货号 | AF3380-SP |
别名 | FLJ14417; MATN4; matrilin 4; matrilin-4 |
反应种属 | Mouse |
应用 | Western Blot(0.1 µg/mL) |
目标/特异性 | Detects mouse Matrilin-4 in direct ELISAs and Western blots. In direct ELISAs, approximately 15% cross-reactivity with recombinant human (rh) Matrilin-4 is observed and less than 2% cross-reactivity with recombinant mouse Matrilin-2 and rhMatrilin-3 is observed. |
使用方法 | Western Blot: 0.1 µg/mL |
来源 | Reconstitute at 0.2 mg/mL in sterile PBS. |
产品组分 |
供应商 | R&D Systems |
Entrez Gene IDs | 8785 (Human); 17183 (Mouse); 296358 (Rat) |
纯化方式 | Antigen Affinity-purified |
免疫原 | Mouse myeloma cell line NS0-derived recombinant mouse Matrilin-4 Gln22-Lys624 Accession # O89029 |
生物活性 | Mouse |
标记 | Unconjugated |
溶解方法 | Reconstitute at 0.2 mg/mL in sterile PBS. |
背景 | Matrilin-4 is a 73 kDa secreted glycoprotein that is a member of the matrilin family of the von Willebrand Factor-A (vWA) domain-containing superfamily (1). Matrilins are modular extracellular matrix proteins that serve as adaptors and linkers for other matrix proteins. Matrilin-4, like Matrilin‑2, has a broad distribution in both cartilage and in loose connective tissue such as dermis, lung and kidney, while Matrilins 1 and 3 are limited to cartilage. Matrilin-4 is present in nervous tissue and is abundant in the brain (2, 3). Mature mouse Matrilin-4 shares 98%, 90%, 89% and 66% amino acid (aa) identity with rat, human, canine and chicken Matrilin-4, respectively. The 624 aa mouse Matrilin-4 contains a 22 aa signal sequence, two potential glycosylation sites, and four cysteine-rich EGF-like domains placed between two vWA domains. A short isoform lacks the N-terminal vWA domain (aa 28‑217). A C-terminal alpha -helix/coiled-coil region (aa 590‑623) by which multimers are formed is often proteolytically removed so that Matrilin-4 is found as a mixture of monomers with homo- or hetero- dimers and trimers. Matrilin-4 forms multimers with Matrilins 1 and 2 but not with Matrilin-3 (3, 4). The N-terminal vWA domains of Matrilins associate with collagen IV microfibrils via the proteoglycans biglycan and decorin, linking the fibrils with other matrix constituents aggrecan and collagen II (5, 6). Matrilins also show calcium-dependent binding to the cartilage oligomeric matrix protein (COMP); this interaction is of high affinity for oligomeric Matrilin-4 and somewhat lower affinity for monomeric Matrilin-4 (6). Functions and distributions of Matrilins overlap enough so that knockouts of Matrilins 1, 2 and 3 lack obvious phenotypes (1). |
运输条件 | Blue Ice |
存放说明 | 4℃ |
参考文献 |
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