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antibody from antibodies-online
Targeting: FOLH1
FOLH, GCP2, GCPII, NAALAD1, NAALAdase, PSM, PSMA
Immunocytochemistry
Flow cytometryAntibody data
- Antibody Data
- Antigen structure
- References [7]
- Comments [0]
- Validations
- Flow cytometry [1]
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- Product number
- ABIN238408 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Folate Hydrolase (Prostate-Specific Membrane Antigen) 1 (FOLH1) (AA 44-750) antibody
- Antibody type
- Monoclonal
- Description
- Protein A Chromatography
- Reactivity
- Human
- Host
- Mouse
- Epitope
- AA 44-750
- Isotype
- IgG
- Antibody clone number
- GCP-05
- Vial size
- 0.1 mg
- Storage
- Store the antibody undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer. Avoid repeated freezing and thawing.Shelf life: one year from despatch.
Submitted references Expression of glutamate carboxypeptidase II in human brain.
Structure of glutamate carboxypeptidase II, a drug target in neuronal damage and prostate cancer.
Crystal structure of prostate-specific membrane antigen, a tumor marker and peptidase.
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.
Glutamate carboxypeptidase II inhibition protects motor neurons from death in familial amyotrophic lateral sclerosis models.
Substrate specificity, inhibition and enzymological analysis of recombinant human glutamate carboxypeptidase II.
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
Structure of glutamate carboxypeptidase II, a drug target in neuronal damage and prostate cancer.
Mesters JR, Barinka C, Li W, Tsukamoto T, Majer P, Slusher BS, Konvalinka J, Hilgenfeld R
The EMBO journal 2006 Mar 22;25(6):1375-84
The EMBO journal 2006 Mar 22;25(6):1375-84
Crystal structure of prostate-specific membrane antigen, a tumor marker and peptidase.
Davis MI, Bennett MJ, Thomas LM, Bjorkman PJ
Proceedings of the National Academy of Sciences of the United States of America 2005 Apr 26;102(17):5981-6
Proceedings of the National Academy of Sciences of the United States of America 2005 Apr 26;102(17):5981-6
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
Glutamate carboxypeptidase II inhibition protects motor neurons from death in familial amyotrophic lateral sclerosis models.
Ghadge GD, Slusher BS, Bodner A, Canto MD, Wozniak K, Thomas AG, Rojas C, Tsukamoto T, Majer P, Miller RJ, Monti AL, Roos RP
Proceedings of the National Academy of Sciences of the United States of America 2003 Aug 5;100(16):9554-9
Proceedings of the National Academy of Sciences of the United States of America 2003 Aug 5;100(16):9554-9
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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