Antibody data
- Antibody Data
- Antigen structure
- References [5]
- Comments [0]
- Validations [0]
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- Product number
- ABIN362995 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Myristoylated Alanine-Rich Protein Kinase C Substrate (MARCKS) (AA 156-160) antibody
- Antibody type
- Polyclonal
- Antigen
- Peptide sequence around AA 156-160 (R-F-S-F-K) derived from Human MARCKS. Antibodies were produced by immunizing rabbits with synthetic peptide and KLH conjugates.
- Description
- The antibody was affinity-purified from rabbit antiserum by affinity-chromatography usingepitope-specific immunogen.
- Reactivity
- Human, Mouse, Rat
- Host
- Rabbit
- Epitope
- AA 156-160
- Isotype
- IgG
- Vial size
- 50 μL
- Concentration
- 1 mg/mL
- Storage
- Store at -20°C for long term preservation (recommended). Store at 4°C for short term use.
Submitted references Signaling pathways mediating phosphorylation and inactivation of glycogen synthase kinase-3β by the recombinant human δ-opioid receptor stably expressed in Chinese hamster ovary cells.
Protein kinase C isoforms zeta and iota mediate collagenase expression and cartilage destruction via STAT3- and ERK-dependent c-fos induction.
Pleiotrophin regulates serine phosphorylation and the cellular distribution of beta-adducin through activation of protein kinase C.
Rho-associated kinase phosphorylates MARCKS in human neuronal cells.
The antibody specific for myristoylated alanine-rich C kinase substrate phosphorylated by protein kinase C: activation of protein kinase C in smooth muscle cells in human coronary arteries.
Olianas MC, Dedoni S, Onali P
Neuropharmacology 2011 Jun;60(7-8):1326-36
Neuropharmacology 2011 Jun;60(7-8):1326-36
Protein kinase C isoforms zeta and iota mediate collagenase expression and cartilage destruction via STAT3- and ERK-dependent c-fos induction.
Litherland GJ, Elias MS, Hui W, Macdonald CD, Catterall JB, Barter MJ, Farren MJ, Jefferson M, Rowan AD
The Journal of biological chemistry 2010 Jul 16;285(29):22414-25
The Journal of biological chemistry 2010 Jul 16;285(29):22414-25
Pleiotrophin regulates serine phosphorylation and the cellular distribution of beta-adducin through activation of protein kinase C.
Pariser H, Herradon G, Ezquerra L, Perez-Pinera P, Deuel TF
Proceedings of the National Academy of Sciences of the United States of America 2005 Aug 30;102(35):12407-12
Proceedings of the National Academy of Sciences of the United States of America 2005 Aug 30;102(35):12407-12
Rho-associated kinase phosphorylates MARCKS in human neuronal cells.
Nagumo H, Ikenoya M, Sakurada K, Furuya K, Ikuhara T, Hiraoka H, Sasaki Y
Biochemical and biophysical research communications 2001 Jan 26;280(3):605-9
Biochemical and biophysical research communications 2001 Jan 26;280(3):605-9
The antibody specific for myristoylated alanine-rich C kinase substrate phosphorylated by protein kinase C: activation of protein kinase C in smooth muscle cells in human coronary arteries.
Yamamoto H, Matsumura T, Kugiyama K, Oishi Y, Ogata N, Yasue H, Miyamoto E
Archives of biochemistry and biophysics 1998 Nov 15;359(2):151-9
Archives of biochemistry and biophysics 1998 Nov 15;359(2):151-9
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