Progesterone Receptor B (C1A2) Rabbit mAb #3157
Filter:
- WB
- IHC
- IF
- F
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 118 |
| Source/Isotype | Rabbit |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
- IF-Immunofluorescence
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunohistochemistry (Paraffin) | 1:800 |
| Immunofluorescence (Immunocytochemistry) | 1:800 |
| Flow Cytometry (Fixed/Permeabilized) | 1:200 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
For a carrier free (BSA and azide free) version of this product see product #31535.
For a carrier free (BSA and azide free) version of this product see product #31535.
Protocol
Specificity / Sensitivity
Progesterone Receptor B (C1A2) Rabbit mAb detects endogenous levels of total progesterone receptor B protein. This antibody does not cross-react with other PR family members.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser115 of human progesterone receptor.
Background
Human progesterone receptor (PR) is expressed as two forms: the full length PR-B and the short form PR-A. PR-A lacks the first 164 amino acid residues of PR-B (1,2). Both PR-A and PR-B are ligand activated, but differ in their relative ability to activate target gene transcription (3,4). The activity of PR is regulated by phosphorylation; at least seven serine residues are phosphorylated in its amino-terminal domain. Three sites (Ser81, Ser102, and Ser162) are unique to full length PR-B, while other sites (Ser190, Ser294, Ser345, and Ser400) are shared by both isoforms (5). Phosphorylation of PR-B at Ser190 (equivalent to Ser26 of PR-A) is catalyzed by CDK2 (6). Mutation of Ser190 results in decreased activity of PR (7), suggesting that the phosphorylation at Ser190 may be critical to its biological function.
- Evans, R.M. (1988) Science 240, 889-895.
- Kastner, P. et al. (1990) EMBO J. 112, 1603-1614.
- Giangrande, P.H. et al. (2000) Mol. Cell. Biol. 20, 3102-3115.
- Wen, D.X. et al. (1994) Mol. Cell. Biol. 14, 8356-8364.
- Clemm, D.L. et al. (2000) Mol. Endocrinol. 14, 52-65.
- Zhang, Y. et al. (1997) Mol. Endocrinol. 11, 823-832.
- Takimoto, G.S. et al. (1996) J. Biol. Chem. 271, 13308-13316.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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U.S. Patent No. 7,429,487, foreign equivalents, and child patents deriving therefrom.
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