GOAT ANTI HUMAN ALPHA 1 ANTITRYPSIN

GWB-1F1A14

Polyclonal IgG

Recognises human alpha 1 antitrypsin a serine protease inhibitor synthesized by the liver. Hereditary deficiency of this protein is associated with pulmonary emphysema and with liver disease due to the loss of inhibition of neutrophil elastase activity. This reagent is available in bulk quantities and may be made available in other formats. Please enquire for further details. Recommended Secondary Antibodies: Rabbit Anti Goat IgG (Fc)

The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable. Post-translational modificationSeveral isomers are observed resulting from the combination of different N-linked glycan structures and mature N-terminus. N-linked glycan at Asn-107 is alternatively di-antennary tri-antennary or tetra-antennary whereas glycan at Asn-70 is di-antennary with trace amounts of tri-antennary and glycan at Asn-271 is exclusively di-antennary. The structure of the antennas is Neu5Ac(alpha1-6)Gal(beta1-4)GlcNAc attached to the core structure Man(alpha1-6)[Man(alpha1-3)]Man(beta1-4)GlcNAc(beta1-4)GlcNAc. Some antennas are fucosylated which forms a Lewis-X determinant. Proteolytic processing may yield the truncated form that ranges from Asp-30 to Lys-418.

The aberrant form is found in the plasma of chronic smokers and persists after smoking is ceased. It can still be found ten years after smoking has ceased. Sequence similaritiesBelongs to the serpin family. Sequence cautionThe sequence CAD62334. 1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAD62585. 1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. 1. Matsuzaki H. et al. (1987) Unique epitopes of common acute lymphoblastic leukemia antigen detected by new monoclonal antibodies. Cancer Res. 47: 2160-2166. 2. Biddle W. C. et al. (1989) in vitro and in vivo cytotoxic activity of anti-human leukemia monoclonal antibodies SN5c and SN6 daunorubicin conjugates. Leuk. Res. 13: 699-707. [1] \" Common acute lymphocytic leukemia antigen is identical to neutral endopeptidase. \" Letarte M. Vera S. Tran R. Addis J. B. L. Onizuka R. J. Quackenbush E. J. Jongeneel C. V. McInnes R. R. J. Exp. Med. 168:1247-1253(1988) [PubMed: 2971756] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney. [2] \" Molecular cloning of the common acute lymphoblastic leukemia antigen (CALLA) identifies a type II integral membrane protein. \" Shipp M. A. Richardson N. E. Sayre P. H. Brown N. R. Masteller E. L. Clayton L. K. Ritz J. Reinherz E. L. Proc. Natl. Acad. Sci. U. S. A. 85:4819-4823(1988) [PubMed: 2968607] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA]. [3] \" Organization of the gene encoding common acute lymphoblastic leukemia antigen (neutral endopeptidase 24. 11): multiple miniexons and separate 5\' untranslated regions. \" D\' Adamio L. Shipp M. A. Masteller E. L. Reinherz E. L. Proc. Natl. Acad. Sci. U. S. A. 86:7103-7107(1989) [PubMed: 2528730] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. [4] \" Complete sequencing and characterization of 21 243 full-length human cDNAs. \" Ota T. Suzuki Y. Nishikawa T. Otsuki T. Sugiyama T. Irie R. Wakamatsu A. Hayashi K. Sato H. Nagai K. Kimura K. Makita H. Sekine M. Obayashi M. Nishi T. Shibahara T. Tanaka T. Ishii S. Yamamoto J. Saito K. Kawai Y. Isono Y. Nakamura Y. Nagahari K. Murakami K. Yasuda T. Iwayanagi T. Wagatsuma M. Shiratori A. Sudo H. Hosoiri T. Kaku Y. Kodaira H. Kondo H. Sugawara M. Takahashi M. Kanda K. Yokoi T. Furuya T. Kikkawa E. Omura Y. Abe K. Kamihara K. Katsuta N. Sato K. Tanikawa M. Yamazaki M. Ninomiya K. Ishibashi T. Yamashita H. Murakawa K. Fujimori K. Tanai H. Kimata M. Watanabe M. Hiraoka S. Chiba Y. Ishida S. Ono Y. Takiguchi S. Watanabe S. Yosida M. Hotuta T. Kusano J. Kanehori K. Takahashi-Fujii A. Hara H. Tanase T. -O. Nomura Y. Togiya S. Komai F. Hara R. Takeuchi K. Arita M. Imose N. Musashino K. Yuuki H. Oshima A. Sasaki N. Aotsuka S. Yoshikawa Y. Matsunawa H. Ichihara T. Shiohata N. Sano S. Moriya S. Momiyama H. Satoh N. Takami S. Terashima Y. Suzuki O. Nakagawa S. Senoh A. Mizoguchi H. Goto Y. Shimizu F. Wakebe H. Hishigaki H. Watanabe T. Sugiyama A. Takemoto M. Kawakami B. Yamazaki M. Watanabe K. Kumagai A. Itakura S. Fukuzumi Y. Fujimori Y. Komiyama M. Tashiro H. Tanigami A. Fujiwara T. Ono T. Yamada K. Fujii Y. Ozaki K. Hirao M. Ohmori Y. Kawabata A. Hikiji T. Kobatake N. Inagaki H. Ikema Y. Okamoto S. Okitani R. Kawakami T. Noguchi S. Itoh T. Shigeta K. Senba T. Matsumura K. Nakajima Y. Mizuno T. Morinaga M. Sasaki M. Togashi T. Oyama M. Hata H. Watanabe M. Komatsu T. Mizushima-Sugano J. Satoh T. Shirai Y. Takahashi Y. Nakagawa K. Okumura K. Nagase T. Nomura N. Kikuchi H. Masuho Y. Yamashita R. Nakai K. Yada T. Nakamura Y. Ohara O. Isogai T. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta. [5] NHLBI resequencing and genotyping service (RS& amp; G)Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. [6] \" The status quality and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). \" The MGC Project TeamGenome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain. [7] \" Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase). \" Malfroy B. Kuang W. -J. Seeburg P. H. Mason A. J. Schofield P. R. FEBS Lett. 229:206-210(1988) [PubMed: 3162217] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-750. Tissue: Placenta. [8] \" Endopeptidase-24. 11 in human plasma degrades atrial natriuretic factor (ANF) to ANF(99-105/106-126). \" Yandle T. G. Brennan S. O. Espiner E. A. Nicholls M. G. Richards A. M. Peptides 10:891-894(1989) [PubMed: 2531377] [Abstract]Cited for: FUNCTION IN THE DEGRADATION OF ANF. [9] \" Asp650 is crucial for catalytic activity of neutral endopeptidase 24-11. \" Le Moual H. Dion N. Roques B. P. Crine P. Boileau G. Eur. J. Biochem. 221:475-480(1994) [PubMed: 8168535] [Abstract]Cited for: ACTIVE SITE ASP-651. [10] \" Identification and quantification of N-linked glycoproteins using hydrazide chemistry stable isotope labeling and mass spectrometry. \" Zhang H. Li X. -J. Martin D. B. Aebersold R. Nat. Biotechnol. 21:660-666(2003) [PubMed: 12754519] [Abstract]Cited for: GLYCOSYLATION AT ASN-145 AND ASN-285.