Recombinant Human Lumican protein (rFc Tag)

Species

Human

Purity

>90 %, SDS-PAGE

Tag

rFc Tag

Activity

not tested

Cat no : Eg2923



Product Information

Purity >90 %, SDS-PAGE
Endotoxin <0.1 EU/μg protein, LAL method
Activity
Not tested
Expression HEK293-derived Human Lumican protein Gln19-Asn338 (Accession# P51884) with a rabbit IgG Fc tag at the C-terminus.
GeneID 4060
Accession P51884
PredictedSize 62.7 kDa
SDS-PAGE 65-75 kDa, reducing (R) conditions
Formulation Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
Reconstitution Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
Storage Conditions
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

Lumican (LUM), a member of the small leucine-rich proteoglycan (SLRP) family, is one of the major extracellular components in interstitial collagenous matrices of the corneal stroma, aorta, skin, skeletal muscle, lung, kidney, bone, cartilage, and intervertebral discs. SLRPs constitute an important fraction of noncollagenous extracellular matrix proteins and have important effects on cell behavior. Lumican regulates collagenous matrix assembly as a keratan sulfate proteoglycan in the cornea and may exist as a glycoprotein in the connective tissues of other organs. Posttranslational modifications lumican goes through can increase its apparent molecular weight to 50-90 kDa. Studies show that lumican participates in the maintenance of tissue homeostasis and modulates cellular functions including cell proliferation, migration, and differentiation.

References:

1. Nikitovic D. et al. (2008) IUBMB Life. 60(12):818-23. 2. Liu CY. et al. (2012) Methods Mol Biol. 836:285-90. 3. Dolhnikoff M. et al. (1998) Am J Respir Cell Mol Biol. 19(4):582-7. 4. Yang CH. et al. (2012) Vet J. 193(2):374-80.