Loading... Please wait...

Our Newsletter

BSA Creatinine L8 Conjugate

  • BSA creatinine L8 conjugate structure
In stock, usually ships within 24 hrs
Calculated at checkout

Download Documents
SDS Product Sheet

Creatinine is a byproduct of creatine produced in the muscles and is removed from the body by the kidneys. Measuring the amount of creatinine in the blood and/or urine can predict how well the kidneys are working. Immunoassay is a general method of detecting creatinine. However, creatinine is a very small molecule and is generally very difficult to generate an antibody against and that binds strongly to the protein for detection. CellMosaic’s BSA-creatinine conjugate is designed with a flexible linker of optimal length (8-atom length, L8) and a labeling chemistry that does not interfere with creatinine binding with the antibody. Each lot of the conjugate consists of an optimally loaded BSA (5-7 creatinine molecules per BSA molecule as determined by mass spectrometry or SEC HPLC).

The product is sold as either 1 vial of 1 mg (Cat# CM52117-1MG) or 5 vials of 1 mg (Cat# CM52117-5MG). For bulk orders, please contact us for a quote.


  • Suitable for antibody production and creatinine assay development

Key Features of this BSA Creatinine Conjugate

  • Frozen liquid in PBS buffer and ready to use 
  • Flexible long linker and non-interfering labeling chemistry for easy access
  • Optimal loading with average of 5-7 creatinine molecules per BSA for strong binding with low background
  • Concentration accurately determined by UV/HPLC 

Example Data

Example 1: MALDI-TOF MS analysis of BSA (left) and BSA Creatinine L8 (Lot#:s6.0809. Number of Creatinine molecules: 5.7) (right) (Intact MS). 

Figure 2: SEC HPLC analysis of unlabeled BSA (top) and BSA creatinine L8 conjugate (bottom, elute earlier. Lot#:s6.0809. Number of Creatinine molecules: 5.7)



Other Details

Average Loading of Creatinine Molecule:

Add to Wish List

Click the button below to add the BSA Creatinine L8 Conjugate to your wish list.

You Recently Viewed...