Recombinant Mouse LOXL2 Protein (His Tag)

Name: Recombinant Mouse LOXL2 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-3224
Availability: InStock

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Enzymes, Protease, Recombinant proteins

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Product Overview

Tag	His
Host Species	Mouse
Accession	NP_201582.2
Synonym	1110004B06Rik, 4930526G11Rik, 9430067E15Rik
Background	Lysyl oxidase homolog 2, also known as Lysyl oxidase-like protein 2, Lysyl oxidase-related protein 2, Lysyl oxidase-related protein WS9-14 and LOXL2, is a secreted protein which belongs to thelysyl oxidase family. LOXL2 contains fourSRCR domains. The lysyl oxidase family is made up of five members: lysyl oxidase (LOX) and lysyl oxidase-like 1-4 ( LOXL1, LOXL2, LOXL3, LOXL4 ). All members share conserved C-terminal catalytic domains that provide for lysyl oxidase or lysyl oxidase-like enzyme activity; and more divergent propeptide regions. LOX family enzyme activities catalyze the final enzymatic conversion required for the formation of normal biosynthetic collagen and elastin cross-links. LOXL2 is expressed by pre-hypertrophic and hypertrophic chondrocytes in vivo, and that LOXL2 expression is regulated in vitro as a function of chondrocyte differentiation. LOXL2 promotes chondrocyte differentiation by mechanisms that are likely to include roles as both a regulator and an effector of chondrocyte differentiation. LOXL2 expression could also be explored as a molecular target in the prevention of breast cancer progression.
Description	A DNA sequence encoding the mouse Loxl2 (NP_201582.2) (Met1-Gln776) was expressed with a His tag at the C-terminus.
Source	HEK293
Predicted N Terminal	Gln 26
AA Sequence	Met1-Gln776
Molecular Weight	The recombinant mouse Loxl2 consists 762 a.a. and predicts a molecular mass of 85.9 kDa.
Purity	>(19.0+61.5)% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg protein as determined by the LAL method.
Bioactivity	Measured by its ability to produce hydrogen peroxide during the oxidation of benzylamine.The specific activity is > 3pmoles/min/ug.
Formulation	Lyophilized from sterile 20 mM MES, 150 mM NaCl, pH 6.5..
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription. LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency including POU5F1/OCT4, NANOG, KLF4 and SOX2. 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. During EMT, involved with SNAI1 in negatively regulating pericentromeric heterochromatin transcription. SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits. Interacts with the endoplasmic reticulum protein HSPA5 which activates the IRE1-XBP1 pathway of the unfolded protein response, leading to expression of several transcription factors involved in EMT and subsequent EMT induction. When secreted into the 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. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation.
Subcellular Location	Secreted, extracellular space, extracellular matrix, basement membrane. Nucleus. Chromosome. Endoplasmic reticulum.
Protein Families	Lysyl oxidase family
Database References	KEGG: mmu:94352 STRING: 10090.ENSMUSP00000022660 UniGene: Mm.116714
Tissue Specificity	Ubiquitous. Highest expression in skin, lung and thymus. Present in chondrocytes: mainly expressed by chondrocytes in healing fractures and in epiphyseal growth plates (at protein level).

Gene Functions References

although Loxl2 is expressed in both dermis and epidermis, its function appears largely confined to the epidermis. PMID: 29953488
LOXL2 controls myofibroblast transformation and migration. PMID: 27966531
The mRNA and protein expression levels of LOXL2 were higher in a mouse model of tubulointerstitial fibrosis compared with in control mice. PMID: 28677767
Findings indicate a pathophysiologic role and function for lysyl oxidase-like protein LOXL2 in breast cancer metastasis. PMID: 28720577
Insulin resistance promotes lysyl oxidase like 2 induction and fibrosis accumulation in non-alcoholic fatty liver disease. PMID: 28468951
glomerular extracellular matrix. Altogether, we demonstrate that LOXL2 is a novel component of the molecular machinery that forms cross-linked collagen IV networks, which are essential for glomerular basement membrane stability and molecular ultrafiltration function. PMID: 27770022
LOX and LOXL2 may play an important role in the pathogenesis of AMD. Targeting LOXL2 could have a broader efficacy than targeting LOX, by reducing angiogenesis and inflammation, as well as fibrosis. PMID: 26258612
Loss and gain of function analyses combined with in vivo studies in syngeneic breast cancer models demonstrate the participation of LOXL2 and E47 in tumor growth and their requirement for lung metastasis. PMID: 24632622
promoted intrahepatic metastasis by increasing tissue stiffness PMID: 25048396
Findings reveal new insight into the mechanisms of fibroblast activation, a novel function of LOXL2, and further highlight the importance of generating LOXL2-targeted therapies for the prevention of tumor progression and metastasis. PMID: 24008674
The Snail1 transcription factor represses mouse pericentromeric transcription, acting through the H3K4 deaminase LOXL2. PMID: 24239292
The enzymatic activity of lysyl oxidas-like-2 (LOXL2) is not required for LOXL2-induced inhibition of keratinocyte differentiation. PMID: 22157764
This study provides the first evidence for the role of LOXL2 in regulating angiogenesis through collagen IV scaffolding. PMID: 21835952
LOXL2 promotes chondrocyte differentiation by mechanisms that are likely to include roles as both a regulator and an effector of chondrocyte differentiation PMID: 21071451
The efficacy and safety of LOXL2-specific monoclonal antibody represents a new therapeutic approach with broad applicability in oncologic and fibrotic diseases. PMID: 20818376
LoxL2 is not expressed in MC3T3-E1 cells. PMID: 15652501

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.