EPR1 Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
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Primary Accession | Q14868 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 36826 Da |
Antigen Region | 308-337 aa |
Other Names | EPR-1; Effector cell protease receptor 1 |
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Target/Specificity | This EPR1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 308-337 amino acids from the C-terminal region of human EPR1. |
Dilution | WB~~1:1000 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | EPR1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | EPR-1 {ECO:0000313|EMBL:AAA19687.1} |
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Provided below are standard protocols that you may find useful for product applications.
Background
Cellular receptors for blood proteases regulate chemotaxis, extracellular proteolysis, and growth behavior of normal and malignant cells. Effector cell protease receptor-1 (EPR1) is a receptor for the coagulation protease factor Xa. EPR1 is characterized by a cysteine-rich extracellular module, a single membrane-spanning domain, and a serine-rich cytoplasmic tail featuring at least 15 potential phosphorylation sites. EPR1 also contains 2 N-linked glycosylation sites, 4 O-linked glycosylation sites, and a chondroitin sulfate attachment site, which may provide anchoring for carbohydrate chains, EPR1 transfectants bind to factor Xa in a specific and saturable manner, and in the absence of factor V/Va promote prothrombin activation in a factor Xa concentration-dependent reaction. Activated platelets and megakaryocytes express EPR1. Both EPR1 and membrane-bound factor Va are thought to be required to mediate factor Xa binding to the activated platelet to form a functional prothrombinase complex.
References
Altieri, D.C., J. Biol. Chem. 269(5):3139-3142 (1994).
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