Description
RP1-Serpin-A9 is a polyclonal antibody made to the serine proteinase inhibitor Germinal Centre B-Cell Expressed Transcript-2 (Serpin-A9). The antibody is made to a synthetic peptide based on the aminoterminal end of mature human serpin-A9. The antibody has been peptide-affinity purified, concentrated to 1.0 mg/ml, with the addition of 0.05% sodium azide as preservative and 50% glycerol as cryoprotectant.
Use
Serpin-A9 was first discovered in gene profiles of diffuse B-cell lymphoma (DLBCL) cells, a subset of adult non-Hodgkin lymphoma. The DLBCL tumors further subdivide into 2 forms by molecular analysis profiles: germinal center B-cell-like DLBCL and activated B-cell-like DLBCL. Patients with the germinal center B-cell-like DLBCL form presented with better clinical outcomes than the activated B-cell-like DLBCL form, and serpin-A9 was found to be expressed specifically in the germinal center (GC) B-cells. Serpin-A9 message was limited to the GC cells, and no significant message was seen in the liver (where most of the other A-clade serpins are made), brain, skeletal muscles, or other tissues analyzed. The overall structure is in alignment with a heparin-binding serpin that inhibits trypsin-like proteinases, and recombinant serpin-A9 inhibited thrombin, plasmin and trypsin. Addition of heparin had little effect on the recombinant serpin-A9, but post-translational modifications might be different in the recombinant protein than the native protein. Serpin-A9 was found associated with the plasma membrane, and message was stimulated by IL-4. Serpin-A9 is an A-clade serpin, the archetype of which is alpha-1 antitrypsin. The mode of action of most A-clade serpins involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of A-clade serpins is in a stressed state, and cleavage converts the molecule to a relaxed, more energetically favorable state. The structural change traps the proteinase that cleaves the reactive center loop (RCL), like a mousetrap. The GCET2 sequence codes for a 435 amino acid protein, with a predicted mass of 48.6 kDa and a pI of 9.7. The basic pI may explain the association with the plasma membrane, where serpin-A9 may be associated with GAGs. A number of different splice variants have been published, starting at different start sites, including a fusion with serpin-A11 at the carboxyterminal end. Since the original serpin-A9 sequences were derived from tumor cells it is possible that they represent the mutant forms, but that is not yet clear. A recommended starting concentration for Western blots is 1:1000 when using colorimetric substrates such as BCIP/NBT, and 1:5000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species. FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for approximately 12 at -20C.
Description
RP2-Serpin-A9 is a polyclonal antibody made to the serine proteinase inhibitor Germinal Centre B-Cell Expressed Transcript-2 (Serpin-A9). The antibody is made to a synthetic peptide based on Helix 4 to Helix 5 of human serpin-A9. The antibody has been peptide-affinity purified, concentrated to 1.0 mg/ml, with the addition of 0.05% sodium azide as preservative and 50% glycerol as cryoprotectant.
Use
Serpin-A9 was first discovered in gene profiles of diffuse B-cell lymphoma (DLBCL) cells, a subset of adult non-Hodgkin lymphoma. The DLBCL tumors further subdivide into 2 forms by molecular analysis profiles: germinal center B-cell-like DLBCL and activated B-cell-like DLBCL. Patients with the germinal center B-cell-like DLBCL form presented with better clinical outcomes than the activated B-cell-like DLBCL form, and serpin-A9 was found to be expressed specifically in the germinal center (GC) B-cells. Serpin-A9 message was limited to the GC cells, and no significant message was seen in the liver (where most of the other A-clade serpins are made), brain, skeletal muscles, or other tissues analyzed. The overall structure is in alignment with a heparin-binding serpin that inhibits trypsin-like proteinases, and recombinant serpin-A9 inhibited thrombin, plasmin and trypsin. Addition of heparin had little effect on the recombinant serpin-A9, but post-translational modifications might be different in the recombinant protein than the native protein. Serpin-A9 was found associated with the plasma membrane, and message was stimulated by IL-4. Serpin-A9 is an A-clade serpin, the archetype of which is alpha-1 antitrypsin. The mode of action of most A-clade serpins involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of A-clade serpins is in a stressed state, and cleavage converts the molecule to a relaxed, more energetically favorable state. The structural change traps the proteinase that cleaves the reactive center loop (RCL), like a mousetrap. The GCET2 sequence codes for a 435 amino acid protein, with a predicted mass of 48.6 kDa and a pI of 9.7. The basic pI may explain the association with the plasma membrane, where serpin-A9 may be associated with GAGs. A number of different splice variants have been published, starting at different start sites, including a fusion with serpin-A11 at the carboxyterminal end. Since the original serpin-A9 sequences were derived from tumor cells it is possible that they represent the mutant forms, but that is not yet clear. A recommended starting concentration for Western blots is 1:1000 when using colorimetric substrates such as BCIP/NBT, and 1:5000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species. FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for approximately 12 at -20C.
Description
RP3-Serpin-A9 is a polyclonal antibody made to the serine proteinase inhibitor Germinal Centre B-Cell Expressed Transcript-2 (Serpin-A9). The antibody is made to a synthetic peptide based on Helix 7 to Helix 8 of human serpin-A9. The antibody has been peptide-affinity purified, concentrated to 1.0 mg/ml, with the addition of 0.05% sodium azide as preservative and 50% glycerol as cryoprotectant.
Use
Serpin-A9 was first discovered in gene profiles of diffuse B-cell lymphoma (DLBCL) cells, a subset of adult non-Hodgkin lymphoma. The DLBCL tumors further subdivide into 2 forms by molecular analysis profiles: germinal center B-cell-like DLBCL and activated B-cell-like DLBCL. Patients with the germinal center B-cell-like DLBCL form presented with better clinical outcomes than the activated B-cell-like DLBCL form, and serpin-A9 was found to be expressed specifically in the germinal center (GC) B-cells. Serpin-A9 message was limited to the GC cells, and no significant message was seen in the liver (where most of the other A-clade serpins are made), brain, skeletal muscles, or other tissues analyzed. The overall structure is in alignment with a heparin-binding serpin that inhibits trypsin-like proteinases, and recombinant serpin-A9 inhibited thrombin, plasmin and trypsin. Addition of heparin had little effect on the recombinant serpin-A9, but post-translational modifications might be different in the recombinant protein than the native protein. Serpin-A9 was found associated with the plasma membrane, and message was stimulated by IL-4. Serpin-A9 is an A-clade serpin, the archetype of which is alpha-1 antitrypsin. The mode of action of most A-clade serpins involves a dramatic structural change after cleavage of a 'bait' region. The normal conformation of A-clade serpins is in a stressed state, and cleavage converts the molecule to a relaxed, more energetically favorable state. The structural change traps the proteinase that cleaves the reactive center loop (RCL), like a mousetrap. The GCET2 sequence codes for a 435 amino acid protein, with a predicted mass of 48.6 kDa and a pI of 9.7. The basic pI may explain the association with the plasma membrane, where serpin-A9 may be associated with GAGs. A number of different splice variants have been published, starting at different start sites, including a fusion with serpin-A11 at the carboxyterminal end. Since the original serpin-A9 sequences were derived from tumor cells it is possible that they represent the mutant forms, but that is not yet clear. A recommended starting concentration for Western blots is 1:1000 when using colorimetric substrates such as BCIP/NBT, and 1:5000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species. FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for approximately 12 at -20C.
