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LearnNBP1-45057
antibody from Novus Biologicals
Targeting: FOLH1
FOLH, GCP2, GCPII, NAALAD1, NAALAdase, PSM, PSMA
Western blot
ImmunocytochemistryAntibody data
- Antibody Data
- Antigen structure
- References [8]
- Comments [0]
- Validations
- Western blot [2]
- Immunohistochemistry [3]
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- Product number
- NBP1-45057 - Provider product page
- Provider
- Novus Biologicals
- Proper citation
- Novus Cat#NBP1-45057, RRID:AB_10008698
- Product name
- Mouse Monoclonal PSMA/FOLH1/NAALADase I Antibody
- Antibody type
- Monoclonal
- Description
- Protein A purified. The antibody GCP-04 recognizes amino acids 100-104 of extracellular domain of denaturated glutamate carboxypeptidase II (PSMA, NAALADase, FOLH1), an approximately 95-110 kDa transmembrane glycoprotein.
- Reactivity
- Human, Mouse, Rat, Porcine
- Host
- Mouse
- Isotype
- IgG
- Vial size
- 0.1 mg
- Concentration
- 1.0 mg/ml
- Storage
- Store at 4C. Do not freeze.
Submitted references High uptake of (68)Ga-PSMA and (18)F-DCFPyL in the peritumoral area of rat gliomas due to activated astrocytes.
Overexpression of prostate specific membrane antigen by canine hemangiosarcoma cells provides opportunity for the molecular detection of disease burdens within hemorrhagic body cavity effusions.
Tissue expression and enzymologic characterization of human prostate specific membrane antigen and its rat and pig orthologs.
Expression of glutamate carboxypeptidase II in human brain.
Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity.
Amino acids at the N- and C-termini of human glutamate carboxypeptidase II are required for enzymatic activity and proper folding.
Substrate specificity, inhibition and enzymological analysis of recombinant human glutamate carboxypeptidase II.
Substrate specificity, inhibition and enzymological analysis of recombinant human glutamate carboxypeptidase II.
Oliveira D, Stegmayr C, Heinzel A, Ermert J, Neumaier B, Shah NJ, Mottaghy FM, Langen KJ, Willuweit A
EJNMMI research 2020 May 25;10(1):55
EJNMMI research 2020 May 25;10(1):55
Overexpression of prostate specific membrane antigen by canine hemangiosarcoma cells provides opportunity for the molecular detection of disease burdens within hemorrhagic body cavity effusions.
Dowling M, Samuelson J, Fadl-Alla B, Pondenis HC, Byrum M, Barger AM, Fan TM
PloS one 2019;14(1):e0210297
PloS one 2019;14(1):e0210297
Tissue expression and enzymologic characterization of human prostate specific membrane antigen and its rat and pig orthologs.
Rovenská M, Hlouchová K, Sácha P, Mlcochová P, Horák V, Zámecník J, Barinka C, Konvalinka J
The Prostate 2008 Feb 1;68(2):171-82
The Prostate 2008 Feb 1;68(2):171-82
Expression of glutamate carboxypeptidase II in human brain.
Sácha P, Zámecník J, Barinka C, Hlouchová K, Vícha A, Mlcochová P, Hilgert I, Eckschlager T, Konvalinka J
Neuroscience 2007 Feb 23;144(4):1361-72
Neuroscience 2007 Feb 23;144(4):1361-72
Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity.
Barinka C, Sácha P, Sklenár J, Man P, Bezouska K, Slusher BS, Konvalinka J
Protein science : a publication of the Protein Society 2004 Jun;13(6):1627-35
Protein science : a publication of the Protein Society 2004 Jun;13(6):1627-35
Amino acids at the N- and C-termini of human glutamate carboxypeptidase II are required for enzymatic activity and proper folding.
Barinka C, Mlcochová P, Sácha P, Hilgert I, Majer P, Slusher BS, Horejsí V, Konvalinka J
European journal of biochemistry 2004 Jul;271(13):2782-90
European journal of biochemistry 2004 Jul;271(13):2782-90
Substrate specificity, inhibition and enzymological analysis of recombinant human glutamate carboxypeptidase II.
Barinka C, Rinnová M, Sácha P, Rojas C, Majer P, Slusher BS, Konvalinka J
Journal of neurochemistry 2002 Feb;80(3):477-87
Journal of neurochemistry 2002 Feb;80(3):477-87
Substrate specificity, inhibition and enzymological analysis of recombinant human glutamate carboxypeptidase II.
Barinka C, Rinnová M, Sácha P, Rojas C, Majer P, Slusher BS, Konvalinka J
Journal of neurochemistry 2002 Feb;80(3):477-87
Journal of neurochemistry 2002 Feb;80(3):477-87
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Supportive validation
- Submitted by
- Novus Biologicals (provider)
- Main image
- Experimental details
- Western Blot: PSMA/FOLH1/NAALADase I Antibody (GCP-04) [NBP1-45057] - PSMA expression in human prostate cancer cell lines. Image from verified customer review.
- Submitted by
- Novus Biologicals (provider)
- Main image
- Experimental details
- Western Blot: PSMA/FOLH1/NAALADase I Antibody (GCP-04) [NBP1-45057] - Fragment of human GCPII (aminoacids 44-750) produced in S2 cells on Western blot by GCP-04 monoclonal antibody. Lanes 1, 2, 3 represent 800, 400 and 200 pg of the protein.
Supportive validation
- Submitted by
- Novus Biologicals (provider)
- Main image
- Experimental details
- Immunohistochemistry-Paraffin: PSMA/FOLH1/NAALADase I Antibody (GCP-04) [NBP1-45057] - GCPII in porcine kidney by GCP-04 monoclonal antibody. Highly positive proximal glomeruli.
- Submitted by
- Novus Biologicals (provider)
- Main image
- Experimental details
- Immunohistochemistry-Paraffin: PSMA/FOLH1/NAALADase I Antibody (GCP-04) [NBP1-45057] - GCPII in human prostate by GCP-04 monoclonal antibody. Mag. 400x; positive epithelium of the prostate glands.
- Submitted by
- Novus Biologicals (provider)
- Main image
- Experimental details
- Immunohistochemistry: PSMA/FOLH1/NAALADase I Antibody (GCP-04) [NBP1-45057] - GCPII in human Medulla oblongata by GCP-04 monoclonal antibody. Mag. 40x; positive astrocytes in white matter.
