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Rabbit Polyclonal Cleaved-MASP-1 HC (R448) antibody (STJ90096)
Supplier: St John’s Laboratory Ltd.
Recommended applications: WB, ELISA
Recommended dilution: WB 1:500-1:2000; ELISA 1:10000;
Recommended protocols: check protocols
Click or hover above images to see image description for Cleaved-MASP-1 HC (R448) Polyclonal Antibody.
Check alternative names for the antibodyExpand
MASP1 antibody, CRARF antibody, CRARF1 antibody, PRSS5 antibody,|Complement factor MASP-3 antibody|Complement factor MASP3 antibody|Complement-activating component of Ra-reactive factor antibody|CRARF antibody|Mannose binding lectin associated serine protease 1 antibody|Mannose binding protein associated serine protease antibody|Mannose-binding lectin-associated serine protease 1 antibody|Mannose-binding lectin-associated serine protease-1 antibody|MASP antibody|PRSS 5 antibody|Ra-reactive factor serine protease p100 antibody|RaRF antibody|Serine protease 5 antibody|Anti-MASP1 antibody (ab72659)
SCBT cat No: sc-50839|sc-50840|sc-50841|sc-50843|sc-166815|sc-166816|sc-48749|sc-17902|
Cleaved-MASP-1 HC (R448) Polyclonal Antibody
|Catalogue No.|| |
Cleaved-MASP-1 HC (R448) Polyclonal Antibody detects endogenous levels of fragment of activated MASP-1 HC protein resulting from cleavage adjacent to R448.
Synthesized peptide derived from Cleaved-MASP-1 HC (R448) at AA range 370-450
|Recommended dilution|| |
WB 1:500-1:2000; ELISA 1:10000;
|Molecular weight|| |
Cleaved-MASP-1 HC (R448) Antibody was tube-contained. Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Cleaved-MASP-1 HC (R448) Antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
-20 Celsius degree. Avoid repeated freeze/thaw cycles.
|Alternative antibody names|| |
Mannan-binding lectin serine protease 1 antibody, Complement factor MASP-3 antibody, Complement-activating component of Ra-reactive factor antibody, Mannose-binding lectin-associated serine protease 1 antibody, MASP-1 antibody, Mannose-binding protein-associated serine protease antibody, Ra-reactive factor serine protease p100 antibody, RaRF antibody, Serine protease 5 antibody
|Protein names|| |
Mannan-binding lectin serine protease 1 , 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
|Protein 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. / Inhibited by SERPING1 and A2M. / 0.10 mM for Ac-Gly-Lys-OMe (at 30 degrees Celsius) / 310 µM for Bz-Arg-OEt (at 30 degrees Celsius) / 4.8 µM for C2 (at 37 degrees Celsius)
|Protein tissue specificity|| |
Protein of the plasma which is primarily expressed by liver.
|Involvement in disease|| |
3MC syndrome 1 (3MC1) [MIM:257920]: A disorder characterized by facial dysmorphism that includes hypertelorism, blepharophimosis, blepharoptosis and highly arched eyebrows, cleft lip and/or palate, craniosynostosis, learning disability and genital, limb and vesicorenal anomalies. The term 3MC syndrome includes Carnevale, Mingarelli, Malpuech, and Michels syndromes. . Note: The disease is caused by mutations affecting the gene represented in this entry.
|Protein sequence and domain|| |
Belongs to the peptidase S1 family. / Contains 2 CUB domains. / Contains 1 EGF-like domain. / Contains 1 peptidase S1 domain. / Contains 2 Sushi (CCP/SCR) domains.
|Protein post-translational modifications|| |
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. / N-glycosylated. Some N-linked glycan are of the complex-type (By similarity). / Autoproteolytic processing of the proenzyme produces the active enzyme composed on the heavy and the light chain held together by a disulfide bond. Isoform 1 but not isoform 2 is activated through autoproteolytic processing.
|Protein cellular localization|| |
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St John’s Laboratory Ltd.
|Product type|| |
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