Description
RP1-AEBP1 is a rabbit polyclonal antibody made to the metalloproteinase AEBP1. The antibody is made to a synthetic peptide based on the aminoterminal end of human AEBP1. 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
AEBP-1 was first identified as an enhancer of adipocyte differentiation, and listed as a transcriptional factor that down regulates the alpha 2P gene. Another protein, Aortic Carboxypeptidase-Like Protein (ACLP) was studied in parallel as a regulator of smooth muscle cell growth and differentiation. The initial sequences of AEBP1 studied were shorter than ACLP, missing the discoidin-like domain, and the two gene products were determined to be splice variants of the same gene. ACLP was found to be highly expressed in adult aortic smooth muscle cells (ASMC), and is induced by serum starvation in cultured ASMC. ACLP was listed as a non-nuclear protein, as opposed to AEBP-1, which is localized to the nucleus. The ACLP protein studied was determined to be catalytically inactive, and the AEBP-1 protein to be active. Sequence analysis showed that the AEBP1/ACLP protein contained a region with about 39% identity to catboxypeptidase-E, but with slightly different catalytic residues (HENNY versus HERHYE for CPE). The AEBP-1 protease activity was found to be stimulated by DNA binding to the AE-1 target sequence. A mouse knock out of ACLP showed impaired abdominal wall muscle development and had defects in wound healing. ACLP was found to be a secreted protein highly expressed in collagen-rich tissues, localized to the ECM. It may be that different splice variants of the AEBP-1/ACLP gene that contain differing amounts of the regulatory amino-portion localize differentially, and have different functions. The domain structure of ACLP/AEBP1 is a signal sequence followed by a proline-lysine rich region, a furin consensus cleavage site, a discoidin/Coagulation Factor 5/8 C-terminal-like domain, a zinc metallocarboxypeptidase domain, and a DNA-binding domain. The human AEBP1 splice variants published to date encode proteins of 1158, 845, 733, 589 and 408 amino acids, with predicted mass of 130.9, 96.2, 82, 66.6 and 45.9 kDa and pI of 4.8, 4.6, 4.8, 4.6 and 4.6 respectively. The 845 amino acid form starts 314 residues downstream from the full length 1158 protein, just before the discoidin-like domain, and lacks the signal sequence, pro-lys rich domain and furin cleavage site. The 733 amino acid form starts near the end of the discoidin-like domain, with a different aminoterminus, and an insert of 32 residues at the start of the catalytic domain, relative to the other isoforms. The 589 form starts at the beginning of the catalytic domain, and the 408 form within the catalytic domain, after the metal binding residues (and is thus proteolytically inactive). 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 approximately 12 months at -20C.
Description
RP2-AEBP1 is a rabbit polyclonal antibody made to the metalloproteinase AEBP1. The antibody is made to a synthetic peptide based on the aminoterminal end of the 845 AA form of human AEBP1. 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
AEBP-1 was first identified as an enhancer of adipocyte differentiation, and listed as a transcriptional factor that down regulates the alpha 2P gene. Another protein, Aortic Carboxypeptidase-Like Protein (ACLP) was studied in parallel as a regulator of smooth muscle cell growth and differentiation. The initial sequences of AEBP1 studied were shorter than ACLP, missing the discoidin-like domain, and the two gene products were determined to be splice variants of the same gene. ACLP was found to be highly expressed in adult aortic smooth muscle cells (ASMC), and is induced by serum starvation in cultured ASMC. ACLP was listed as a non-nuclear protein, as opposed to AEBP-1, which is localized to the nucleus. The ACLP protein studied was determined to be catalytically inactive, and the AEBP-1 protein to be active. Sequence analysis showed that the AEBP1/ACLP protein contained a region with about 39% identity to catboxypeptidase-E, but with slightly different catalytic residues (HENNY versus HERHYE for CPE). The AEBP-1 protease activity was found to be stimulated by DNA binding to the AE-1 target sequence. A mouse knock out of ACLP showed impaired abdominal wall muscle development and had defects in wound healing. ACLP was found to be a secreted protein highly expressed in collagen-rich tissues, localized to the ECM. It may be that different splice variants of the AEBP-1/ACLP gene that contain differing amounts of the regulatory amino-portion localize differentially, and have different functions. The domain structure of ACLP/AEBP1 is a signal sequence followed by a proline-lysine rich region, a furin consensus cleavage site, a discoidin/Coagulation Factor 5/8 C-terminal-like domain, a zinc metallocarboxypeptidase domain, and a DNA-binding domain. The human AEBP1 splice variants published to date encode proteins of 1158, 845, 733, 589 and 408 amino acids, with predicted mass of 130.9, 96.2, 82, 66.6 and 45.9 kDa and pI of 4.8, 4.6, 4.8, 4.6 and 4.6 respectively. The 845 amino acid form starts 314 residues downstream from the full length 1158 protein, just before the discoidin-like domain, and lacks the signal sequence, pro-lys rich domain and furin cleavage site. The 733 amino acid form starts near the end of the discoidin-like domain, with a different aminoterminus, and an insert of 32 residues at the start of the catalytic domain, relative to the other isoforms. The 589 form starts at the beginning of the catalytic domain, and the 408 form within the catalytic domain, after the metal binding residues (and is thus proteolytically inactive). 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 approximately 12 months at -20C.
Description
RP3-AEBP1 is a rabbit polyclonal antibody made to the metalloproteinase AEBP1. The antibody is made to a synthetic peptide based on the catalytic domain of human AEBP1. 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
AEBP-1 was first identified as an enhancer of adipocyte differentiation, and listed as a transcriptional factor that down regulates the alpha 2P gene. Another protein, Aortic Carboxypeptidase-Like Protein (ACLP) was studied in parallel as a regulator of smooth muscle cell growth and differentiation. The initial sequences of AEBP1 studied were shorter than ACLP, missing the discoidin-like domain, and the two gene products were determined to be splice variants of the same gene. ACLP was found to be highly expressed in adult aortic smooth muscle cells (ASMC), and is induced by serum starvation in cultured ASMC. ACLP was listed as a non-nuclear protein, as opposed to AEBP-1, which is localized to the nucleus. The ACLP protein studied was determined to be catalytically inactive, and the AEBP-1 protein to be active. Sequence analysis showed that the AEBP1/ACLP protein contained a region with about 39% identity to catboxypeptidase-E, but with slightly different catalytic residues (HENNY versus HERHYE for CPE). The AEBP-1 protease activity was found to be stimulated by DNA binding to the AE-1 target sequence. A mouse knock out of ACLP showed impaired abdominal wall muscle development and had defects in wound healing. ACLP was found to be a secreted protein highly expressed in collagen-rich tissues, localized to the ECM. It may be that different splice variants of the AEBP-1/ACLP gene that contain differing amounts of the regulatory amino-portion localize differentially, and have different functions. The domain structure of ACLP/AEBP1 is a signal sequence followed by a proline-lysine rich region, a furin consensus cleavage site, a discoidin/Coagulation Factor 5/8 C-terminal-like domain, a zinc metallocarboxypeptidase domain, and a DNA-binding domain. The human AEBP1 splice variants published to date encode proteins of 1158, 845, 733, 589 and 408 amino acids, with predicted mass of 130.9, 96.2, 82, 66.6 and 45.9 kDa and pI of 4.8, 4.6, 4.8, 4.6 and 4.6 respectively. The 845 amino acid form starts 314 residues downstream from the full length 1158 protein, just before the discoidin-like domain, and lacks the signal sequence, pro-lys rich domain and furin cleavage site. The 733 amino acid form starts near the end of the discoidin-like domain, with a different aminoterminus, and an insert of 32 residues at the start of the catalytic domain, relative to the other isoforms. The 589 form starts at the beginning of the catalytic domain, and the 408 form within the catalytic domain, after the metal binding residues (and is thus proteolytically inactive). 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 approximately 12 months at -20C.
Description
RP4-AEBP1 is a rabbit polyclonal antibody made to the metalloproteinase AEBP1. The antibody is made to a synthetic peptide based on the DNA-binding domain of human AEBP1. 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
AEBP-1 was first identified as an enhancer of adipocyte differentiation, and listed as a transcriptional factor that down regulates the alpha 2P gene. Another protein, Aortic Carboxypeptidase-Like Protein (ACLP) was studied in parallel as a regulator of smooth muscle cell growth and differentiation. The initial sequences of AEBP1 studied were shorter than ACLP, missing the discoidin-like domain, and the two gene products were determined to be splice variants of the same gene. ACLP was found to be highly expressed in adult aortic smooth muscle cells (ASMC), and is induced by serum starvation in cultured ASMC. ACLP was listed as a non-nuclear protein, as opposed to AEBP-1, which is localized to the nucleus. The ACLP protein studied was determined to be catalytically inactive, and the AEBP-1 protein to be active. Sequence analysis showed that the AEBP1/ACLP protein contained a region with about 39% identity to catboxypeptidase-E, but with slightly different catalytic residues (HENNY versus HERHYE for CPE). The AEBP-1 protease activity was found to be stimulated by DNA binding to the AE-1 target sequence. A mouse knock out of ACLP showed impaired abdominal wall muscle development and had defects in wound healing. ACLP was found to be a secreted protein highly expressed in collagen-rich tissues, localized to the ECM. It may be that different splice variants of the AEBP-1/ACLP gene that contain differing amounts of the regulatory amino-portion localize differentially, and have different functions. The domain structure of ACLP/AEBP1 is a signal sequence followed by a proline-lysine rich region, a furin consensus cleavage site, a discoidin/Coagulation Factor 5/8 C-terminal-like domain, a zinc metallocarboxypeptidase domain, and a DNA-binding domain. The human AEBP1 splice variants published to date encode proteins of 1158, 845, 733, 589 and 408 amino acids, with predicted mass of 130.9, 96.2, 82, 66.6 and 45.9 kDa and pI of 4.8, 4.6, 4.8, 4.6 and 4.6 respectively. The 845 amino acid form starts 314 residues downstream from the full length 1158 protein, just before the discoidin-like domain, and lacks the signal sequence, pro-lys rich domain and furin cleavage site. The 733 amino acid form starts near the end of the discoidin-like domain, with a different aminoterminus, and an insert of 32 residues at the start of the catalytic domain, relative to the other isoforms. The 589 form starts at the beginning of the catalytic domain, and the 408 form within the catalytic domain, after the metal binding residues (and is thus proteolytically inactive). 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 approximately 12 months at -20C.
