TPA Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P00750 |
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Clone Names | 80821053 |
Gene ID | 5327 |
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Other Names | Tissue-type plasminogen activator, t-PA, t-plasminogen activator, tPA, Alteplase, Reteplase, Tissue-type plasminogen activator chain A, Tissue-type plasminogen activator chain B, PLAT |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP6778c was selected from the Center region of human TPA. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | PLAT (HGNC:9051) |
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Function | Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. During oocyte activation, plays a role in cortical granule reaction in the zona reaction, which contributes to the block to polyspermy (By similarity). |
Cellular Location | Secreted, extracellular space. |
Tissue Location | Synthesized in numerous tissues (including tumors) and secreted into most extracellular body fluids, such as plasma, uterine fluid, saliva, gingival crevicular fluid, tears, seminal fluid, and milk |
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Provided below are standard protocols that you may find useful for product applications.
Background
TPA is a tissue-type plasminogen activator, a secreted serine protease which converts the proenzyme plasminogen to plasmin, a fibrinolytic enzyme. Tissue-type plasminogen activator is synthesized as a single chain which is cleaved by plasmin to a two chain disulfide linked protein. This enzyme plays a role in cell migration and tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysis which can result in thrombosis or embolism.
References
de Vos,A.M., et.al., Biochemistry 31 (1), 270-279 (1992)Bentov,Y., et.al., PLoS ONE 4 (6), E5918 (2009)
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