BHLH3 (N-Term) antibody
| Antigen | BHLH3 |
| Binding Site |
N-Term |
| Clonality | Polyclonal |
| Host |
Rabbit |
| Reactivity |
Human |
| Application |
Western Blotting (WB), ELISA
|
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4 references available |
| Certificates | ISO 9001:2008 |
| Catalog no. | ABIN651934 |
| Quantity | 0.1 mg (0.25 mg/ml) |
| Price | 280.50 $ Plus shipping costs $45.00 |
| Shipping to |
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| Availability | Will be delivered in 2 to 3 Business Days |
Additional Information
| Gene ID | 79365 |
| UniProt | Q9C0J9, NP_110389 |
| Immunogen | This BHLH3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 24-54 amino acids from the N-terminal region of human BHLH3. |
| Isotype | Ig |
| Description | Other names: Class E basic helix-loop-helix protein 41,BHLHE41,SHARP1, DEC2, BHLHB3 |
| Characteristics | Peptide Affinity Purified Rabbit Polyclonal Antibody (Pab) |
| Specificity | This BHLH3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 24-54 amino acids from the N-terminal region of human BHLH3. |
| Molecular Weight | 50498 DA |
| Comments |
Background: BHLHE41 may be a transcriptional repressor that represses both basal and activated transcription. |
Application Details
| Application Notes | The suggested dilution is: ELISA ~~ 1:1,000 Western blotting~~ 1:100~500 |
| Concentration | 0.25 mg/ml |
| Purification | Purified |
| Buffer | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8 deg C for up to 6 months. For long term storage store at -20 deg C in small aliquots to prevent freeze-thaw cycles |
| Research Area | Translation Factors, Transcription Factors, Signaling, Cell Structure |
| Restrictions | For Research Use only |
Images
Publications
| Product |
Grottke, Mantwill, Dietel et al.: "Identification of differentially expressed genes in human melanoma cells with acquired resistance to various antineoplastic drugs." in: International journal of cancer. Journal international du cancer, Vol. 88, Issue 4, pp. 535-46, 2000 (PubMed).
Fujimoto, Shen, Noshiro et al.: "Molecular cloning and characterization of DEC2, a new member of basic helix-loop-helix proteins." in: Biochemical and biophysical research communications, Vol. 280, Issue 1, pp. 164-71, 2001 (PubMed). Garriga-Canut, Roopra, Buckley: "The basic helix-loop-helix protein, sharp-1, represses transcription by a histone deacetylase-dependent and histone deacetylase-independent mechanism." in: The Journal of biological chemistry, Vol. 276, Issue 18, pp. 14821-8, 2001 (PubMed). Honma, Kawamoto, Takagi et al.: "Dec1 and Dec2 are regulators of the mammalian molecular clock." in: Nature, Vol. 419, Issue 6909, pp. 841-4, 2002 (PubMed). |




