PAPLN Antibody
Purified Mouse Monoclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
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Primary Accession | O95428 |
Reactivity | Human |
Host | Mouse |
Clonality | Monoclonal |
Clone Names | 5F2D10 |
Isotype | IgG1 |
Calculated MW | 137.7kDa |
Description | Papilin is an extracellular matrix glycoprotein involved in, thin matrix layers during gastrulation, matrix associated with wandering, phagocytic hemocytes, basement membranes and space-filling matrix during Drosophila development.Determination of its cDNA sequence led to the identification of Caenorhabditis and mammalian papilins. A distinctly conserved 'papilin cassette' of domains at the amino-end of papilins is also the carboxyl-end of the ADAMTS subgroup of secreted, matrix-associated metalloproteinases; this cassette contains one thrombospondin type 1 (TSR) domain, a specific cysteine-rich domain and several partial TSR domains. In vitro, papilin non-competitively inhibits procollagen N-proteinase, an ADAMTS metalloproteinase. |
Immunogen | Purified recombinant fragment of human PAPLN (AA: 766-870) expressed in E. Coli. |
Formulation | Purified antibody in PBS with 0.05% sodium azide |
Gene ID | 89932 |
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Other Names | Papilin, PAPLN |
Dilution | E~~1/10000 WB~~1/500 - 1/2000 |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | PAPLN Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | PAPLN |
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Cellular Location | Secreted. |
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Background
Papilin is an extracellular matrix glycoprotein involved in, thin matrix layers during gastrulation, matrix associated with wandering, phagocytic hemocytes, basement membranes and space-filling matrix during Drosophila development.Determination of its cDNA sequence led to the identification of Caenorhabditis and mammalian papilins. A distinctly conserved 'papilin cassette' of domains at the amino-end of papilins is also the carboxyl-end of the ADAMTS subgroup of secreted, matrix-associated metalloproteinases; this cassette contains one thrombospondin type 1 (TSR) domain, a specific cysteine-rich domain and several partial TSR domains. In vitro, papilin non-competitively inhibits procollagen N-proteinase, an ADAMTS metalloproteinase. ; ;
References
1. Int J Biochem Cell Biol. 2004 Jun; 36(6):1079-84. 2. Development. 2000 Dec;127(24):5475-85.
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