Progesterone Receptor B (C1A2) Rabbit mAb (BSA and Azide Free) #31535

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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

This product is the carrier free version of product #3157. All data were generated using the same antibody clone in the standard formulation which contains BSA and glycerol.

This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.

BSA and Azide Free antibodies are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity.

Formulation

Supplied in 1X PBS (10 mM Na₂HPO₄, 3 mM KCl, 2 mM KH₂PO₄, and 140 mM NaCl (pH 7.8)). BSA and Azide Free.

For standard formulation of this product see product #3157

Storage

Store at -20°C. This product will freeze at -20°C so it is recommended to aliquot into single-use vials to avoid multiple freeze/thaw cycles. A slight precipitate may be present and can be dissolved by gently vortexing. This will not interfere with antibody performance.

Specificity / Sensitivity

Progesterone Receptor B (C1A2) Rabbit mAb (BSA and Azide Free) 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.

Database Links

UniProt ID: P06401

Entrez-Gene Id: 5241

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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