Recombinant Human Mannan-Binding Lectin Serine Protease 2 (MASP2) Protein (His)

Name: Recombinant Human Mannan-Binding Lectin Serine Protease 2 (MASP2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-01355P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Mannan-Binding Lectin Serine Protease 2 (MASP2) Protein (His) is produced by our Baculovirus expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	O00187
Target Symbol	MASP2
Synonyms	MBL-associated serine protease 2;Mannose-binding protein-associated serine protease 2;MASP-2
Species	Homo sapiens (Human)
Expression System	Baculovirus
Tag	C-6His
Target Protein Sequence	TPLGPKWPEPVFGRLASPGFPGEYANDQERRWTLTAPPGYRLRLYFTHFDLELSHLCEYDFVKLSSGAKVLATLCGQESTDTERAPGKDTFYSLGSSLDITFRSDYSNEKPFTGFEAFYAAEDIDECQVAPGEAPTCDHHCHNHLGGFYCSCRAGYVLHRNKRTCSALCSGQVFTQRSGELSSPEYPRPYPKLSSCTYSISLEEGFSVILDFVESFDVETHPETLCPYDFLKIQTDREEHGPFCGKTLPHRIETKSNTVTITFVTDESGDHTGWKIHYTSTAQPCPYPMAPPNGHVSPVQAKYILKDSFSIFCETGYELLQGHLPLKSFTAVCQKDGSWDRPMPACSIVDCGPPDDLPSGRVEYITGPGVTTYKAVIQYSCEETFYTMKVNDGKYVCEADGFWTSSKGEKSLPVCEPVCGLSARTTGGRIYGGQKAKPGDFPWQVLILGGTTAAGALLYDNWVLTAAHAVYEQKHDASALDIRMGTLKRLSPHYTQAWSEAVFIHEGYTHDAGFDNDIALIKLNNKVVINSNITPICLPRKEAESFMRTDDIGTASGWGLTQRGFLARNLMYVDIPIVDHQKCTAAYEKPPYPRGSVTANMLCAGLESGGKDSCRGDSGGALVFLDSETERWFVGGIVSWGSMNCGEAGQYGVYTKVINYIPWIENIISDF
Expression Range	16-686aa
Protein Length	Full Length of Mature Protein
Mol. Weight	79.3 kDa
Research Area	Cardiovascular
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	Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase.
Subcellular Location	Secreted.
Protein Families	Peptidase S1 family
Database References	HGNC: 6902 OMIM: 605102 KEGG: hsa:10747 STRING: 9606.ENSP00000383690 UniGene: PMID: 28303635 The complement lectin pathway serine proteases, MASP-1 and MASP-2, can be associated with ischaemic stroke development risk and may participate in pathological events leading to post-ischaemic brain damage. Moreover rs3203210 and rs147270785 single nucleotide polymorphisms in the MASP1 and MASP2 genes, respectively, are strongly associated with ischaemic stroke. PMID: 28720568 The results of this study show that MASP-2 contributes to severity and outcome in pneumococcal meningitis. In patients with pneumococcal meningitis, MASP-2 concentration was elevated in the CSF and high levels were associated with poor functional outcome. PMID: 28086930 Genetically determined MASP-2 levels seem to have a two-edge effect in HIV and probably HCV/HBV coinfection, whereas low levels increase the susceptibility to infection, but on the other side protects against AIDS. PMID: 27588826 MASP-2 was not associated with adverse cardiovascular outcomes in diabetics. PMID: 27055907 This is the first comprehensive meta-analysis indicates that the MASP-2 functional gene (rs72550870) polymorphism is not associated with the infection diseases, and the key functional gene polymorphism of rs72550870 did not increase susceptibility to the infection diseases. PMID: 27725284 This study suggests that hMASP-2 can induce a protective efficacy in BCG-infected rabbit skin models, which affects both the progress of lesions and the survival of the mycobacteria within them. PMID: 27585546 genotype not associated with acute cellular rejection after kidney transplantation PMID: 26924055 The ficolin-3/MASP-2 complex was significantly lower in the cardiac syndrome X patients compared to controls. PMID: 27312152 MASP-1 and MASP-2 are activated during blood clotting. This activation is triggered by activated platelets and by the generation of fibrin during thrombotic reactions in vitro and in vivo, and may represent a novel activation/amplification mechanism in thromboinflammation. PMID: 26614707 MBL2 and MASP2 deficiencies protect against the development of systemic inflammatory response after pediatric cardiac surgery. PMID: 26382056 Data show that the vector expressing mannose-binding lectin associated protein 19 (MAp19) has been prepared successfully, and can express the target protein (MAp19) in the eukaryotic cells (HeLa cells). PMID: 26728378 polymorphism of MASP-2 (rs6695096) gene was associated with susceptibility to tuberculosis. PMID: 25312983 Polymorphisms of mannose-binding lectin (rs7096206) and MASP-2 (rs2273346 and rs6695096) were associated with the susceptibility of tuberculosis, and there were gene-gene interactions among them. PMID: 25887173 Polymorphisms in MASP1 and MASP2 genes are associated with the susceptibility or protection to infectious diseases. (Review) PMID: 25862418 MASP2 gene polymorphisms and protein levels seem to play an important role in the development of rheumatic fever and establishment of rheumatic heart disease. PMID: 25318078 Because MASP-1 and MASP-2 have been shown to interact directly with blood coagulation, elevated levels of these proteins may play a role in the enhanced thrombotic environment and consequent vascular complications in diabetes. PMID: 25533914 TFPI inhibits lectin pathway of complement activation by direct interaction with MASP-2. PMID: 25359215 expression of MBL and MASP-2 is altered in ovarian cancer, possibly indicating involvement of the lectin pathway of complement activation in the disease PMID: 25038892 Both ficolin-3 and MASP-2 levels correlated inversely with the time from the onset of the attack of hereditary angioedema until blood sampling PMID: 25042985 Study found the first evidence that MASP-2 deficiency might play an important role in the development of RA and articular symptoms among relatives of RA patients. PMID: 24632598 Bipolar disorder is associated with the MBL2 LXPA haplotype and lower MASP-2 levels. PMID: 24856568 Data indicate that MASP-1 and MASP-2 can readily form heterodimers after dissociation and re-association, however, in the presence of Ca(2+) exchange of subunits is slow between the homodimers. PMID: 24424083 low MASP-2 levels increase the susceptibility to leprosy in general and to lepromatous leprosy in particular. MASP2 genotypes and MASP-2 levels might thus be of prognostic value for leprosy progression. PMID: 23935922 The present study describes an association between a polymorphism in the MASP2 gene and susceptibility to HTLV-1 infection, and provides further evidence of an association between the MBL2 gene and HTLV-1 infection. PMID: 23861212 MASP-2 levels in the peripheral circulation are significantly reduced in myocardial infarction (MI) patients compared with those of healthy individuals or of coronary artery disease (CAD) patients without acute MI. PMID: 22178059 results show that SNPS in MASP2 are significantly more susceptible to infectious complications, SIRS and septic shock. PMID: 24227370 Studies indicate that initiation of lectin compleme pathway leads to activation of the serine proteases MASP-1 and MASP-2 resulting in deposition of C4 on the activator and assembly of the C3 convertase. PMID: 23911397 collectin-11 associates with all the known MBL-associated serine proteases (MASP-1, MASP-2 and MASP-3) as well as the lectin complement pathway regulator MAP-1. PMID: 23220946 In this study, we demonstrate that, although MASPs do not directly form heterodimers, the addition of mannan-binding lectin or ficolins allows the formation of MASP-1-MASP-2 co-complexes. PMID: 23785123 Data indicate that the median concentration of MASP-2/ficolin-3 complexes was 119.7 AU/ml (range: 2.9-615.5 AU/ml). PMID: 23142462 MASP-2 is a key enzyme that cleaves C4 and C2 to assemble a C3 convertase--{review} PMID: 23402018 A crucial role of MASP-1 is demonstrated in the activation of MASP-2, as well as of MASP-3, based on a patient harboring a nonsense mutation in the common part of the MASP1 gene. PMID: 22966085 Monospecific inhibitors show that both mannan-binding lectin-associated serine protease-1 (MASP-1) and -2 Are essential for lectin pathway activation and reveal structural plasticity of MASP-2. PMID: 22511776 MASP-1 activates MASP-2 and, moreover, inhibition of MASP-1 prevents autoactivation of MASP-2 PMID: 22691502 A common MASP2 mutation (R439H, rs12085877), was protective against placental malaria and occurred in 33% of non-affected women. PMID: 22380611 Data show no association of donor and recipient MBL2 and MASP2 genotype with allograft outcome, and analysis of SNPs and haplotypes in the FCN2 gene of the donor and recipient did not reveal an association with transplant outcome. PMID: 22173059 Interactions required for the cleavage of C4 by MASP-2 are likely to be facilitated by the initial binding of C4 to an exosite on the protease. PMID: 22071314 In patients with haematological malignancy undergoing chemotherapy, those with low M-ficolin levels were more likely to develop severe infections. PMID: 22236007 It is postulated that the elevation of concentration of the two components of the leptin pathway, L-ficolin and MASP-2, may compensate for the insufficient activity of the LP in mannose-binding lectin deficiency. PMID: 21974696 Data show that both MAp19 and MASP-2 were mainly expressed in hepatocytes. PMID: 21871896 MASP2 gene polymorphism is associated with susceptibility to hepatitis C virus infection. PMID: 21843573 Results suggest that MBL and MASP-2 play only a minor role in the inflammatory response in acute pancreatitis. PMID: 21926545 MASP2*CD genotypes, most of them generating low MASP-2 levels, are associated with high risk of chagasic cardiomyopathy PMID: 21489885 binding of Mannan Binding Lectin to hepatitis C virus glycoproteins was able to activate the complement system via MBL-associated serine protease 2 PMID: 21203938 In contrast to what has been demonstrated for serum levels of mannan-binding lectin (MBL) and MBL-associated serine protease 2, the genotypes do not predict disease course of the colorectal cancer patients PMID: 21198752 Donor and recipient gene polymorphisms in the lectin complement pathway (MBL2, FCN2, MASP2) are major determinants of the risk of clinically significant bacterial infection and mortality after orthotopic liver transplantation. PMID: 20593422 MASP-1 has a crucial role in the initiation steps of lectin pathway activation most probably by activating MASP-2 PMID: 20817870 The MASP2-mediated release of FPA and FPB may play a role in early immune activation. Additionally, MASP-catalysed deposition and polymerization of fibrin on the surface of micro-organisms may be protective by limiting the dissemination of infection. PMID: 20002787 the outcome of intensive care unit (ICU) patients with systemic inflammatory response syndrome (SIRS) regarding the existence of functionally relevant MBL2 and MASP2 gene polymorphisms was studied PMID: 20042521

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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.

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