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Recombinant Human LOXL2 Protein(His tag) (HH0192LL)

Recombinant Human LOXL2 Protein (Q9Y4K0) (Met 1-Gln 774) with a polyhistidine tag at the C-terminus was expressed in HEK293.

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10ug $429.00
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PRODUCT INFORMATION

Cat.No.
HH0192LL
Synonyms
LOXL2; WS9 14; LOR2; WS9-14
Species
Human
Accession
Source
HEK293
Tag
His
Predicted N Terminal
Gln 26
Form
Lyophilized from sterile PBS, pH 7.4, 5 % trehalose and 5 % mannitol.
Bio-activity
Measured by its ability to produce hydrogen peroxide during the oxidation of benzylamine. The specific activity is> 2 pmoles/min/μg.
Molecular Mass
Recombinant Human LOXL2 consists of 760 amino acids and has a predicted molecular mass of 85.5 kDa. The apparent molecular mass of rhLOXL2 is approximately 100 & 60 KDa in SDS-PAGE under reducing conditions, corresponding to the unprocessed and processed form
respectively.
Endotoxin
< 1.0 EU per 1 microgram of protein (determined by LAL method).
Purity
> 60 % by SDS-PAGE.

BACKGROUND

Background
Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). When secreted in extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. When nuclear, acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E-cadherin, probably by mediating deamination of histone H3. Also involved in E-cadherin repression following hypoxia, a hallmark of epithelial to mesenchymal transition believed to amplify tumor aggressiveness, suggesting that it may play a role in tumor progression. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation.
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