Natural human Kallikrein 1 protein (ab90351)

Overview

Description

  • NatureNatural
  • SourceNative
  • Amino Acid Sequence
    • SpeciesHuman

Specifications

Our Abpromise guarantee covers the use of ab90351 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Biological activity Activity: 15 units per mg. One unit is defined as the amount of enzyme that hydrolyzes one umole of D-Pro-Phe-Arg-pNA per minute at 25°C, pH 7.8.
  • Applications

    SDS-PAGE

  • Purity> 95 % SDS-PAGE.

  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -20ºC. Avoid freeze / thaw cycles.

    Preservative: None
    Constituents: 20mM Tris HCl, 100mM Sodium chloride, pH 7.8

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

General Info

  • Alternative names
    • Glandular kallikrein 1
    • hK 1
    • hK1
    • Kallikrein serine protease 1
    • Kallikrein-1
    • Kidney/pancreas/salivary gland kallikrein
    • Klk 6
    • KLK1
    • KLK1_HUMAN
    • Klk6
    • KLKR
    • Tissue kallikrein
    see all
  • FunctionGlandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.
  • Tissue specificityIsoform 2 is expressed in pancreas, salivary glands, kidney, colon, prostate gland, testis, spleen and the colon adenocarcinoma cell line T84.
  • Sequence similaritiesBelongs to the peptidase S1 family. Kallikrein subfamily.
    Contains 1 peptidase S1 domain.
  • Post-translational
    modifications
    The O-linked polysaccharides on Ser-93, Ser-104 and Ser-167 are probably the mucin type linked to GalNAc. In PubMed:3163150, GalNAc was detected with the corresponding peptides but not located.
  • Information by UniProt

References for Natural human Kallikrein 1 protein (ab90351)

ab90351 has not yet been referenced specifically in any publications.

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