Recombinant Mouse Transmembrane Protease Serine 6 (TMPRSS6) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-08685P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.
Based on the SEQUEST from database of Baculovirus host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Baculovirus-expressed Mus musculus (Mouse) Tmprss6.
Based on the SEQUEST from database of Baculovirus host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Baculovirus-expressed Mus musculus (Mouse) Tmprss6.
Based on the SEQUEST from database of Baculovirus host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Baculovirus-expressed Mus musculus (Mouse) Tmprss6.
Based on the SEQUEST from database of Baculovirus host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Baculovirus-expressed Mus musculus (Mouse) Tmprss6.

Recombinant Mouse Transmembrane Protease Serine 6 (TMPRSS6) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-08685P
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Product Overview

Description Recombinant Mouse Transmembrane Protease Serine 6 (TMPRSS6) Protein (His&Myc) is produced by our Baculovirus expression system. This is a extracellular protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb Q9DBI0
Target Symbol TMPRSS6
Synonyms Tmprss6; Transmembrane protease serine 6; EC 3.4.21.-; Matriptase-2
Species Mus musculus (Mouse)
Expression System Baculovirus
Tag N-10His&C-Myc
Target Protein Sequence KAEVTVSQVYSGSLRVLNRHFSQDLGRRESIAFRSESAKAQKMLQELVASTRLGTYYNSSSVYSFGEGPLTCFFWFILDIPEYQRLTLSPEVVRELLVDELLSNSSTLASYKTEYEVDPEGLVILEASVNDIVVLNSTLGCYRYSYVNPGQVLPLKGPDQQTTSCLWHLQGPEDLMIKVRLEWTRVDCRDRVAMYDAAGPLEKRLITSVYGCSRQEPVMEVLASGSVMAVVWKKGMHSYYDPFLLSVKSVAFQDCQVNLTLEGRLDTQGFLRTPYYPSYYSPSTHCSWHLTVPSLDYGLALWFDAYALRRQKYNRLCTQGQWMIQNRRLCGFRTLQPYAERIPMVASDGVTINFTSQISLTGPGVQVYYSLYNQSDPCPGEFLCSVNGLCVPACDGIKDCPNGLDERNCVCRAMFQCQEDSTCISLPRVCDRQPDCLNGSDEEQCQEGVPCGTFTFQCEDRSCVKKPNPECDGQSDCRDGSDEQHCDCGLQGLSSRIVGGTVSSEGEWPWQASLQIRGRHICGGALIADRWVITAAHCFQEDSMASPKLWTVFLGKMRQNSRWPGEVSFKVSRLFLHPYHEEDSHDYDVALLQLDHPVVYSATVRPVCLPARSHFFEPGQHCWITGWGAQREGGPVSNTLQKVDVQLVPQDLCSEAYRYQVSPRMLCAGYRKGKKDACQGDSGGPLVCREPSGRWFLAGLVSWGLGCGRPNFFGVYTRVTRVINWIQQVLT
Expression Range 81-811aa
Protein Length Extracellular Domain
Mol. Weight 86.1 kDa
Research Area Cell Biology
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.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
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 Membrane-bound serine protease. Through the cleavage of cell surface HJV, a regulator of the expression of the iron absorption-regulating hormone hepicidin/HAMP, plays a role in iron homeostasis.
Subcellular Location Cell membrane; Single-pass type II membrane protein.
Protein Families Peptidase S1 family
Database References

KEGG: mmu:71753

STRING: 10090.ENSMUSP00000017086

UniGene: PMID: 29636509

  • Erythroferrone and matriptase-2 independently regulate hepcidin expression. PMID: 28187515
  • Data (including data from studies using knockout mice) suggest that Mt2/Tmprss6 suppresses hepcidin expression in hepatocytes independently of Hjv; Mt2/Tmprss6 cleaves Alk2, Alk3, ActRIIA, Bmpr2, Hfe, and, to a lesser extent, Hjv and Tfr2; thus, Mt2/Tmprss6 suppresses hepcidin expression by cleaving multiple components of the hepcidin induction pathway. (Mt2/Tmprss6 = matriptase-2; Hjv = hemojuvelin) PMID: 28924039
  • Studies in colonic T84 cell monolayers revealed that barrier disruption by the colitis-associated Th2-type cytokines, IL-4 and IL-13, down-regulates matriptase as well as prostasin through phosphorylation of the transcriptional regulator STAT6 PMID: 28490634
  • the function of matriptase-2 is dominant over that of ERFE and is essential in facilitating hepcidin suppression by attenuating the BMP-SMAD signaling. PMID: 26755707
  • role of fetuin-A in iron homeostasis and provide new insights into the mechanism of how matriptase-2 might modulate hepcidin expression PMID: 25205713
  • TMPRSS6 inhibition via decreased STAT5 phosphorylation may be an additional mechanism by which inflammation stimulates hepcidin expression to regulate iron homeostasis and immunity. PMID: 24376517
  • matriptase-2 (encoded by Tmprss6)-is responsible for hepcidin repression throughout development, with its deficiency leading to increased hepcidin levels triggering iron deficiency and anemia starting in utero PMID: 24904115
  • The iron-regulatory serine protease matriptase-2 is expressed in the retina, and absence of this enzyme leads to iron deficiency. PMID: 24791141
  • Results confirm the anti-inflammatory status of Tmprss6 KO mice and identify new potential target pathways/genes of Tmprss6. PMID: 23922777
  • Tmprss6 gene knockdown reduces iron overload in an animal model of hemochromatosis and improves both iron overload and anemia in mice affected by beta-thalassemia. PMID: 23524968
  • Double mutant mice lacking functional Hfe or Tfr2 and Tmprss6 exhibited a severe iron deficiency microcytic anemia phenotype mimicking the phenotype of single mutant mice lacking functional Tmprss6 demonstrating that Hfe and Tfr2 are not substrates for Tmprss6. PMID: 22244935
  • Preventing iron overload improves beta-thalassemia and strengthens the essential role of Tmprss6 for Hamp suppression, providing a proof of concept that Tmprss6 manipulation can offer a novel therapeutic option in this condition. PMID: 22490684
  • Heterozygous loss of Tmprss6 in Hfe(-/-) mice reduced systemic iron overload, whereas homozygous loss caused systemic iron deficiency and elevated hepatic expression of hepcidin and other Bmp/Smad target genes PMID: 21355094
  • Loss of TMPRSS6 is associated with iron-deficiency anemia and involves up-regulation of Bmp/Smad signaling. PMID: 20200349
  • identification, characterization and comparative mRNA expression analysis with mouse hepsin in adult and embryonic tissues PMID: 12744720
  • identification, structural features, enzymology, expression pattern and potential roles of TMPRSS6 [review] PMID: 17981570
  • findings show that TMPRSS6 is an essential component of a pathway that detects iron deficiency and blocks Hamp transcription, permitting enhanced dietary iron absorption PMID: 18451267
  • matriptase-2 activity represents a novel and relevant step in hepcidin regulation and iron homeostasis PMID: 18523150
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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.

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