Description
RP1-Paraplegin is a rabbit polyclonal antibody made to the metalloprotease paraplegin. The antibody is made to a synthetic peptide based on the amino region, before the first transmembrane domain of human paraplegin. 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
Paraplegin, also known as Spastic Paraplegia Protein 7, is a metalloproteinase of the MA clan, family M41, which includes the Yme1 and FtsH proteases. The overall protein primary structure homology is 38% with YME1 and 47% with AFG3-like protein-2, the closest ortholog. All three enzymes are bound to the mitochondrial membrane, and contain an ATP-binding site. These enzymes are distinguished from the other mammalian metalloproteinases in their requirement for ATP activation, and their localization to the mitochondria. In the mitochondria paraplegin is thought to degrade misfolded proteins. Loss of function and null mutations in paraplegin lead to a disorder termed hereditary spastic paraplegia, caused by the buildup of the misfolded proteins which interfere with oxidative phosphorylation. Paraplegin contains the 'classical' zinc binding motif of HExxHxxxxxH in the catalytic domain and is considered a zinc metalloprotease. The human sequences for paraplegin published thus far include different splice variants of 795, 782, 677, 489 and 212 amino acid length. The full-length human paraplegin is 795 amino acids in length, with predicted mass of 88.2 kDa, and pI of 8.83. The 782, 677, 489 and 212 amino acid forms are predicted to have masses of 86.6, 74.8, 53.9 and 23.8 kDa respectively, with pI of 9.24, 8.0, 9.73 and 5.19. It is unclear if all of these splice variants are produced, and if so whether they posess different activity or localization. The 212 amino acid form starts at the end of the zinc binding domain, and is thus not proteolytically active. Likewise the 489 form ends before the zinc site, and is not an active enzyme. The 782 form differs in the carboxyterminus, but contains the zinc site, and is likely to be an active enzyme. The 677 form has a different aminoterminus, and starts 120 residues later than the 795 form, and has the same carboxy end as the 782 form, but contains the zinc site and is likely a competent protease. RP1-paraplegin recognizes all but the shortest (212 amino acid) form of human paraplegin. 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. EDTA/EGTA treatment of tissues or lysates is required to see latent zymogen. FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for 12 months at -20C.
Description
RP2-Paraplegin is a rabbit polyclonal antibody made to the metalloprotease paraplegin. The antibody is made to a synthetic peptide based on the FtsH extracellular domain of human paraplegin. 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
Paraplegin, also known as Spastic Paraplegia Protein 7, is a metalloproteinase of the MA clan, family M41, which includes the Yme1 and FtsH proteases. The overall protein primary structure homology is 38% with YME1 and 47% with AFG3-like protein-2, the closest ortholog. All three enzymes are bound to the mitochondrial membrane, and contain an ATP-binding site. These enzymes are distinguished from the other mammalian metalloproteinases in their requirement for ATP activation, and their localization to the mitochondria. In the mitochondria paraplegin is thought to degrade misfolded proteins. Loss of function and null mutations in paraplegin lead to a disorder termed hereditary spastic paraplegia, caused by the buildup of the misfolded proteins which interfere with oxidative phosphorylation. Paraplegin contains the 'classical' zinc binding motif of HExxHxxxxxH in the catalytic domain and is considered a zinc metalloprotease. The human sequences for paraplegin published thus far include different splice variants of 795, 782, 677, 489 and 212 amino acid length. The full-length human paraplegin is 795 amino acids in length, with predicted mass of 88.2 kDa, and pI of 8.83. The 782, 677, 489 and 212 amino acid forms are predicted to have masses of 86.6, 74.8, 53.9 and 23.8 kDa respectively, with pI of 9.24, 8.0, 9.73 and 5.19. It is unclear if all of these splice variants are produced, and if so whether they posess different activity or localization. The 212 amino acid form starts at the end of the zinc binding domain, and is thus not proteolytically active. Likewise the 489 form ends before the zinc site, and is not an active enzyme. The 782 form differs in the carboxyterminus, but contains the zinc site, and is likely to be an active enzyme. The 677 form has a different aminoterminus, and starts 120 residues later than the 795 form, and has the same carboxy end as the 782 form, but contains the zinc site and is likely a competent protease. RP2-paraplegin recognizes all but the shortest (212 amino acid) form of human paraplegin. 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. EDTA/EGTA treatment of tissues or lysates is required to see latent zymogen. FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for 12 months at -20C.
Description
RP3-Paraplegin is a rabbit polyclonal antibody made to the metalloprotease paraplegin. The antibody is made to a synthetic peptide based on the AAA domain of human paraplegin. 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
Paraplegin, also known as Spastic Paraplegia Protein 7, is a metalloproteinase of the MA clan, family M41, which includes the Yme1 and FtsH proteases. The overall protein primary structure homology is 38% with YME1 and 47% with AFG3-like protein-2, the closest ortholog. All three enzymes are bound to the mitochondrial membrane, and contain an ATP-binding site. These enzymes are distinguished from the other mammalian metalloproteinases in their requirement for ATP activation, and their localization to the mitochondria. In the mitochondria paraplegin is thought to degrade misfolded proteins. Loss of function and null mutations in paraplegin lead to a disorder termed hereditary spastic paraplegia, caused by the buildup of the misfolded proteins which interfere with oxidative phosphorylation. Paraplegin contains the 'classical' zinc binding motif of HExxHxxxxxH in the catalytic domain and is considered a zinc metalloprotease. The human sequences for paraplegin published thus far include different splice variants of 795, 782, 677, 489 and 212 amino acid length. The full-length human paraplegin is 795 amino acids in length, with predicted mass of 88.2 kDa, and pI of 8.83. The 782, 677, 489 and 212 amino acid forms are predicted to have masses of 86.6, 74.8, 53.9 and 23.8 kDa respectively, with pI of 9.24, 8.0, 9.73 and 5.19. It is unclear if all of these splice variants are produced, and if so whether they posess different activity or localization. The 212 amino acid form starts at the end of the zinc binding domain, and is thus not proteolytically active. Likewise the 489 form ends before the zinc site, and is not an active enzyme. The 782 form differs in the carboxyterminus, but contains the zinc site, and is likely to be an active enzyme. The 677 form has a different aminoterminus, and starts 120 residues later than the 795 form, and has the same carboxy end as the 782 form, but contains the zinc site and is likely a competent protease. RP3-paraplegin recognizes all but the shortest (212 amino acid) form of human paraplegin. 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. EDTA/EGTA treatment of tissues or lysates is required to see latent zymogen. FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for 12 months at -20C.
Description
RP4-Paraplegin is a rabbit polyclonal antibody made to the metalloprotease paraplegin. The antibody is made to a synthetic peptide based on the catalytic domain of human paraplegin. 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
Paraplegin, also known as Spastic Paraplegia Protein 7, is a metalloproteinase of the MA clan, family M41, which includes the Yme1 and FtsH proteases. The overall protein primary structure homology is 38% with YME1 and 47% with AFG3-like protein-2, the closest ortholog. All three enzymes are bound to the mitochondrial membrane, and contain an ATP-binding site. These enzymes are distinguished from the other mammalian metalloproteinases in their requirement for ATP activation, and their localization to the mitochondria. In the mitochondria paraplegin is thought to degrade misfolded proteins. Loss of function and null mutations in paraplegin lead to a disorder termed hereditary spastic paraplegia, caused by the buildup of the misfolded proteins which interfere with oxidative phosphorylation. Paraplegin contains the 'classical' zinc binding motif of HExxHxxxxxH in the catalytic domain and is considered a zinc metalloprotease. The human sequences for paraplegin published thus far include different splice variants of 795, 782, 677, 489 and 212 amino acid length. The full-length human paraplegin is 795 amino acids in length, with predicted mass of 88.2 kDa, and pI of 8.83. The 782, 677, 489 and 212 amino acid forms are predicted to have masses of 86.6, 74.8, 53.9 and 23.8 kDa respectively, with pI of 9.24, 8.0, 9.73 and 5.19. It is unclear if all of these splice variants are produced, and if so whether they posess different activity or localization. The 212 amino acid form starts at the end of the zinc binding domain, and is thus not proteolytically active. Likewise the 489 form ends before the zinc site, and is not an active enzyme. The 782 form differs in the carboxyterminus, but contains the zinc site, and is likely to be an active enzyme. The 677 form has a different aminoterminus, and starts 120 residues later than the 795 form, and has the same carboxy end as the 782 form, but contains the zinc site and is likely a competent protease. RP4-paraplegin recognizes the 795, 782 and 677 forms of human paraplegin. 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. EDTA/EGTA treatment of tissues or lysates is required to see latent zymogen. FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for 12 months at -20C.
Description
RP5-Paraplegin is a rabbit polyclonal antibody made to the metalloprotease paraplegin. The antibody is made to a synthetic peptide based on the carboxyterminal end of the 782 and 677 amino acid forms of human paraplegin. 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
Paraplegin, also known as Spastic Paraplegia Protein 7, is a metalloproteinase of the MA clan, family M41, which includes the Yme1 and FtsH proteases. The overall protein primary structure homology is 38% with YME1 and 47% with AFG3-like protein-2, the closest ortholog. All three enzymes are bound to the mitochondrial membrane, and contain an ATP-binding site. These enzymes are distinguished from the other mammalian metalloproteinases in their requirement for ATP activation, and their localization to the mitochondria. In the mitochondria paraplegin is thought to degrade misfolded proteins. Loss of function and null mutations in paraplegin lead to a disorder termed hereditary spastic paraplegia, caused by the buildup of the misfolded proteins which interfere with oxidative phosphorylation. Paraplegin contains the 'classical' zinc binding motif of HExxHxxxxxH in the catalytic domain and is considered a zinc metalloprotease. The human sequences for paraplegin published thus far include different splice variants of 795, 782, 677, 489 and 212 amino acid length. The full-length human paraplegin is 795 amino acids in length, with predicted mass of 88.2 kDa, and pI of 8.83. The 782, 677, 489 and 212 amino acid forms are predicted to have masses of 86.6, 74.8, 53.9 and 23.8 kDa respectively, with pI of 9.24, 8.0, 9.73 and 5.19. It is unclear if all of these splice variants are produced, and if so whether they posess different activity or localization. The 212 amino acid form starts at the end of the zinc binding domain, and is thus not proteolytically active. Likewise the 489 form ends before the zinc site, and is not an active enzyme. The 782 form differs in the carboxyterminus, but contains the zinc site, and is likely to be an active enzyme. The 677 form has a different aminoterminus, and starts 120 residues later than the 795 form, and has the same carboxy end as the 782 form, but contains the zinc site and is likely a competent protease. RP5-paraplegin recognizes only the 677 and 782 forms of human paraplegin. 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. EDTA/EGTA treatment of tissues or lysates is required to see latent zymogen. FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for 12 months at -20C.
Description
RP6-Paraplegin is a rabbit polyclonal antibody made to the metalloprotease paraplegin. The antibody is made to a synthetic peptide based on the carboxyterminal end of full length human paraplegin. 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
Paraplegin, also known as Spastic Paraplegia Protein 7, is a metalloproteinase of the MA clan, family M41, which includes the Yme1 and FtsH proteases. The overall protein primary structure homology is 38% with YME1 and 47% with AFG3-like protein-2, the closest ortholog. All three enzymes are bound to the mitochondrial membrane, and contain an ATP-binding site. These enzymes are distinguished from the other mammalian metalloproteinases in their requirement for ATP activation, and their localization to the mitochondria. In the mitochondria paraplegin is thought to degrade misfolded proteins. Loss of function and null mutations in paraplegin lead to a disorder termed hereditary spastic paraplegia, caused by the buildup of the misfolded proteins which interfere with oxidative phosphorylation. Paraplegin contains the 'classical' zinc binding motif of HExxHxxxxxH in the catalytic domain and is considered a zinc metalloprotease. The human sequences for paraplegin published thus far include different splice variants of 795, 782, 677, 489 and 212 amino acid length. The full-length human paraplegin is 795 amino acids in length, with predicted mass of 88.2 kDa, and pI of 8.83. The 782, 677, 489 and 212 amino acid forms are predicted to have masses of 86.6, 74.8, 53.9 and 23.8 kDa respectively, with pI of 9.24, 8.0, 9.73 and 5.19. It is unclear if all of these splice variants are produced, and if so whether they posess different activity or localization. The 212 amino acid form starts at the end of the zinc binding domain, and is thus not proteolytically active. Likewise the 489 form ends before the zinc site, and is not an active enzyme. The 782 form differs in the carboxyterminus, but contains the zinc site, and is likely to be an active enzyme. The 677 form has a different aminoterminus, and starts 120 residues later than the 795 form, and has the same carboxy end as the 782 form, but contains the zinc site and is likely a competent protease. RP6-paraplegin recognizes all but the 489 form of human paraplegin. 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. EDTA/EGTA treatment of tissues or lysates is required to see latent zymogen. FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for 12 months at -20C.
