Rabbit anti-Human PC2 Polyclonal Antibody | anti-PC2 antibody

Anti-PC2 (Paired Basic Amino Acid Cleaving Enzyme-2, SPC2), Amino End Mature Enzyme Antibody

Cat. Num. AAA4157589

• Reactivity: Human
• Applications: Western Blot
• Purity: Immunogen Affinity Purified
• Synonyms: PC2; Polyclonal Antibody; Anti-PC2 (Paired Basic Amino Acid Cleaving Enzyme-2; SPC2); Amino End Mature Enzyme Antibody; anti-PC2 antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Isotype: IgG
• Purity/Purification: Immunogen Affinity Purified
• Form/Format: Liquid; PBS, pH 7.4 with 0.05% sodium azide.
• Concentration: 1ug/ul (varies by lot)
• Sequence Length: 822

• Applicable Applications for anti-PC2 antibody: Western Blot (WB)
• Application Notes: WB: 1:1000 (when using colorimetric substrates such as BCIP/NBT)-1:5000 (for chemiluminescent substrates). Detects bands of approximately 75 kDa (pre-pro form) due to glycosylation, 71 kDa (mature form) and a 66 kDa (carboxy-processed form). (Predicted molecular weight: 70 kDa). Dilution optimised using Chromogenic detection.
• Immunogen: Synthetic peptide based on the amino end of mature human PACE2.
• Cellular Localization: Secretory Vesicle. Localized in the secretion granules.
• Preparation and Storage: This product is stable for several weeks at 4 degree C as an undiluted liquid. Dilute only prior to immediate use.; For extended storage, aliquot contents and freeze at-20 degree C or below. Avoid cycles of freezing and thawing. Expiration date is one (1) year from date of receipt.

Testing Data

Related Product Information for anti-PC2 antibody

Description: The antibody is a rabbit polyclonal antibody made to the subtilisin-like serine protease PC2. The antibody is made to a synthetic peptide based on the amino end of mature human PC2. 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. PC2 was initially found as an insulin processing enzyme, and was the third of the human prohormone convertasae enzymes to be discovered. Like furin, PC1 and PACE4, PC2 is a serine proteinase that cleaves after pairs of basic amino acids, but with some differences in substrate specificity and distribution. The catalytic domain has homology to other PC enzymes, the prohormone convertase family initially discovered for their role in processing POMC, insulin and other pro-hormones, and later found to process a wider range of precursor proteins. Some have renamed the prohormone convertases as proprotein convertases, and another group has renamed the entire family with a uniform nomenclature of SPCs (s ubtilisin-like p roprotein c onvertases), with PC2 getting the SPC2 moniker. PC2 structure contains a propeptide domain, a catalytic domain and an RGD containing cystein-rich domain (homo-B). The PCs have an RxxR consensus cleavage requirement, and the propeptide is separated from the mature protein by just such a sequence. After cleavage of the propeptide domain, PC2 becomes a two-chain form, and the propeptide piece is released after a second internal cleavage. PC2 resides along with PC1, mainly in the dense core secretory vesicles and the TGN, and is cycled to the surface, with some of the PC2 being secreted from the cells. PC2 has been reported to be elevated in tumor cell lines and to increase tumor progression. PC2 is expressed at low levels in most tissues, but found in highest concentration in the brain, the anterior pituitary, pancreatic islet cells, thyroid, parathyroid and gut. PC2 cleaves a wide variety of proteins, including growth factors, viral coat proteins, matrix metalloproteinases, mostly after PC1 cleavage. The maturation of PC2 appears to require association with the 7B2 protein, which both helps fold PC2 properly and keeps the PC2 latent until the 7B2 protein is clipped by a PC enzyme. The message for PC2 encodes a 638 amino acid protein with a predicted mass of 70.57 kDa, and a pI of 6.03, but glycosylation and other post-translational modifications make the pre-pro PC2 run at 75 kDa, the mature PC2 at 71 kDa, and carboxy-processed PC2 at 66 kDa. Smaller cleavage products_recover are also detected. 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.

Relevance: PC2 was initially found as an insulin processing enzyme, and was the third of the human prohormone convertasae enzymes to be discovered. Like furin, PC1 and PACE4, PC2 is a serine proteinase that cleaves after pairs of basic amino acids, but with some differences in substrate specificity and distribution. The catalytic domain has homology to other PC enzymes, the prohormone convertase family initially discovered for their role in processing POMC, insulin and other pro-hormones, and later found to process a wider range of precursor proteins. Some have renamed the prohormone convertases as proprotein convertases, and another group has renamed the entire family with a uniform nomenclature of SPCs (s ubtilisin-like p roprotein c onvertases), with PC2 getting the SPC2 moniker. PC2 structure contains a propeptide domain, a catalytic domain and an RGD containing cystein-rich domain (homo-B). The PCs have an RxxR consensus cleavage requirement, and the propeptide is separated from the mature protein by just such a sequence. After cleavage of the propeptide domain, PC2 becomes a two-chain form, and the propeptide piece is released after a second internal cleavage. PC2 resides along with PC1, mainly in the dense core secretory vesicles and the TGN, and is cycled to the surface, with some of the PC2 being secreted from the cells. PC2 has been reported to be elevated in tumor cell lines and to increase tumor progression. PC2 is expressed at low levels in most tissues, but found in highest concentration in the brain, the anterior pituitary, pancreatic islet cells, thyroid, parathyroid and gut. PC2 cleaves a wide variety of proteins, including growth factors, viral coat proteins, matrix metalloproteinases, mostly after PC1 cleavage. The maturation of PC2 appears to require association with the 7B2 protein, which both helps fold PC2 properly and keeps the PC2 latent until the 7B2 protein is clipped by a PC enzyme.

NCBI and Uniprot Product Information

• NCBI GI #: 549130065
• NCBI Official Full Name: PC2
• Protein Family: Putative envelope glycoprotein