Recombinant Human Elastin/ELN Protein (His-tag)
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Recombinant Human Elastin/ELN Protein (His-tag) is a Human Fragment protein, expressed in Escherichia coli, with >95%, <0.005 EU/µg endotoxin level, suitable for Mass Spec, SDS-PAGE.
View Alternative Names
Elastin, Tropoelastin, ELN
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human Elastin/ELN Protein (His-tag) (AB322313)
SDS-PAGE analysis of ab322313 under reducing conditions for 2ug protein.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Elastin provides mechanical support and elasticity to tissues. It does so by being part of elastic fibers playing an important role in many connective tissue structures. The unique ability to stretch and return to its original shape allows tissues to resume their shape after stretching or contracting. Elastin is not part of larger protein complexes but interacts with other matrix proteins such as fibrillin to form a fibrous network required for the structural integrity of elastic tissues.
Pathways
Elastin plays an integral role in the extracellular matrix remodeling pathway which is important for maintaining tissue structure and function. It also participates in the TGF-beta signaling pathway where elastin interacts indirectly with proteins such as fibrillin-1 and fibulin. These interactions influence cellular processes like proliferation and differentiation highlighting elastin's involvement in both maintaining tissue elasticity and cell signaling.
Specifications
Form
Lyophilized
General info
Function
Major 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 (By similarity).
Sequence similarities
Belongs to the elastin family.
Post-translational modifications
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.
Target data
Product promise
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