Natural Cow Elastin protein (FITC) (ab123533)



  • NatureNatural
  • SourceNative
  • Amino Acid Sequence
    • AccessionP04985
    • SpeciesCow
    • Molecular weight61 kDa
    • Amino acids27 to 747
    • Additional sequence informationSource = bovine neck ligament elastin
  • ConjugationFITC. Ex: 493nm, Em: 528nm

Associated products


Our Abpromise guarantee covers the use of ab123533 in the following tested applications.

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

  • FormLyophilised
  • Additional notesProtect from light.
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at -20°C. Store under Desiccating conditions.

General Info

  • Alternative names
    • Elastin
    • ELN
    • SVAS
    • Tropoelastin
    • WBS
    • WS
    see all
  • FunctionMajor structural protein of tissues such as aorta and nuchal ligament, which must expand rapidly and recover completely. Molecular determinant of the late arterial morphogenesis, stabilizing arterial structure by regulating proliferation and organization of vascular smooth muscle.
  • Tissue specificityExpressed within the outer myometrial smooth muscle and throughout the arteriolar tree of uterus (at protein level). Also expressed in the large arteries, lung and skin.
  • Involvement in diseaseDefects in ELN are a cause of autosomal dominant cutis laxa (ADCL) [MIM:123700]. Cutis laxa is a rare connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. The skin changes are often accompanied by extracutaneous manifestations, including pulmonary emphysema, bladder diverticula, pulmonary artery stenosis and pyloric stenosis.
    Defects in ELN are the cause of supravalvular aortic stenosis (SVAS) [MIM:185500]. SVAS is a congenital narrowing of the ascending aorta which can occur sporadically, as an autosomal dominant condition, or as one component of Williams-Beuren syndrome.
    Note=ELN is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of ELN may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease.
  • Sequence similaritiesBelongs to the elastin family.
  • Post-translational
    Elastin is formed through the cross-linking of its soluble precursor tropoelastin. Cross-linking is initiated through the action of lysyl oxidase on exposed lysines to form allysine. Subsequent spontaneous condensation reactions with other allysine or unmodified lysine residues result in various bi-, tri-, and tetrafunctional cross-links. The most abundant cross-links in mature elastin fibers are lysinonorleucine, allysine aldol, desmosine, and isodesmosine.
    Hydroxylation on proline residues within the sequence motif, GXPG, is most likely 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates.
  • Cellular localizationSecreted > extracellular space > extracellular matrix. Extracellular matrix of elastic fibers.
  • Information by UniProt

References for Natural Cow Elastin protein (FITC) (ab123533)

ab123533 has not yet been referenced specifically in any publications.

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