828/ https://pubmed.ncbi.nlm.nih.gov/26421291/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%