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AB322313

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

1 Images
SDS-PAGE - Recombinant Human Elastin/ELN Protein (His-tag) (AB322313)
  • 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.

Key facts

Purity

>95% HPLC

Endotoxin level

<0.005 EU/µg

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

Mass Spec, SDS-PAGE

applications

Biologically active

No

Mass Spectrometry

LC-MS/MS

Accession

P15502

Animal free

Yes

Carrier free

No

Species

Human

Reconstitution

Lyophilized contents may appear as either a translucent film or a white powder. This variance does not affect the quality of the product. Store lyophilized form at room temperature. Reconstitute in phosphate buffered saline, aliquot and store at -80°C for 12 months or +4°C for 1 week. Avoid repeated freeze-thaw.

Storage buffer

pH: 7.9 Constituents: 6.4993% Trehalose, 2.4309% Sodium chloride, 0.3819% Sodium bicarbonate

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"GGIPTYGVGAGGFPGFGVGVGGIPGVAGVPGVGGVPGVGGVPGVGISPEAQAAAAAKAAKYGAAGAGVLGGLVPGAPGAVPGVPGTGGVPGVGTPAAAAAKAAAKAAQFGLVPGVGVAPGVGVAPGVGVAPGVGLAPGVGVAPGVGVAPGVGVAPGIGPGGVAAAAKSAAKVAAKAQLRAAAGLGAGIPGLGVGVGVPGLGVGAGVPGLGVGAGVPGFGAGADEGVRRSLSPELREGDPSSSQHLPSTPSSPRV","proteinLength":"Fragment","predictedMolecularWeight":"23.61 kDa","actualMolecularWeight":"23.48 kDa","aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P15502","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
Ambient
Appropriate long-term storage conditions
Ambient
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Elastin also known as elastin protein is an essential component of the extracellular matrix known for imparting elasticity and resilience to tissues. With a molecular mass of approximately 60-70 kDa some scientists may also refer to it as elastin et. Elastin is expressed in elastic tissues such as the skin lungs and blood vessels. These tissues require the elastic properties provided by elastin. Additionally elastin forms the core of elastic fibers surrounded by a sheath of microfibrils.
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.

Elastin is linked to pathologies like Williams-Beuren syndrome and cutis laxa. Williams-Beuren syndrome associated with elastin deletions leads to cardiovascular issues while cutis laxa results in reduced elasticity of the skin due to elastin mutations. In these conditions elastin interacts with proteins such as fibrillin and fibulin contributing to the observed clinical manifestations. Understanding these interactions helps in diagnosing and developing therapeutic approaches for such disorders.

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.

Product protocols

Target data

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).
See full target information ELN

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