Rabbit anti-Human PC1 Polyclonal Antibody | anti-PC1 antibody

Anti-PC1 (Paired Basic Amino Acid Cleaving Enzyme-1, PC3, SPC3), Homo-B Domain Antibody

Cat. Num. AAA4157588

• Gene Names: PCSK1; PC1; PC3; NEC1; SPC3; BMIQ12
• Reactivity: Human
• Applications: Western Blot
• Purity: Immunogen Affinity Purified
• Synonyms: PC1; Polyclonal Antibody; Anti-PC1 (Paired Basic Amino Acid Cleaving Enzyme-1; PC3; SPC3); Homo-B Domain Antibody; anti-PC1 antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Isotype: IgG
• Specificity: This antibody recognises the Homo-B domain of subtilisin-like serine protease PC1.
• 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: 753

• Applicable Applications for anti-PC1 antibody: Western Blot (WB)
• Application Notes: WB: 1:1000 when using colorimetric substrates such as BCIP/NBT and 1:5000 for chemiluminescent substrates. Predicted molecular weight: 84 kDa. Dilution optimised using Chromogenic detection.
• Immunogen: Synthetic peptide corresponding to the carboxy end of the homo B domain of human PC1.
• Cellular Localization: Golgi Apparatus and Nuclear
• 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-PC1 antibody

Description: The antibody is a rabbit polyclonal antibody made to the subtilisin-like serine protease PC1. The antibody is made to a synthetic peptide based on the carboxy end of the homo-B domain of human PC1. 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. PC1 was the first of the human prohormone convertasae enzymes to be discovered. A literature alias is PC3, and PC1 is often referred to as PC1/3. Like furin, PC2 and PACE4, PC1 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 PC1 getting the SPC3 moniker. PC1 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, PC1 becomes a two-chain form, and the propeptide piece is released after a second internal cleavage. PC1 is further processed by cleavage at the carboxyterminal end, which enhances the PC1 enzymatic activity. PC1 resides mainly in the dense core secretory vesicles and the TGN, and is cycled to the surface, with some of the PC1 being secreted from the cells. PC1 has been reported to be elevated in tumor cell lines and to increase tumor progression. PC1 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. PC1 null mutant mice suffer dwarfism, and PC1 mutants have been linked to obesity and diabetes in humans. PC1 cleaves a wide variety of proteins, including growth factors, viral coat proteins, matrix metalloproteinases, mostly activating latent forms of the proteins. The message for PC1 encodes a 753 amino acid protein with a predicted mass of 84.15 kDa, and a pI of 5.58, but glycosylation and other post-translational modifications make the pre-pro PC1 run at 94 kDa, the mature PC1 at 87 and 83 kDa, and carboxy-processed PC1 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: The subtilisin-like Prohormone Convertase (PC) family is a group of cellular enzymes that cleave most prohormones and neuropeptide precursors. Numerous other cellular proteins, some viral proteins, and bacterial toxins that are transported by the constitutive secretory pathway are also targeted for maturation by PCs. PC family members share structural similarities, which include a heterogeneous ~10 kDa amino-terminal proregion, a highly conserved ~55 kDa subtilisin-like catalytic domain, and carboxyl-terminal domain that is heterogeneous in length and sequence. These enzymes become catalytically active following proregion cleavage within the appropriate cellular compartment. The subcellular localization of PC family members varies. Immunolocalization studies show that PC1 is found in the perinuclear region as well as the trans-Golgi network, whereas PC2 can be found in the trans-Golgi network as well as diffusely distributed in the peripheral cytoplasm.

NCBI and Uniprot Product Information

• NCBI GI #: 189117
• NCBI GeneID: 5122
• NCBI Official Full Name: PC1
• NCBI Official Synonym Full Names: proprotein convertase subtilisin/kexin type 1
• NCBI Official Symbol: PCSK1
• NCBI Official Synonym Symbols: PC1; PC3; NEC1; SPC3; BMIQ12
• NCBI Protein Information: neuroendocrine convertase 1

NCBI Description

This gene encodes a member of the subtilisin-like proprotein convertase family, which includes proteases that process protein and peptide precursors trafficking through regulated or constitutive branches of the secretory pathway. The encoded protein undergoes an initial autocatalytic processing event in the ER to generate a heterodimer which exits the ER and sorts to subcellular compartments where a second autocatalytic even takes place and the catalytic activity is acquired. The protease is packaged into and activated in dense core secretory granules and expressed in the neuroendocrine system and brain. This gene encodes one of the seven basic amino acid-specific members which cleave their substrates at single or paired basic residues. It functions in the proteolytic activation of polypeptide hormones and neuropeptides precursors. Mutations in this gene have been associated with susceptibility to obesity and proprotein convertase 1/3 deficiency. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene [provided by RefSeq, Jan 2014]