Product Name: AurC (190-196) pS193
Product Number: PE-04AFV95
Size: 200 µg      Price:42.00
1 mg      $US84.00
5 mg      185.00
Peptide Name: AurC (190-196) pS193

Product Use: Services as a blocking peptide for use with the AurKC-pS193 rabbit polyclonal antibody (Cat. No.: AB-PK532) that is also available from Kinexus. This phosphopeptide may also be useful as a substrate for screening the phosphatase activity of protein phosphatases. The peptide sequence is located in the protein kinase catalytic domain activation T loop region between subdomains VII and VIII. S193 phosphorylation is predicted to be stimulatory for phosphotransferase activity.

Peptide Production Method: Solid-phase peptide synthesis

Peptide Origin: Homo sapiens

Peptide Sequence: HTP-pS-LRR

Peptide Modifications N Terminus: Free amino

Peptide Modifications C Terminus: βAla-Cys

Peptide Modifications Other: Phosphorylated

Peptide Molecular Mass Calculated: 1120.18 Da

Peptide Purity Percent after Synthesis and Purification: >95

Peptide Appearance: White powder

Peptide Form: Solid

Storage Conditions: -20°C

Related Product 1: AurC - pS193 phosphosite-specific antibody (Cat. No.: AB-PK532)

Scientific Background: AurC (AurKC) is a protein-serine/threonine kinase of the Other group and AUR family. It serves an essential component of the chromosomal passenger complex (CPC), which functions to ensure correct chromosomal alignment and segregation during mitosis. In addition, this protein complex is necessary for chromatin-induced microtubule stabilization and formation of the spindle apparatus. AurC has also been shown to play a key role in meiosis, specifically during spermatogenesis (production of sperm). Several mutations in the AurC gene have been observed in male patients with spermatogenic failure 5, including a 1-bp deletion (144delC) leading to premature translation termination at position 71 and a truncated protein without a catalytic domain, a C229Y substitution mutation in the kinase catalytic domain of the protein, and a 2A-to-G transition mutation at the splice site of intron 4 (436-2A-G) leading to the omission of exon 5 from the protein. These mutations result in a loss-of-function for the protein catalytic activity, therefore defects in AurC activity are thought to be the primary contributing factor to the development of spermatogenic failure 5.