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Western blotAntibody data
- Antibody Data
- Antigen structure
- References [23]
- Comments [0]
- Validations
- Western blot [1]
- Immunocytochemistry [1]
- Immunohistochemistry [2]
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- Product number
- MA1-2012 - Provider product page
- Provider
- Invitrogen Antibodies
- Product name
- NF-H Monoclonal Antibody (3G3)
- Antibody type
- Monoclonal
- Antigen
- Synthetic peptide
- Description
- MA1-2012 detects the neurofilament, heavy chain in human and rat samples. MA1-2012 has been successfully used in Western blot, immunohistochemistry and immunofluorecence procedures. By Western blot this antibody detects a ~200 kDa protein representing the neurofilament, heavy chain in rat brain microsome. In immunohistochemistry procedures MA1-2012 recognizes the neurofilament, heavy chain in rat hippocampal neurons. The MA1-2012 immunogen is a synthetic peptide corresponding to 226 amino acids of the C-terminus of neurofilament, heavy chain.
- Reactivity
- Human, Rat
- Host
- Mouse
- Antibody clone number
- 3G3
- Vial size
- 100 µg
- Concentration
- 1 mg/mL
- Storage
- -20° C, Avoid Freeze/Thaw Cycles
Submitted references Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation.
Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation.
Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin.
Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin.
Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor.
Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor.
Compartmentation of alpha-internexin and neurofilament triplet proteins in cultured hippocampal neurons.
A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains.
A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains.
Definition of a minimal domain of the dioxin receptor that is associated with Hsp90 and maintains wild type ligand binding affinity and specificity.
Definition of a minimal domain of the dioxin receptor that is associated with Hsp90 and maintains wild type ligand binding affinity and specificity.
Identification of functional domains of the aryl hydrocarbon receptor.
Identification of functional domains of the aryl hydrocarbon receptor.
The basic helix-loop-helix/PAS factor Sim is associated with hsp90. Implications for regulation by interaction with partner factors.
The basic helix-loop-helix/PAS factor Sim is associated with hsp90. Implications for regulation by interaction with partner factors.
The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90.
A tyrosine kinase-dependent pathway regulates ligand-dependent activation of the dioxin receptor in human keratinocytes.
All of the factors required for assembly of the glucocorticoid receptor into a functional heterocomplex with heat shock protein 90 are preassociated in a self-sufficient protein folding structure, a "foldosome".
A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor.
A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor.
A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor.
Characterization of the protein-protein interactions determining the heat shock protein (hsp90.hsp70.hsp56) heterocomplex.
Evidence that the 90-kDa heat shock protein (HSP90) exists in cytosol in heteromeric complexes containing HSP70 and three other proteins with Mr of 63,000, 56,000, and 50,000.
Dittmar KD, Pratt WB
The Journal of biological chemistry 1997 May 16;272(20):13047-54
The Journal of biological chemistry 1997 May 16;272(20):13047-54
Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation.
Dittmar KD, Pratt WB
The Journal of biological chemistry 1997 May 16;272(20):13047-54
The Journal of biological chemistry 1997 May 16;272(20):13047-54
Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin.
Silverstein AM, Galigniana MD, Chen MS, Owens-Grillo JK, Chinkers M, Pratt WB
The Journal of biological chemistry 1997 Jun 27;272(26):16224-30
The Journal of biological chemistry 1997 Jun 27;272(26):16224-30
Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin.
Silverstein AM, Galigniana MD, Chen MS, Owens-Grillo JK, Chinkers M, Pratt WB
The Journal of biological chemistry 1997 Jun 27;272(26):16224-30
The Journal of biological chemistry 1997 Jun 27;272(26):16224-30
Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor.
Gradin K, McGuire J, Wenger RH, Kvietikova I, fhitelaw ML, Toftgård R, Tora L, Gassmann M, Poellinger L
Molecular and cellular biology 1996 Oct;16(10):5221-31
Molecular and cellular biology 1996 Oct;16(10):5221-31
Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor.
Gradin K, McGuire J, Wenger RH, Kvietikova I, fhitelaw ML, Toftgård R, Tora L, Gassmann M, Poellinger L
Molecular and cellular biology 1996 Oct;16(10):5221-31
Molecular and cellular biology 1996 Oct;16(10):5221-31
Compartmentation of alpha-internexin and neurofilament triplet proteins in cultured hippocampal neurons.
Benson DL, Mandell JW, Shaw G, Banker G
Journal of neurocytology 1996 Mar;25(3):181-96
Journal of neurocytology 1996 Mar;25(3):181-96
A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains.
Owens-Grillo JK, Czar MJ, Hutchison KA, Hoffmann K, Perdew GH, Pratt WB
The Journal of biological chemistry 1996 Jun 7;271(23):13468-75
The Journal of biological chemistry 1996 Jun 7;271(23):13468-75
A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains.
Owens-Grillo JK, Czar MJ, Hutchison KA, Hoffmann K, Perdew GH, Pratt WB
The Journal of biological chemistry 1996 Jun 7;271(23):13468-75
The Journal of biological chemistry 1996 Jun 7;271(23):13468-75
Definition of a minimal domain of the dioxin receptor that is associated with Hsp90 and maintains wild type ligand binding affinity and specificity.
Coumailleau P, Poellinger L, Gustafsson JA, Whitelaw ML
The Journal of biological chemistry 1995 Oct 20;270(42):25291-300
The Journal of biological chemistry 1995 Oct 20;270(42):25291-300
Definition of a minimal domain of the dioxin receptor that is associated with Hsp90 and maintains wild type ligand binding affinity and specificity.
Coumailleau P, Poellinger L, Gustafsson JA, Whitelaw ML
The Journal of biological chemistry 1995 Oct 20;270(42):25291-300
The Journal of biological chemistry 1995 Oct 20;270(42):25291-300
Identification of functional domains of the aryl hydrocarbon receptor.
Fukunaga BN, Probst MR, Reisz-Porszasz S, Hankinson O
The Journal of biological chemistry 1995 Dec 8;270(49):29270-8
The Journal of biological chemistry 1995 Dec 8;270(49):29270-8
Identification of functional domains of the aryl hydrocarbon receptor.
Fukunaga BN, Probst MR, Reisz-Porszasz S, Hankinson O
The Journal of biological chemistry 1995 Dec 8;270(49):29270-8
The Journal of biological chemistry 1995 Dec 8;270(49):29270-8
The basic helix-loop-helix/PAS factor Sim is associated with hsp90. Implications for regulation by interaction with partner factors.
McGuire J, Coumailleau P, Whitelaw ML, Gustafsson JA, Poellinger L
The Journal of biological chemistry 1995 Dec 29;270(52):31353-7
The Journal of biological chemistry 1995 Dec 29;270(52):31353-7
The basic helix-loop-helix/PAS factor Sim is associated with hsp90. Implications for regulation by interaction with partner factors.
McGuire J, Coumailleau P, Whitelaw ML, Gustafsson JA, Poellinger L
The Journal of biological chemistry 1995 Dec 29;270(52):31353-7
The Journal of biological chemistry 1995 Dec 29;270(52):31353-7
The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90.
Hutchison KA, Stancato LF, Owens-Grillo JK, Johnson JL, Krishna P, Toft DO, Pratt WB
The Journal of biological chemistry 1995 Aug 11;270(32):18841-7
The Journal of biological chemistry 1995 Aug 11;270(32):18841-7
A tyrosine kinase-dependent pathway regulates ligand-dependent activation of the dioxin receptor in human keratinocytes.
Gradin K, Whitelaw ML, Toftgård R, Poellinger L, Berghard A
The Journal of biological chemistry 1994 Sep 23;269(38):23800-7
The Journal of biological chemistry 1994 Sep 23;269(38):23800-7
All of the factors required for assembly of the glucocorticoid receptor into a functional heterocomplex with heat shock protein 90 are preassociated in a self-sufficient protein folding structure, a "foldosome".
Hutchison KA, Dittmar KD, Pratt WB
The Journal of biological chemistry 1994 Nov 11;269(45):27894-9
The Journal of biological chemistry 1994 Nov 11;269(45):27894-9
A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor.
McGuire J, Whitelaw ML, Pongratz I, Gustafsson JA, Poellinger L
Molecular and cellular biology 1994 Apr;14(4):2438-46
Molecular and cellular biology 1994 Apr;14(4):2438-46
A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor.
McGuire J, Whitelaw ML, Pongratz I, Gustafsson JA, Poellinger L
Molecular and cellular biology 1994 Apr;14(4):2438-46
Molecular and cellular biology 1994 Apr;14(4):2438-46
A cellular factor stimulates ligand-dependent release of hsp90 from the basic helix-loop-helix dioxin receptor.
McGuire J, Whitelaw ML, Pongratz I, Gustafsson JA, Poellinger L
Molecular and cellular biology 1994 Apr;14(4):2438-46
Molecular and cellular biology 1994 Apr;14(4):2438-46
Characterization of the protein-protein interactions determining the heat shock protein (hsp90.hsp70.hsp56) heterocomplex.
Czar MJ, Owens-Grillo JK, Dittmar KD, Hutchison KA, Zacharek AM, Leach KL, Deibel MR Jr, Pratt WB
The Journal of biological chemistry 1994 Apr 15;269(15):11155-61
The Journal of biological chemistry 1994 Apr 15;269(15):11155-61
Evidence that the 90-kDa heat shock protein (HSP90) exists in cytosol in heteromeric complexes containing HSP70 and three other proteins with Mr of 63,000, 56,000, and 50,000.
Perdew GH, Whitelaw ML
The Journal of biological chemistry 1991 Apr 15;266(11):6708-13
The Journal of biological chemistry 1991 Apr 15;266(11):6708-13
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Supportive validation
- Submitted by
- Invitrogen Antibodies (provider)
- Main image
- Experimental details
- Western blot analysis of Neurofilament, Heavy chain was performed by loading 25 µg of SH-SY5Y (lane 1) and rat brain (lane 2) lysates onto an SDS polyacrylamide gel. Proteins were transferred to a PVDF membrane and blocked at 4ºC overnight. The membrane was probed with a Neurofilament, Heavy chain monoclonal antibody (Product # MA1-2012) at a dilution of 1:500 overnight at 4°C, washed in TBST, and probed with an HRP-conjugated secondary antibody for 1 hr at room temperature in the dark. Chemiluminescent detection was performed using Pierce ECL Plus Western Blotting Substrate (Product # 32132). Results show a band at ~200 kDa.
Supportive validation
- Submitted by
- Invitrogen Antibodies (provider)
- Main image
- Experimental details
- Immunofluorescence of neurofilament, heavy chain in rat cerebral cortex cultures in green.
Supportive validation
- Submitted by
- Invitrogen Antibodies (provider)
- Main image
- Experimental details
- Immunohistochemistry analysis of Neurofilament, Heavy chain showing staining in the cytoplasm and axons of formalin-fixed, paraffin-embedded human brain tissue (B) and magnified section (C) compared with an isotype control (A). To expose target proteins, antigen retrieval was performed using HEIR with a buffer (pH 6.2). Tissues were probed with a Neurofilament, Heavy chain monoclonal antibody (Product # MA1-2012) for 60 minutes at a dilution of 2 µg/mL and detection was performed using an HRP-conjugated detection system for 30 minutes followed by DAB staining.
- Submitted by
- Invitrogen Antibodies (provider)
- Main image
- Experimental details
- Immunohistochemistry analysis of Neurofilament Heavy Chain showing staining in the cytoplasm and nucleus of paraffin-embedded rat brain tissue (right) compared to a negative control without primary antibody (left). To expose target proteins, antigen retrieval was performed using 10mM sodium citrate (pH 6.0), microwaved for 8-15 min. Following antigen retrieval, tissues were blocked in 3% H2O2-methanol for 15 min at room temperature, washed with ddH2O and PBS, and then probed with a Neurofilament Heavy Chain monoclonal antibody (Product # MA1-2012) diluted in 3% BSA-PBS at a dilution of 1:20 overnight at 4°C in a humidified chamber. Tissues were washed extensively in PBST and detection was performed using an HRP-conjugated secondary antibody followed by colorimetric detection using a DAB kit. Tissues were counterstained with hematoxylin and dehydrated with ethanol and xylene to prep for mounting.
