Merck Anti-Protein C Affinity Matrix

Anti-Protein C Affinity Matrix

from mouse IgG1κ

affinity matrix, anti-protein c

Quality Level

100

생물학적 소스

mouse

결합

agarose conjugate

항체 형태

purified immunoglobulin

클론

HPC4, monoclonal

form

slurry

포장

pkg of 1 mL (settled resin volume)

manufacturer/tradename

Roche

동형

IgG1, kappa

용량

2-10 nmol/mL binding capacity

배송 상태

wet ice

저장 온도

2-8°C

Protein C is a Vitamin K-dependent plasma zymogen that is activated by proteolytic cleavage of the thrombin-thrombomodulin complex to form an anticoagulant enzyme. Anti-Protein C mouse monoclonal antibody (clone HPC4) binds specifically to an epitope sequence spanning the thrombin cleavage site of protein C and is immobilized. Anti-Protein C recognizes the 12-amino acid sequence (EDQVDPRLIDGK), which encodes residues 6 through 17 of the heavy chain of Protein C. The formation of the Anti-Protein C/protein C epitope complex is dependent on the presence of calcium ions. In the presence of Ca2+, the antibody binds with high affinity and specificity to this sequence in native human Protein C or in proteins tagged with this epitope. This efficient binding within the recombinant fusion protein occurs regardless of the site of incorporation of the epitope tag (i.e., N terminus, C terminus, or within the reading frame). This unique antibody is especially well suited for purification of recombinant fusion proteins tagged with the protein C epitope.

• Insertion of the protein C tag does not introduce a new metal-ion binding site. The antibody contains the Ca2+ binding site.
• Protein C tag can be integrated either at the N-terminus, C-terminus or internally without any change in antibody specificity.
• Rapid immunoaffinity purification under non-denaturing conditions using economical calcium chelating agent (e.g., EDTA) or alternatively a specific protein C-tag peptide.

Monoclonal mouse antibody Anti-Protein C (clone HPC4) is covalently coupled to agarose beads. In the coupling reaction 4mg of antibody is reacted per 1ml of beads.