Description
RP2-Chymase is a rabbit polyclonal antibody made to the chymotrypsin-like protease chymase. The antibody is made to a synthetic peptide based on the catalytic domain of human chymase. 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
Chymase, also known as mast cell chymase, alpha-chymase and mast cell protease-1 is a chymotrypsin-like proteinase produced in mast cells. Chymase, along with the tryptases and MMP-9 are released from mast cells in response to inflammatory stimuli, with different subpopulations of mast cells containing varying ratios of the proteinases. The mast cell populations found in skin and connective tissue contain relatively more chymase than tryptases, and the reverse in the case in the gut. Chymase is known to cleave a wide variety of substrates, and is a broad specificity proteinase. Chymase further promotes degradation by cleaving and inactivating TIMP-1, as well as activating MMP-9. Chymase in the vascular system has been implicated in processing of angiotensin I to angiotensin II, and modifying blood pressure, part of the rennin-angiotensin system. Extravascular conversion of angiotensin I to angiotensin II is thought to be principally due to chymase. Chymase mutations are proposed to lead to gastric cancers in some populations, and have also been invoked in forms of asthma. Chymase complexes with the SERPIN SLPI, found in high concentrations in the skin, but unlike other serine proteinases chymase cleaves and inactivates SLPI. The cleaved SLPI remains attached to chymase, and may lead to modified activity. Chymase also binds to heparin, which greatly modifies the chymase activity. Human chymase is a 247 amino acid protein, with a predicted mass of 27.3 kDa and a pI of 9.92. The basic pI promotes association with heparin and GAGs. Glycosylation gives chymase a higher mass of 31 kDa on SDS PAGE gels. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 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 12 months at -20C.
Description
RP3-Chymase is a rabbit polyclonal antibody made to the chymotrypsin-like protease chymase. The antibody is made to a synthetic peptide based on the carboxyterminal end of human chymase. 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
Chymase, also known as mast cell chymase, alpha-chymase and mast cell protease-1 is a chymotrypsin-like proteinase produced in mast cells. Chymase, along with the tryptases and MMP-9 are released from mast cells in response to inflammatory stimuli, with different subpopulations of mast cells containing varying ratios of the proteinases. The mast cell populations found in skin and connective tissue contain relatively more chymase than tryptases, and the reverse in the case in the gut. Chymase is known to cleave a wide variety of substrates, and is a broad specificity proteinase. Chymase further promotes degradation by cleaving and inactivating TIMP-1, as well as activating MMP-9. Chymase in the vascular system has been implicated in processing of angiotensin I to angiotensin II, and modifying blood pressure, part of the rennin-angiotensin system. Extravascular conversion of angiotensin I to angiotensin II is thought to be principally due to chymase. Chymase mutations are proposed to lead to gastric cancers in some populations, and have also been invoked in forms of asthma. Chymase complexes with the SERPIN SLPI, found in high concentrations in the skin, but unlike other serine proteinases chymase cleaves and inactivates SLPI. The cleaved SLPI remains attached to chymase, and may lead to modified activity. Chymase also binds to heparin, which greatly modifies the chymase activity. Human chymase is a 247 amino acid protein, with a predicted mass of 27.3 kDa and a pI of 9.92. The basic pI promotes association with heparin and GAGs. Glycosylation gives chymase a higher mass of 31 kDa on SDS PAGE gels. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 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 12 months at -20C.
