Overview

Description

  • Nature
    Synthetic
  • Amino Acid Sequence
    • Species
      Human
    • Sequence
      CQSRRCRKNAFQEL
    • Amino acids
      637 to 650

Associated products

Specifications

Our Abpromise guarantee covers the use of ab45734 in the following tested applications.

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

  • Applications

    Blocking - Blocking peptide for Anti-ADAM33 antibody (ab36172)

  • Form
    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.

General Info

  • Alternative names
    • A disintegrin and metalloprotease 33
    • A disintegrin and metalloproteinase domain 33
    • ADA33_HUMAN
    • ADAM 33
    • ADAM metallopeptidase domain 33
    • ADAM33
    • C20orf153
    • Disintegrin and metalloproteinase domain-containing protein 33
    • Disintegrin and reprolysin metalloproteinase family protein
    • DJ964F7.1
    • DKFZp434K0521
    • FLJ35308
    • FLJ36751
    • Metalloprotease disintegrin
    • MGC149823
    • MGC71889
    • PRO1891
    • UNQ873
    see all
  • Tissue specificity
    Expressed in all tissues, except liver, with high expression in placenta, lung, spleen and veins.
  • Involvement in disease
    Genetic variations in ADAM33 are associated with susceptibility to asthma (ASTHMA) [MIM:600807]. The most common chronic disease affecting children and young adults. It is a complex genetic disorder with a heterogeneous phenotype, largely attributed to the interactions among many genes and between these genes and the environment. It is characterized by recurrent attacks of paroxysmal dyspnea, with weezing due to spasmodic contraction of the bronchi.
  • Sequence similarities
    Contains 1 disintegrin domain.
    Contains 1 EGF-like domain.
    Contains 1 peptidase M12B domain.
  • Domain
    The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
  • Post-translational
    modifications
    The precursor is cleaved by a furin endopeptidase.
  • Cellular localization
    Membrane.
  • Information by UniProt

References

ab45734 has not yet been referenced specifically in any publications.

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

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