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Complement Factor MASP3 Protein, Human, Recombinant (His)
Catalog No. TMPJ-00980 Copy Product Info
MASP3 is a member of the MASPs involved in mannan-binding lectin (MBL) complement pathway. The MBL pathway is initiated by the binding of MBL to specific carbohydrate structures found on the surface of a variety of microorganisms. Activation of the complement pathway via MBL is initiated by specific MASPs. Three MASPs have been identified and all have domain structures similar to those of C1r and C1s with a heavy chain (chain A) and a light chain (chain B). Chain A is composed of CUB1, EGF, CUB2, CCP1 and CCP2 while chain B corresponds to the catalytic domain found in many serine proteases. MASP1 and MASP3 are two alternatively spliced products of a single gene, which contain the same A chains but entirely different B chains. Distinct MASPs found in different MBL oligomers may have different biological activities. For example, MASP3, found together with MASP2, downregulates the C4 and C2 cleaving activity of MASP2. The protease activity of MASP3 is first revealed here using rhMASP3CD, which is inhibited by serine protease inhibitors such as Ecotin and AEBSF.
Complement Factor MASP3 Protein, Human, Recombinant (His)
Catalog No. TMPJ-00980
Copy Product InfoMASP3 is a member of the MASPs involved in mannan-binding lectin (MBL) complement pathway. The MBL pathway is initiated by the binding of MBL to specific carbohydrate structures found on the surface of a variety of microorganisms. Activation of the complement pathway via MBL is initiated by specific MASPs. Three MASPs have been identified and all have domain structures similar to those of C1r and C1s with a heavy chain (chain A) and a light chain (chain B). Chain A is composed of CUB1, EGF, CUB2, CCP1 and CCP2 while chain B corresponds to the catalytic domain found in many serine proteases. MASP1 and MASP3 are two alternatively spliced products of a single gene, which contain the same A chains but entirely different B chains. Distinct MASPs found in different MBL oligomers may have different biological activities. For example, MASP3, found together with MASP2, downregulates the C4 and C2 cleaving activity of MASP2. The protease activity of MASP3 is first revealed here using rhMASP3CD, which is inhibited by serine protease inhibitors such as Ecotin and AEBSF.
| Pack Size | Price | USA Stock | Global Stock | Quantity |
|---|---|---|---|---|
| 5 μg | $112 | 7-10 days | 7-10 days | |
| 10 μg | $183 | 7-10 days | 7-10 days | |
| 20 μg | $292 | 7-10 days | 7-10 days | |
| 50 μg | $545 | 7-10 days | 7-10 days | |
| 100 μg | $792 | 7-10 days | 7-10 days | |
| 200 μg | $1,150 | 7-10 days | 7-10 days | |
| 500 μg | $1,900 | 7-10 days | 7-10 days | |
| 1 mg | $2,730 | 7-10 days | 7-10 days |
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For research use only—not for human use. No sales to individuals. Use as intended only.
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| Biological Activity | Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first. |
| Description | MASP3 is a member of the MASPs involved in mannan-binding lectin (MBL) complement pathway. The MBL pathway is initiated by the binding of MBL to specific carbohydrate structures found on the surface of a variety of microorganisms. Activation of the complement pathway via MBL is initiated by specific MASPs. Three MASPs have been identified and all have domain structures similar to those of C1r and C1s with a heavy chain (chain A) and a light chain (chain B). Chain A is composed of CUB1, EGF, CUB2, CCP1 and CCP2 while chain B corresponds to the catalytic domain found in many serine proteases. MASP1 and MASP3 are two alternatively spliced products of a single gene, which contain the same A chains but entirely different B chains. Distinct MASPs found in different MBL oligomers may have different biological activities. For example, MASP3, found together with MASP2, downregulates the C4 and C2 cleaving activity of MASP2. The protease activity of MASP3 is first revealed here using rhMASP3CD, which is inhibited by serine protease inhibitors such as Ecotin and AEBSF. |
| Species | Human |
| Expression System | HEK293 Cells |
| Tag | C-6xHis |
| Accession Number | P48740-2 |
| Synonyms | Serine Protease 5,RaRF,PRSS5,MASP-1,MASP1,Mannose-Binding Lectin-Associated Serine Protease 1,CRARF1,CRARF,Complement Factor MASP-3,Complement Factor MASP3 |
| Amino Acid | His20-Arg728 |
| Construction | His20-Arg728 |
| Protein Purity | Greater than 95% as determined by reducing SDS-PAGE. (QC verified) |
| Molecular Weight | 95-120 KDa (reducing condition) |
| Endotoxin | < 0.1 ng/µg (1 EU/µg) as determined by LAL test. |
| Formulation | Supplied as a 0.2 μm filtered solution of 20 mM Tris-HCl, 200 mM NaCl, 10% Glycerol, pH 8.0. |
| Stability & Storage | Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots. |
| Shipping | Proteins are shipped with blue ice. |
| Research Background | MASP3 is a member of the MASPs involved in mannan-binding lectin (MBL) complement pathway. The MBL pathway is initiated by the binding of MBL to specific carbohydrate structures found on the surface of a variety of microorganisms. Activation of the complement pathway via MBL is initiated by specific MASPs. Three MASPs have been identified and all have domain structures similar to those of C1r and C1s with a heavy chain (chain A) and a light chain (chain B). Chain A is composed of CUB1, EGF, CUB2, CCP1 and CCP2 while chain B corresponds to the catalytic domain found in many serine proteases. MASP1 and MASP3 are two alternatively spliced products of a single gene, which contain the same A chains but entirely different B chains. Distinct MASPs found in different MBL oligomers may have different biological activities. For example, MASP3, found together with MASP2, downregulates the C4 and C2 cleaving activity of MASP2. The protease activity of MASP3 is first revealed here using rhMASP3CD, which is inhibited by serine protease inhibitors such as Ecotin and AEBSF. |
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