Products
Research Areas
COVID-19
Resources
Login
Quick Order
Cart
Login
Registration enables users to use special features of this website, such as past
order histories, retained contact details for faster checkout, review submissions, and special promotions.


Fields marked with a * are required.

Login
Quick Order
Contact Us

Locations


Orders Processing,
Shipping & Receiving,
Warehouse

2 Shaker Rd Suites
B001/B101
Shirley, MA 01464


Production Lab

Floor 6, Suite 620
20700 44th Avenue W
Lynnwood, WA 98036

Telephone Numbers



Tel: +1 (206) 374-1102
Fax: +1 (206) 577-4565

Contact Us



Additional Contact Details

Login
Registration enables users to use special features of this website, such as past
order histories, retained contact details for faster checkout, review submissions, and special promotions.


Fields marked with a * are required.

Login
Quick Order

SERPINA1 / Alpha 1 Antitrypsin

serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1

Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.Short peptide from AAT: reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE).

Gene Name: serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1
Synonyms: SERPINA1, A1A, A1AT, AAT, Alpha 1 Antitrypsin, Alpha-1 protease inhibitor, Alpha-1-antiproteinase, Alpha-1-antitrypsin, Alpha1AT, PRO2275, Alpha-1-antitrypsin null, PI1, Serpin A1, Alpha 1 AT
Target Sequences: K02212 AAB59495.1 P01009

Publications (5)

1
Skeletal muscle lipogenic protein expression is not different between lean and obese individuals: a potential factor in ceramide accumulation. Thrush AB, Brindley DN, Chabowski A, Heigenhauser GJ, Dyck DJ. The Journal of clinical endocrinology and metabolism. 2009 94:5053-61. [PubMed:19837942]
2
Derlin-2-deficient mice reveal an essential role for protein dislocation in chondrocytes. Dougan SK, Hu CC, Paquet ME, Greenblatt MB, Kim J, Lilley BN, Watson N, Ploegh HL. Molecular and cellular biology. 2011 31:1145-59. (WB, IP; Mouse) [PubMed:21220515] [PMC:PMC3067910]
3
Dual role of ancient ubiquitous protein 1 (AUP1) in lipid droplet accumulation and endoplasmic reticulum (ER) protein quality control. Klemm EJ, Spooner E, Ploegh HL. The Journal of biological chemistry. 2011 286:37602-14. [PubMed:21857022] [PMC:PMC3199505]
4
Analysis of proteins in human gingival crevicular fluid by mass spectrometry. Kido J, Bando M, Hiroshima Y, Iwasaka H, Yamada K, Ohgami N, Nambu T, Kataoka M, Yamamoto T, Shinohara Y, Sagawa I, Nagata T. Journal of periodontal research. 2012 47:488-99. (WB; Human) [PubMed:22220998]
5
Neonatal NET-inhibitory factor and related peptides inhibit neutrophil extracellular trap formation. Yost CC, Schwertz H, Cody MJ, Wallace JA, Campbell RA, Vieira-de-Abreu A, Araujo CV, Schubert S, Harris ES, Rowley JW, Rondina MT, Fulcher JM, Koening CL, Weyrich AS, Zimmerman GA. The Journal of clinical investigation. 2016 126:3783-3798. (WB; Human) [Full Text Article] [PubMed:27599294]
more

Your search did not match any products.


If you do not find the reagent or information you require, please contact Customer.Support@LSBio.com to inquire about additional products in development.

PLEASE NOTE

For RESEARCH USE ONLY. Intended for use by laboratory professionals. Not intended for human diagnostic or therapeutic purposes.

The data on this page has been compiled from LifeSpan internal sources, the National Center for Biotechnology Information (NCBI), and The Universal Protein Resource (UniProt).