Antibody data
- Antibody Data
- Antigen structure
- References [12]
- Comments [0]
- Validations
- Western blot [1]
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- Product number
- NB500-144 - Provider product page

- Provider
- Novus Biologicals
- Proper citation
- Novus Cat#NB500-144, RRID:AB_10001662
- Product name
- Rabbit Polyclonal MEK1 Antibody
- Antibody type
- Polyclonal
- Description
- Immunogen affinity purified. Specific for the ~45k MEK 1 protein phosphorylated at Thr386. The immunolabeling is completely eliminated by treatment with lambda-phosphatase.
- Reactivity
- Human, Rat
- Host
- Rabbit
- Isotype
- IgG
- Vial size
- 0.1 ml
- Storage
- Store at -20C. Avoid freeze-thaw cycles.
Submitted references Mechanisms of regulating the Raf kinase family.
Mechanisms of regulating the Raf kinase family.
Molecular psychology: roles for the ERK MAP kinase cascade in memory.
Mitogen-activated protein (MAP) kinase phosphorylation of MAP kinase kinase: determination of phosphorylation sites by mass spectrometry and site-directed mutagenesis.
Mitogen-activated protein (MAP) kinase phosphorylation of MAP kinase kinase: determination of phosphorylation sites by mass spectrometry and site-directed mutagenesis.
The MAP kinase cascade. Discovery of a new signal transduction pathway.
The MAP kinase cascade. Discovery of a new signal transduction pathway.
The primary structure of MEK, a protein kinase that phosphorylates the ERK gene product.
The primary structure of MEK, a protein kinase that phosphorylates the ERK gene product.
pp54 microtubule-associated protein-2 kinase requires both tyrosine and serine/threonine phosphorylation for activity.
Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophosphorylation on both tyrosine and threonine residues: implications for their mechanism of activation.
Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophosphorylation on both tyrosine and threonine residues: implications for their mechanism of activation.
Chong H, Vikis HG, Guan KL
Cellular signalling 2003 May;15(5):463-9
Cellular signalling 2003 May;15(5):463-9
Mechanisms of regulating the Raf kinase family.
Chong H, Vikis HG, Guan KL
Cellular signalling 2003 May;15(5):463-9
Cellular signalling 2003 May;15(5):463-9
Molecular psychology: roles for the ERK MAP kinase cascade in memory.
Adams JP, Sweatt JD
Annual review of pharmacology and toxicology 2002;42:135-63
Annual review of pharmacology and toxicology 2002;42:135-63
Mitogen-activated protein (MAP) kinase phosphorylation of MAP kinase kinase: determination of phosphorylation sites by mass spectrometry and site-directed mutagenesis.
Mansour SJ, Resing KA, Candi JM, Hermann AS, Gloor JW, Herskind KR, Wartmann M, Davis RJ, Ahn NG
Journal of biochemistry 1994 Aug;116(2):304-14
Journal of biochemistry 1994 Aug;116(2):304-14
Mitogen-activated protein (MAP) kinase phosphorylation of MAP kinase kinase: determination of phosphorylation sites by mass spectrometry and site-directed mutagenesis.
Mansour SJ, Resing KA, Candi JM, Hermann AS, Gloor JW, Herskind KR, Wartmann M, Davis RJ, Ahn NG
Journal of biochemistry 1994 Aug;116(2):304-14
Journal of biochemistry 1994 Aug;116(2):304-14
The MAP kinase cascade. Discovery of a new signal transduction pathway.
Ahn NG
Molecular and cellular biochemistry 1993 Nov;127-128:201-9
Molecular and cellular biochemistry 1993 Nov;127-128:201-9
The MAP kinase cascade. Discovery of a new signal transduction pathway.
Ahn NG
Molecular and cellular biochemistry 1993 Nov;127-128:201-9
Molecular and cellular biochemistry 1993 Nov;127-128:201-9
The primary structure of MEK, a protein kinase that phosphorylates the ERK gene product.
Crews CM, Alessandrini A, Erikson RL
Science (New York, N.Y.) 1992 Oct 16;258(5081):478-80
Science (New York, N.Y.) 1992 Oct 16;258(5081):478-80
The primary structure of MEK, a protein kinase that phosphorylates the ERK gene product.
Crews CM, Alessandrini A, Erikson RL
Science (New York, N.Y.) 1992 Oct 16;258(5081):478-80
Science (New York, N.Y.) 1992 Oct 16;258(5081):478-80
pp54 microtubule-associated protein-2 kinase requires both tyrosine and serine/threonine phosphorylation for activity.
Kyriakis JM, Brautigan DL, Ingebritsen TS, Avruch J
The Journal of biological chemistry 1991 Jun 5;266(16):10043-6
The Journal of biological chemistry 1991 Jun 5;266(16):10043-6
Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophosphorylation on both tyrosine and threonine residues: implications for their mechanism of activation.
Seger R, Ahn NG, Boulton TG, Yancopoulos GD, Panayotatos N, Radziejewska E, Ericsson L, Bratlien RL, Cobb MH, Krebs EG
Proceedings of the National Academy of Sciences of the United States of America 1991 Jul 15;88(14):6142-6
Proceedings of the National Academy of Sciences of the United States of America 1991 Jul 15;88(14):6142-6
Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophosphorylation on both tyrosine and threonine residues: implications for their mechanism of activation.
Seger R, Ahn NG, Boulton TG, Yancopoulos GD, Panayotatos N, Radziejewska E, Ericsson L, Bratlien RL, Cobb MH, Krebs EG
Proceedings of the National Academy of Sciences of the United States of America 1991 Jul 15;88(14):6142-6
Proceedings of the National Academy of Sciences of the United States of America 1991 Jul 15;88(14):6142-6
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Supportive validation
- Submitted by
- Novus Biologicals (provider)
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- Experimental details
- Western Blot: MEK1 [p Thr386] Antibody [NB500-144] - Analysis of recombinant WT and mutant MEK 1 immunolabeled with the Anti Thr386 MEK1 antibody. Lanes 1 and 2 are WT MEK 1 and Lanes 3 and 4 are mutant MEK 1 (T386A). MAP kinase was coexpressed in the samples run in Lanes 2 and 4.