SERPINC1 Antibody (C-term) Blocking Peptide
€363.00
In stock
SKU
AC-BP6715b
Background:
SERPINC1 is a plasma protease inhibitor and a member of the serpin superfamily. This protein inhibits thrombin as well as other activated serine proteases of the coagulation system, and it regulates the blood coagulation cascade. The protein includes two functional domains: the heparin binding-domain at the N-terminus of the mature protein, and the reactive site domain at the C-terminus. The inhibitory activity is enhanced by the presence of heparin.
Other Names:
Antithrombin-III, ATIII, Serpin C1, SERPINC1, AT3
Target/Specificity:
The synthetic peptide sequence used to generate the antibody AP6715b was selected from the C-term region of human SERPINC1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Gene Name: SERPINC1
Gene ID: 462
Primary Accession: P01008
Format: Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
SERPINC1 is a plasma protease inhibitor and a member of the serpin superfamily. This protein inhibits thrombin as well as other activated serine proteases of the coagulation system, and it regulates the blood coagulation cascade. The protein includes two functional domains: the heparin binding-domain at the N-terminus of the mature protein, and the reactive site domain at the C-terminus. The inhibitory activity is enhanced by the presence of heparin.
Other Names:
Antithrombin-III, ATIII, Serpin C1, SERPINC1, AT3
Target/Specificity:
The synthetic peptide sequence used to generate the antibody AP6715b was selected from the C-term region of human SERPINC1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Gene Name: SERPINC1
Gene ID: 462
Primary Accession: P01008
Format: Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
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