| Reactivity | HuSpecies Glossary |
| Applications | Bioactivity |
| Format | Carrier-Free |
| Details of Functionality | Bioassay data are not available. |
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| Source | Human embryonic kidney cell, HEK293-derived human MFAP3L protein
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| Accession # | |||||||
| N-terminal Sequence | Lys29 |
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| Structure / Form | Disulfide-linked homodimer |
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| Protein/Peptide Type | Recombinant Proteins |
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| Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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| Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
| Dilutions |
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| Theoretical MW | 40 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
| SDS-PAGE | 54-66 kDa, under reducing conditions |
| Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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| Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
| Reconstitution Instructions | Reconstitute at 500 µg/mL in PBS. |
Microbibrillar-Associated Protein 3-Like (MFAP3L), also known as NYD-sp9, is part of the microfibrillar-associated protein family (MFAPs). MFAPs are non‐fibrillin, extracellular matrix glycoproteins that interact with fibrillin and were originally characterized in microfibrillar assembly (1,2). In humans, there several subfamily members with varying amino acid (aa) sequence homology and functions (1,2). Among the family, MFAP2 and MFAP5 are more closely related and while MFAP1, 3 and 4 share no structural or sequence homology with MFAP2, MFAP5 or with each other (1,2). Human MFAP3L shows 71% amino acid (aa) sequence homology to MFAP3, but not other MFAPs (3). Mature, human MFAP3L consists of an extracellular domain (ECD) containing N-linked glycosylation sites, a transmembrane domain, and a cytoplasmic domain with a conserved SH2 motif (3). The ECD of human MFAP3L shares 89% and 90% aa sequence identity with mouse and rat MFAP3L, respectively. MFAPs have the unique ability to interact with TGF-beta family growth factors, Notch and Notch ligands and multiple elastic fiber proteins, in addition to interacting with fibrillin (1, 2). MFAPs are expressed in a wide variety of tissues and, along with microfibril assembly, they play roles in the regulation of tissue homeostasis, cell survival, and tumor progression (1,2). MFAP3L is often located within colorectal cancer (CRC) cells, which metastasize by activation of the nuclear ERK pathway via MFAP3L phosphorylation (3). Regulation of this MFAP3L activity could have pharmaceutical effects on CRC tumor progression (3).
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