Description
RP1-BBS-1 is a rabbit polyclonal antibody made to the dipeptidyl peptidase-3 associated protein BBS-1. The antibody is made to a synthetic peptide based on the aminoterminal end of the short form of human BBS-1. 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
BBS-1 is one of a group of BBS proteins which when mutated produce Bardet-Biedl Syndrome. These BBS proteins are part of a heteromultimeric protein bundle that forms cilia, and the majority of the mutants reported are in the BBS-1 protein. BBS-1 constitutes the carboxyterminal end of a longer predicted protein, the aminoterminal portion of which is DPP-3. The BBS-1 sequence starts after the end of the DPP-3 sequence, and there is no sequence overlap. It is unclear what the relative production or distribution is for the chimeric protein, and several different splice variants are reported. BBS-1 protein without the DPP-3 sequence is the form that has been studied in Bardet-Biedl Syndrome, and there are several different variants published. DPP-3 was first described as an aminopeptidase from bovine pituitary that cleaved oligopeptides of four amino acids or longer. Poly-alanine, poly-lysine, poly-phenylalanine were cleaved, but not poly-glutamic acid or poly-glycine. Oligopeptides longer than 10 amino acids in length are thought to be poor substrates for DPP-3. Native substrates for DPP-3 include angiotensin II, angiotensin III, Leu-enkephalin, procolin, include (alpha)-melanocyte-stimulating hormone (6-9). Later works found DPP-3 to be fairly ubiquitous in expression, found in muscle tissue, erythrocytes, brain, lung, liver, and most tissues examined. Earlier names for DPP-3 include enkephalinase B, and red cell angiotensinase. DPP-3 is a zinc metalloproteinase of the gluzincin class, with a catalytic HELLGH motif, and a Glu508 as the final zinc coordinating residue. The HELLGH motif has an extra leucine in the zinc binding domain, relative to the matrix metalloproteinase and ADAM sequences, and interestingly is able to tolerate cobalt, nickel or zinc in the active enzyme. The BBS-1 sequences all start after the zinc metalloproteinase domain, and are not thought to be proteolytically active. The four published isoforms of BBS-1 are 593, 482, 463 and 446 amino acids in length, with predicted mass of 65.1, 53.1, 51.4 and 49 kDa respectively, and pI of 8.37, 7.5, 9.8 and 6.8. The 463 amino acid form has a distinct aminoterminus, which starts 100 residues downstream from the longer forms, and merges with the common form 60 residues later. RP1-BBS-1 recognizes all four forms of BBS-1, as well as the 1358 and 1355 amino acid forms of the chimeric protein. The antibody does not recognize DPP-3. 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. FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for approximately 12 months at -20C.
Description
RP2-BBS-1 is a rabbit polyclonal antibody made to the dipeptidyl peptidase-3 associated protein BBS-1. The antibody is made to a synthetic peptide based on carboxyterminal region of human BBS-1. 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
BBS-1 is one of a group of BBS proteins which when mutated produce Bardet-Biedl Syndrome. These BBS proteins are part of a heteromultimeric protein bundle that forms cilia, and the majority of the mutants reported are in the BBS-1 protein. BBS-1 constitutes the carboxyterminal end of a longer predicted protein, the aminoterminal portion of which is DPP-3. The BBS-1 sequence starts after the end of the DPP-3 sequence, and there is no sequence overlap. It is unclear what the relative production or distribution is for the chimeric protein, and several different splice variants are reported. BBS-1 protein without the DPP-3 sequence is the form that has been studied in Bardet-Biedl Syndrome, and there are several different variants published. DPP-3 was first described as an aminopeptidase from bovine pituitary that cleaved oligopeptides of four amino acids or longer. Poly-alanine, poly-lysine, poly-phenylalanine were cleaved, but not poly-glutamic acid or poly-glycine. Oligopeptides longer than 10 amino acids in length are thought to be poor substrates for DPP-3. Native substrates for DPP-3 include angiotensin II, angiotensin III, Leu-enkephalin, procolin, include (alpha)-melanocyte-stimulating hormone (6-9). Later works found DPP-3 to be fairly ubiquitous in expression, found in muscle tissue, erythrocytes, brain, lung, liver, and most tissues examined. Earlier names for DPP-3 include enkephalinase B, and red cell angiotensinase. DPP-3 is a zinc metalloproteinase of the gluzincin class, with a catalytic HELLGH motif, and a Glu508 as the final zinc coordinating residue. The HELLGH motif has an extra leucine in the zinc binding domain, relative to the matrix metalloproteinase and ADAM sequences, and interestingly is able to tolerate cobalt, nickel or zinc in the active enzyme. The BBS-1 sequences all start after the zinc metalloproteinase domain, and are not thought to be proteolytically active. The four published isoforms of BBS-1 are 593, 482, 463 and 446 amino acids in length, with predicted mass of 65.1, 53.1, 51.4 and 49 kDa respectively, and pI of 8.37, 7.5, 9.8 and 6.8. The 463 amino acid form has a distinct aminoterminus, which starts 100 residues downstream from the longer forms, and merges with the common form 60 residues later. RP2-BBS-1 recognizes all four forms of BBS-1, as well as the 1358 and 1355 amino acid forms of the chimeric protein. The antibody does not recognize DPP-3. 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. FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for approximately 12 months at -20C.
