Recombinant Human Mannan-binding lectin serine protease 1(MASP1)

Code CSB-EP013508HU
Size US$1726
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names MASP1
Uniprot No. P48740
Research Area Immunology
Alternative Names MASP1; CRARF; CRARF1; PRSS5Mannan-binding lectin serine protease 1; EC 3.4.21.-; Complement factor MASP-3; Complement-activating component of Ra-reactive factor; Mannose-binding lectin-associated serine protease 1; MASP-1; Mannose-binding protein-associated serine protease; Ra-reactive factor serine protease p100; RaRF; Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain]
Species Homo sapiens (Human)
Source E.coli
Expression Region 20-699aa
Target Protein Sequence HTVELNNMFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGSFMSITFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDIFDIEDHPEVPCPYDYIKIKVGPKVLGPFCGEKAPEPISTQSHSVLILFHSDNSGENRGWRLSYRAAGNECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDTFQIECLKDGTWSNKIPTCKIVDCRAPGELEHGLITFSTRNNLTTYKSEIKYSCQEPYYKMLNNNTGIYTCSAQGVWMNKVLGRSLPTCLPVCGLPKFSRKLMARIFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSLDPEDPTLRDSDLLSPSDFKIILGKHWRLRSDENEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQQEGAMVIVSGWGKQFLQRFPETLMEIEIPIVDHSTCQKAYAPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTLNRERGQWYLVGTVSWGDDCGKKDRYGVYSYIHHNKDWIQRVTGVRN
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 93.0kDa
Protein Length Full Length of Mature Protein
Tag Info N-terminal 6xHis-SUMO-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

Target Data

Function Functions in the lectin pathway of complement, which performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them. The lectin pathway is triggered upon binding of mannan-binding lectin (MBL) and ficolins to sugar moieties which leads to activation of the associated proteases MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2 or C2 or directly activate C3 the key component of complement reaction. Isoform 2 may have an inhibitory effect on the activation of the lectin pathway of complement or may cleave IGFBP5.
Gene References into Functions
  1. PTX-3 and MASP-3 enhanced prediction of myocardial infarction compared to the traditional Framingham risk score alone PMID: 28216633
  2. Study proposes that RaRF may be a factor in the resistance mechanism and thus a potential target for leukemia therapy using retinoic acid. PMID: 28945224
  3. We present the first case with an intragenic MASP1 deletion featuring 3MC syndrome. Our patient features typical 3MCS symptoms and a characteristic face but no cleft lip/palate. PMID: 29407414
  4. Studies results provide evidence that Crohn's disease patients have an impairment in mannose-binding lectin-mannose-associated serine protease functional activity and that this defect is associated with mannose-binding lectin 2 and NOD2 variants. PMID: 27404661
  5. These results indicate that PLTP and MASP-1 can serve as plasma biomarkers for the early diagnosis and treatment of Age-related macular degeneration , which is critical for preventing Age-related macular degeneration -related blindness. PMID: 27605007
  6. MASP-3 is the exclusive pro-factor D activator in resting blood: the lectin and the alternative complement pathways are fundamentally linked. PMID: 27535802
  7. a strong influence of MASP-1, complement activation and pathway-specific inhibition on coagulation in a microvascular flow system PMID: 29324883
  8. 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
  9. Our finding suggests that complement MASP-1 can increase adhesion between neutrophils and endothelial cells in a direct fashion PMID: 27219453
  10. Study discovered novel and independent associations of prediabetes and related traits with MASP1, and some evidence for associations with THBS1, GPLD1 and ApoA-IV, suggesting a role for these proteins in the pathophysiology of type 2 diabetes. PMID: 27344311
  11. MASP-1 plasma levels were higher among patients with type 2 diabetes and diabetic mice PMID: 28318015
  12. MASP-1 was not associated with adverse cardiovascular outcomes in diabetics. PMID: 27055907
  13. high serum CL-L1 concentration in critically ill children upon PICU admission is associated with an increased risk of infection and prolonged need of intensive care, and counteracts the protective effect of having a high MASP-3 concentration PMID: 27057739
  14. Our study provided novel evidence that genetic variations in complement genes C6 and MASP1were associated with preeclampsia risk, and that the risk varied by preeclampsia subtypes PMID: 27405496
  15. The exclusion of the MASP1 and COLEC11 Loci in two individuals from different consanguineous families and the absence of mutations in four further individuals sequenced for both genes raises the possibility that that there is further genetic heterogeneity of 3MC syndrome PMID: 26789649
  16. Plasma MASP-1 concentration at the early stage of Kawasaki disease is predictive of length of time of recovery from coronary artery lesions. PMID: 26536449
  17. 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
  18. described for the first time a detailed model of prothrombin activation by MASP-1 PMID: 26645987
  19. Fusion of MAP-1 with FH domains represents a novel therapeutic approach for selective targeting upstream and central complement activation at sites of inflammation PMID: 26260032
  20. The levels of MASP-1 and MASP-1/C1-INH complexes are reduced in HAE patients compared with controls. Both MASP-1 and MASP-1/C1-INH complexes are related to the degree of complement C4 consumption PMID: 26371246
  21. Polymorphisms in MASP1 and MASP2 genes are associated with the susceptibility or protection to infectious diseases. (Review) PMID: 25862418
  22. 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
  23. MASP-1 cleaves prothrombin and identified its cleavage sites, suggesting that MASP-1 gives rise to an alternative active form of thrombin by cleaving at the cleavage site R393. PMID: 25745807
  24. MASP-1 may activate neutrophils indirectly via endothelial cells. PMID: 24489848
  25. 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
  26. Data show that among the components of the mannose-binding lectin (MBL) and associated serine proteases (MASPs) only MASP-1 is able to trigger response in endothelial cells (HUVECs) and the proteolytic activity of MASP-1 is essential. PMID: 24472859
  27. We found that rMAP-1 can engage in heterocomplexes with rMASP-1 and rMASP-3 in a calcium-dependent manner PMID: 24683193
  28. Polymorphisms in the MASP1 gene are associated with serum levels of MASP-1, MASP-3, and MAp44 PMID: 24023860
  29. The serine protease domain of MASP-3 exerts weak enzymatic activity. PMID: 23861840
  30. 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
  31. accelerates fibrosis progression in hepatitis C virus-induced liver disease PMID: 23841802
  32. 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
  33. insights into the function of MASP-3 reveal how a mutation in this enzyme causes it to be inactive and thus contribute to the 3MC syndrome. PMID: 23792966
  34. 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
  35. autoactivation of MASP-1 is crucial for the activation of MBL/ficolin.MASP complexes, and in the proenzymic phase zymogen MASP-1 controls the process PMID: 23386610
  36. MASP-1 seems to be involved in activation of both the lectin and alternative complement pathways--{review} PMID: 23402018
  37. 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
  38. MAP-1 competes with all three MASPs for ligand binding and is able to mediate a strong dose-dependent inhibitory effect on the lectin pathway activation, as measured by levels of C3 and C9. PMID: 22854970
  39. 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
  40. MASP-1 activates MASP-2 and, moreover, inhibition of MASP-1 prevents autoactivation of MASP-2 PMID: 22691502
  41. MASP-1, in concerted action with other complement and coagulation proteins, may play a role in fibrin clot formation. PMID: 22536427
  42. MASP-1 was present at adult level at 1 year of age, while it was 60% at birth. The present data prepare the ground for studies on the associations of MASP-1 levels with disease. PMID: 22670777
  43. The interaction of mannan-binding lectin (MBL) with its associated serine proteases (MASPs) was investigated using recombinant (r) MBL, plasma-derived (pd) MBL, rMASP-3 and rMAp19. rMASP-3 and rMAp19 bound to free available sites on rMBL and pdMBL. PMID: 22607836
  44. showed that MASP-1 was able to cleave HK resulting in BK production. MASP-2 could also cleave HK but could not release BK. The cleavage pattern of MASPs is similar but not strictly identical to that of kallikrein PMID: 21625439
  45. these findings demonstrate a role for complement pathway factors in fundamental developmental processes and in the etiology of 3MC syndrome. PMID: 21258343
  46. MBL-associated serine protease-3 down-regulate Ficolin-3 mediated complement activation through the lectin pathway. PMID: 19939495
  47. These results implicate mutations of MASP1 as the cause of a human malformation syndrome and demonstrate the involvement of MASP1 in facial, umbilical, and ear development during the embryonic period. PMID: 21035106
  48. MBL-associated serine protease 3 (MASP-3) also inhibited binding between MBL and CD91, suggesting that the site of interaction is located at or near the MASP-MBL interaction site. PMID: 21054788
  49. We present a novel, phylogenetically conserved protein, MAp44, which is found in human serum at 1.4 microg/ml in Ca(2+)-dependent complexes with the soluble pattern recognition molecules. PMID: 19917686
  50. MASP-1 has a crucial role in the initiation steps of lectin pathway activation most probably by activating MASP-2 PMID: 20817870
  51. The normal serum level of the second and third splice products of the MASP1 gene, MASP-3 and MAp44, have been established, as well as their ontogeny and acute phase response. PMID: 20673767
  52. MAp44, a novel third splice product of the MASP1 gene, which associates with pattern-recognition molecules of the complement system and regulates the lectin pathway of complement activation. PMID: 19917686
  53. novel 45-kDa serum protein derived from the MASP1 gene, which is highly expressed in striated muscle tissues and is found in complex with MBL and ficolins and may function as a potent inhibitor of the complement system in vivo PMID: 20053996
  54. When incubated with the pathogenic organism Staphylococcus aureus, mannose-binding lectin-associated MASP enhances complement activation and opsonophagocytosis. PMID: 12370377
  55. The interaction of recombinant MASP1, its N-terminal complement modules, and MBL-associated protein 19 with L-ficolin/p35 has been characterized by surface plasmon resonance spectroscopy. PMID: 12421953
  56. detection of a processed pseudogene of this protein PMID: 12601245
  57. On average, high MASP-1 correlates with low MASP-2 and vice-versa, and confirms the hypothesis that native MBL-MASP complexes on average do not have fixed MBL-(MASP-1)-(MASP-2) stoichiometry. PMID: 16102832
  58. The mRNA distribution of masp1 and masp2 were found very similar to that of mbl2, while masp3 mRNA seemed ubiquitous present at quite high levels when compared to liver. PMID: 16112196
  59. The mRNA distribution of masp1 and masp2 were found very similar to that of mbl2, while masp3 mRNA seemed ubiquitous present at quite high levels when compared to liver. (masp3) PMID: 16112196
  60. MASP1 gene harbors a low-frequent polymorphic site resulting in an amino acid substitution, which may influence the function of the gene product. PMID: 17444953
  61. mannose-binding lectin (MBL)/MBL-associated serine protease (MASP) complexes and L-ficolin/MASP complexes bind to different strains of GBS to activate the lectin pathway PMID: 17938215
  62. rMASP1 and thrombin cleave factor XIII A-chain and the fibrinogen beta-chain at identical sites, but differ in cleavage of the fibrinogen alpha-chain. PMID: 18456010
  63. crystallographic analysis of the CUB1-EGF-CUB2 domain of human MASP-1/3 and identification of its interaction sites with mannan-binding lectin and ficolins PMID: 18596036
  64. structure shows that its substrate binding groove is accessible; however, its reactivity could be modulated by an unusually large 60-loop and an internal salt bridge involving the S1 Asp. PMID: 19564340
  65. EPHB3, MASP1 and SST map to 3q26.2-q29 and may have roles in squamous cell carcinoma of the lung PMID: 19607727
  66. MASP-1-induced protease-activated receptor (PAR)4 activation could contribute to the development of the inflammatory reaction. PMID: 19667088

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Involvement in disease 3MC syndrome 1 (3MC1)
Subcellular Location Secreted
Protein Families Peptidase S1 family
Tissue Specificity Protein of the plasma which is primarily expressed by liver.
Database Links

HGNC: 6901

OMIM: 257920

KEGG: hsa:5648

UniGene: Hs.89983

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