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Mouse Anti-SERPINA1 Recombinant Antibody (F46.4.1) (CBMAB-S6324-CQ)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
F46.4.1
Antibody Isotype
IgG1, κ
Application
ELISA, IHC-P

Basic Information

Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.1% BSA
Preservative
0.1% sodium azide
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Serpin Family A Member 1
Introduction
The protein encoded by this gene is secreted and is a serine protease inhibitor whose targets include elastase, plasmin, thrombin, trypsin, chymotrypsin, and plasminogen activator. Defects in this gene can cause emphysema or liver disease. Several transcript variants encoding the same protein have been found for this gene.
Entrez Gene ID
5265
UniProt ID
P01009
Alternative Names
Serpin Family A Member 1; Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 1; Protease Inhibitor 1 (Anti-Elastase), Alpha-1-Antitrypsin; Alpha-1 Protease Inhibitor; Alpha-1-Antiproteinase; Serpin A1; AAT; PI; Serine (Or Cysteine) Proteinase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 1; Serpin Peptidase Inhibitor Clade A (Alpha-1antiproteinase, Antitrypsin) Member 1; Serine (Or Cysteine) Proteinase Inhibitor, Clade A, Member 1; Alpha-1-Antitrypsin Short Transcript Variant 1C4;
Function
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).
Biological Process
Biological Process acute-phase responseIEA:UniProtKB-KW
Biological Process blood coagulationIEA:UniProtKB-KW
Biological Process negative regulation of endopeptidase activityManual Assertion Based On ExperimentIBA:GO_Central
Cellular Location
Secreted
Endoplasmic reticulum
The S and Z allele are not secreted effectively and accumulate intracellularly in the endoplasmic reticulum.
Short peptide from AAT
Secreted, extracellular space, extracellular matrix
Involvement in disease
Alpha-1-antitrypsin deficiency (A1ATD):
A disorder whose most common manifestation is emphysema, which becomes evident by the third to fourth decade. A less common manifestation of the deficiency is liver disease, which occurs in children and adults, and may result in cirrhosis and liver failure. Environmental factors, particularly cigarette smoking, greatly increase the risk of emphysema at an earlier age.
PTM
N-glycosylated. Differential glycosylation produces a number of isoforms. N-linked glycan at Asn-107 is alternatively di-antennary, tri-antennary or tetra-antennary. The glycan at Asn-70 is di-antennary with trace amounts of tri-antennary. Glycan at Asn-271 is exclusively di-antennary. Structure of glycans at Asn-70 and Asn-271 is Hex5HexNAc4. The structure of the antennae 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 antennae are fucosylated, which forms a Lewis-X determinant.
Proteolytic processing may yield the truncated form that ranges from Asp-30 to Lys-418.
(Microbial infection) Proteolytically processed by Staphylococcus aureus seryl, cysteinyl, and metallo-proteases.
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For research use only. Not intended for any clinical use.

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