ADP-Ribosyltransferase 1 (ART1) Peptide
ART1
Reactivity: Mammalian
Host: Synthetic
BP, WB, IHC
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- Target See all ART1 products
- ART1 (ADP-Ribosyltransferase 1 (ART1))
- Peptide Type
- Synthetic
- Origin
- Mammalian
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Source
- Synthetic
- Application
- Blocking Peptide (BP), Western Blotting (WB), Immunohistochemistry (IHC)
- Sequence
- KHSTYNCEYI KDKKCKSGPC HLDNSAMGQS PLSAVWSLLL LLWFLVVRAF
- Characteristics
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A synthetic peptide for use as a blocking control in assays to test for specificity of ART1 antibody,
Alternative Names: ART1 control peptide, ART1 antibody Blocking Peptide, Anti-ART1 Blocking Peptide, ADP-ribosyltransferase 1 Blocking Peptide, ART2 Blocking Peptide, CD296 Blocking Peptide, MGC133217 Blocking Peptide, RT6 Blocking Peptide, ART1, ART-1, ART 1, ART-1 Blocking Peptide, ART 1 Blocking Peptide
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- Application Notes
- Optimal conditions should be determined by the investigator
- Restrictions
- For Research Use only
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- Format
- Lyophilized
- Reconstitution
- Add 100 µL of distilled water for a final peptide concentration is 1 mg/mL.
- Buffer
- PBS
- Handling Advice
- Avoid repeated freeze/thaw cycles.
- Storage
- -20 °C
- Storage Comment
- Store at -20 °C long term.
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- Target
- ART1 (ADP-Ribosyltransferase 1 (ART1))
- Synonyms
- ART2 Peptide, ARTC1 Peptide, CD296 Peptide, RT6 Peptide, ADPRT Peptide, Yac-1 Peptide, ART7.1 Peptide, ART1 Peptide, art1 Peptide, art2 Peptide, cd296 Peptide, rt6 Peptide, ADP-ribosyltransferase 1 Peptide, ADP-ribosyltransferase 1 L homeolog Peptide, ART1 Peptide, Art1 Peptide, art1.L Peptide
- Background
- ADP-ribosyltransferase catalyzes the ADP-ribosylation of arginine residues in proteins. Mono-ADP-ribosylation is a posttranslational modification of proteins that is interfered with by a variety of bacterial toxins including cholera, pertussis, and heat-labile enterotoxins of E. coli. The amino acid sequence consists of predominantly hydrophobic N- and C-terminal regions, which is characteristic of glycosylphosphatidylinositol (GPI)-anchored proteins.
- Molecular Weight
- 36 kDa
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