Mouse Anti-UMOD Recombinant Antibody (CBYJT-5572) (CBMAB-T5205-YJ)

Mouse

Human

CBYJT-5572

IgG2b

ELISA, IHC-P

Human

IgG2b

Monoclonal

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Ascites

Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Uromodulin

UMOD is the most abundant protein in mammalian urine under physiological conditions. Its excretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. UMOD may act as a constitutive inhibitor of calcium crystallization in renal fluids. Excretion of this protein in urine may provide defense against urinary tract infections caused by uropathogenic bacteria. Defects in UMOD are associated with the renal disorders medullary cystic kidney disease-2 (MCKD2), glomerulocystic kidney disease with hyperuricemia and isosthenuria (GCKDHI), and familial juvenile hyperuricemic nephropathy (FJHN).

Uromodulin; Tamm-Horsfall Urinary Glycoprotein; Uromucoid; THP; Uromodulin (Uromucoid, Tamm-Horsfall Glycoprotein); Tamm-Horsfall Glycoprotein; ADMCKD2

Uromodulin
Functions in biogenesis and organization of the apical membrane of epithelial cells of the thick ascending limb of Henle's loop (TALH), where it promotes formation of complex filamentous gel-like structure that may play a role in the water barrier permeability (Probable). May serve as a receptor for binding and endocytosis of cytokines (IL-1, IL-2) and TNF (PubMed:3498215).
Facilitates neutrophil migration across renal epithelia (PubMed:20798515).
Uromodulin, secreted form
In the urine, may contribute to colloid osmotic pressure, retards passage of positively charged electrolytes, and inhibits formation of liquid containing supersaturated salts and subsequent formation of salt crystals (By similarity).
Protects against urinary tract infections by binding to type 1 fimbriated E.coli (PubMed:11134021, PubMed:32616672).
Binds to bacterial adhesin fimH which mediates the stable formation of bacterial aggregates, prevents the binding of E.coli to uroplakins UPK1A and UPK1B which act as urothelial receptors for type I fimbriae, and allows for pathogen clearance through micturation (PubMed:11134021, PubMed:32616672).
Also promotes aggregation of other bacteria including K.pneumoniae, P.aeruginosa and S.mitis and so may also protect against other uropathogens (PubMed:32616672).

Biological Process antibacterial innate immune response Source:UniProtKB1 Publication
Biological Process apoptotic signaling pathway Source:Ensembl
Biological Process autophagy Source:Ensembl
Biological Process cellular calcium ion homeostasis Source:Ensembl
Biological Process cellular chloride ion homeostasis Source:Ensembl
Biological Process cellular defense response Source:ProtInc1 Publication
Biological Process cellular phosphate ion homeostasis Source:Ensembl
Biological Process cellular response to unfolded protein Source:Ensembl
Biological Process cellular sodium ion homeostasis Source:Ensembl
Biological Process chaperone-mediated protein folding Source:Ensembl
Biological Process citric acid secretion Source:Ensembl
Biological Process collecting duct development Source:Ensembl
Biological Process connective tissue replacement Source:Ensembl
Biological Process creatinine homeostasis Source:Ensembl
Biological Process defense response to Gram-negative bacterium Source:UniProtKB1 Publication
Biological Process endoplasmic reticulum organization Source:Ensembl
Biological Process glomerular filtration Source:Ensembl
Biological Process heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source:BHF-UCL1 Publication
Biological Process inflammatory response Source:Ensembl
Biological Process juxtaglomerular apparatus development Source:Ensembl
Biological Process leukocyte cell-cell adhesion Source:BHF-UCL1 Publication
Biological Process lipid metabolic process Source:Ensembl
Biological Process metanephric ascending thin limb development Source:Ensembl
Biological Process metanephric distal convoluted tubule development Source:Ensembl
Biological Process metanephric thick ascending limb development Source:Ensembl
Biological Process micturition Source:Ensembl
Biological Process multicellular organismal response to stress Source:Ensembl
Biological Process negative regulation of cell population proliferation Source:ProtInc1 Publication
Biological Process neutrophil migration Source:BHF-UCL1 Publication
Biological Process organ or tissue specific immune response Source:Ensembl
Biological Process peptidyl-threonine phosphorylation Source:Ensembl
Biological Process potassium ion homeostasis Source:Ensembl
Biological Process protein localization to vacuole Source:Ensembl
Biological Process protein transport into plasma membrane raft Source:Ensembl
Biological Process regulation of blood pressure Source:Ensembl
Biological Process regulation of protein transport Source:Ensembl
Biological Process regulation of urine volume Source:Ensembl
Biological Process renal sodium ion absorption Source:Ensembl
Biological Process renal urate salt excretion Source:Ensembl
Biological Process renal water homeostasis Source:Ensembl
Biological Process response to lipopolysaccharide Source:Ensembl
Biological Process response to water deprivation Source:Ensembl
Biological Process response to xenobiotic stimulus Source:Ensembl
Biological Process RNA splicing Source:Ensembl
Biological Process tumor necrosis factor-mediated signaling pathway Source:Ensembl
Biological Process ubiquitin-dependent ERAD pathway Source:Ensembl
Biological Process urate transport Source:Ensembl
Biological Process urea transmembrane transport Source:Ensembl

Apical cell membrane
Basolateral cell membrane
Cell projection, cilium membrane
Only a small fraction sorts to the basolateral pole of tubular epithelial cells compared to apical localization (PubMed:22776760).
Secreted into urine after cleavage (PubMed:18375198, PubMed:26811476).
Colocalizes with NPHP1 and KIF3A (PubMed:20172860).
Uromodulin, secreted form
Secreted
Detected in urine.

Tubulointerstitial kidney disease, autosomal dominant, 1 (ADTKD1):
A form of autosomal dominant tubulointerstitial kidney disease, a genetically heterogeneous disorder characterized by slowly progressive loss of kidney function, bland urinary sediment, hyperuricemia, absent or mildly increased albuminuria, lack of severe hypertension during the early stages, and normal or small kidneys on ultrasound. Renal histology shows variable abnormalities including interstitial fibrosis with tubular atrophy, microcystic dilatation of the tubules, thickening of tubular basement membranes, medullary cysts, and secondary glomerulosclerotic or glomerulocystic changes with abnormal glomerular tufting. There is significant variability, as well as incomplete penetrance.

N-glycosylated (PubMed:19005207, PubMed:26673890, PubMed:26811476, PubMed:32815518, PubMed:33196145).
N-glycan heterogeneity at Asn-232: Hex7HexNAc6 (major) and dHex1Hex7HexNAc6 (minor); at Asn-322: dHex1Hex6HexNAc5 (minor), dHex1Hex7HexNAc6 (major) and dHex1Hex8HexNAc7 (minor); at Asn-396: Hex6HexNAc5 (major), dHex1Hex6HexNAc5 (minor) and Hex7HexNAc6 (minor) (PubMed:22171320).
Glycosylated Asn-232 interacts with E.coli adhesin fimH (PubMed:32616672).
Other complex glycosylation sites may serve as binding sites for proteins from other bacteria inclduding K.pneumoniae, P.aeruginosa and S.mitis (PubMed:32616672).
Proteolytically cleaved at a conserved C-terminal proteolytic cleavage site to generate the secreted form found in urine (PubMed:18375198, PubMed:19005207).
This cleavage is catalyzed by HPN (PubMed:26673890).