Recombinant Human Matrilin-3 (MATN3) Protein (His&Myc)

Name: Recombinant Human Matrilin-3 (MATN3) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-04825P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Matrilin-3 (MATN3) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O15232
Target Symbol	MATN3
Synonyms	AV009181; DIPOA; EDM5; HOA; MATN3; MATN3_HUMAN; Matrilin 3; Matrilin-3; OADIP; OS2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	DPVARPGFRRLETRGPGGSPGRRPSPAAPDGAPASGTSEPGRARGAGVCKSRPLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGPADTRVAVVNYASTVKIEFQLQAYTDKQSLKQAVGRITPLSTGTMSGLAIQTAMDEAFTVEAGAREPSSNIPKVAIIVTDGRPQDQVNEVAARAQASGIELYAVGVDRADMASLKMMASEPLEEHVFYVETYGVIEKLSSRFQETFCALDPCVLGTHQCQHVCISDGEGKHHCECSQGYTLNADKKTCSALDRCALNTHGCEHICVNDRSGSYHCECYEGYTLNEDRKTCSAQDKCALGTHGCQHICVNDRTGSHHCECYEGYTLNADKKTCSVRDKCALGSHGCQHICVSDGAASYHCDCYPGYTLNEDKKTCSATEEARRLVSTEDACGCEATLAFQDKVSSYLQRLNTKLDDILEKLKINEYGQIHR
Expression Range	29-486aa
Protein Length	Full Length of Mature Protein
Mol. Weight	57.2 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Major component of the extracellular matrix of cartilage and may play a role in the formation of extracellular filamentous networks.
Subcellular Location	Secreted.
Database References	HGNC: 6909 OMIM: 140600 KEGG: hsa:4148 STRING: 9606.ENSP00000383894 UniGene: Hs.656199
Associated Diseases	Multiple epiphyseal dysplasia 5 (EDM5); Spondyloepimetaphyseal dysplasia MATN3-related (SEMD-MATN3); Osteoarthritis 2 (OS2)
Tissue Specificity	Expressed only in cartilaginous tissues, such as vertebrae, ribs and shoulders.

Gene Functions References

miR-448 contributed to the progression of osteoarthritis by directly targeting matrilin-3. PMID: 29483929
Study confirmed that MATN3 protein was highly expressed in GAC patients, and MATN3 overexpression could be used as an independent predictor of poor prognosis in GAC patients. PMID: 29343680
our results revealed miR-483-5p directly targeted to the cartilage matrix protein matrilin 3 (Matn3) and tissue inhibitor of metalloproteinase 2 (Timp2) to stimulate chondrocyte hypertrophy, extracellular matrix degradation, and cartilage angiogenesis, and it consequently initiated and accelerated the development of OA. PMID: 28139355
The results of the study indicate a potential role for the MATN3 rs28598872 polymorphism in the pathogenesis of Temporomandibular Joint Internal Derangement. PMID: 27533128
This report is the first to show the involvement of MATN3 in C-type natriuretic peptide/natriuretic peptide receptor-B signaling pathway during the process of transforming growth factor-beta induced chondrogenic differentiation of mesenchymal stem cells. PMID: 24934313
MATN3 plays a regulatory role in cartilage homeostasis due to its capacity to induce IL-1Ra, upregulate gene expression of major cartilage matrix components, and downregulate the expression of OA-associated matrix-degrading proteinases in chondrocytes. PMID: 22967398
MATN3 may have the inherent ability to inhibit premature chondrocyte hypertrophy by suppressing BMP-2/Smad1 activity PMID: 25331953
The VWA1 domain of matrilin-3 is primarily responsible for the induction of IL-6 release from primary human chondrocytes. PMID: 23523902
Polymorphism in the MATN3 gene might play a role in osteoarthritis in the Chinese Han population. PMID: 22973175
Haplotype-4 of MATN3 is associated with vertebral fracture risk independent of bone mineral density in Chinese postmenopausal women. PMID: 22270056
MATN3 mutations were identified in 13 multiple epiphyseal dysplasia patients and comprised predominantly of missense mutations. PMID: 21922596
Radiographic findings in patients with COMP and MATN3 mutations showed marked abnormalities in hip and knee joints. PMID: 21965141
a matrilin-3 mutation associated with osteoarthritis does not affect collagen affinity but promotes the formation of wider cartilage collagen fibrils PMID: 20077500
increased expression of MATN3 in osteoarthritis might contribute to the degeneration of articular cartilage. PMID: 18759284
potential of matrilin-3 to modulate gene expression profile of primary chondrocytes; tested matrilin3-dependent induction of pro-inflammatory cytokines, inducible nitric oxide synthetase & cyclooxygenase-2, MMP1, -3 & -13, & matrilin-3 itself PMID: 19840795
Mutation in MATN3 had significant association for patients with osteoarthritis. PMID: 12736871
Four novel missense mutations and one recurrent missense mutation were identified in MATN3 in seven families with multiple epiphyseal dysplasia. PMID: 14729835
MATN3 mutations is associated with multiple epiphyseal dysplasia PMID: 14994237
Contrary to the previous assumption that the MATN3 mutation in multiple epiphyseal dysplasia is confined to the beta-sheet regions, one novel mutation is located outside the beta-sheet region, within an alpha-helix region PMID: 15459972
COMP, type IX collagen and MATN3 play important roles in matrix assembly PMID: 15694129
mutations in matrilin-3 causing chondrodysplasias (R116W and C299S) interfere with intracellular protein trafficking and formation of filamentous extracellular structures PMID: 16199550
Multiple epiphyseal dysplasia caused by MATN3 mutations is the result of an intracellular retention of the mutant protein. PMID: 16287128
Patients carrying the T(303)M mutation in the gene for matrilin-3 express a form of HOA that is radiologically indistinguishable from idiopathic HOA in individual patients but they have more severe thumb-base involvement, particularly in the STT joint. PMID: 16641049
We have demonstrated intergenic splicing between two sets of family genes, the matrilin-3 (MATN3) and lysosomal-associated protein transmembrane 4alpha (LAPTM4A). PMID: 16769693
recombinant ADAMTS-4 effectively cleaved intact matrilin-3 at the predicted motif at Glu435/Ala436 generating two species of 45 and 5 kDa PMID: 17311924
a matn3 mutation causes decreased chondrocyte proliferation and dysregulated apoptosis leading to epiphyseal dysplasia PMID: 17517694
the matrilin-3 A-domain appears to bind exclusively to the COL3 domain of type IX collagen and this binding is abolished in the presence of a disease causing mutation in type IX collagen PMID: 17881354
The characterization of two additional alpha-helical mutations (p.Ala173Asp and p.Lys231Asn) is described. Both p.Phe105Ser and pAla173Asp prevent the secretion of A-domain in vitro. PMID: 18205203

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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.