Human SERPINA1 Recombinant Protein (RPPB4625)
- SKU:
- RPPB4625
- Product type:
- Recombinant Protein
- Size:
- 25ug
- Species:
- Human
- Target:
- SERPINA1
- Synonyms:
- Alpha-1-antitrypsin
- Alpha-1 protease inhibitor
- Alpha-1-antiproteinase
- SERPINA1
- Source:
- Escherichia Coli
- Uniprot:
- P01009
Description
| Product Name: | Human SERPINA1 Recombinant Protein |
| Product Code: | RPPB4625 |
| Size: | 25µg |
| Species: | Human |
| Target: | SERPINA1 |
| Synonyms: | Alpha-1-antitrypsin, Alpha-1 protease inhibitor, Alpha-1-antiproteinase, SERPINA1, A1AT, PI, A1A, AAT, PI1, MGC9222, PRO2275, MGC23330. |
| Source: | Escherichia Coli |
| Physical Appearance: | Sterile Filtered colorless solution. |
| Formulation: | The protein solution contains 20mM Tris-HCl pH-7.5, 1mM DTT, 10% glycerol, and 2mM EDTA. |
| Stability: | Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles. |
| Purity: | Greater than 90% as determined by SDS-PAGE. |
| Amino Acid Sequence: | MEDPQGDAAQ KTDTSHHDQD HPTFNKITPN LAEFAFSLYR QLAHQSNSTN IFFSPVSIAT AFAMLSLGTK ADTHDEILEG LNFNLTEIPE AQIHEGFQEL LRTLNQPDSQ LQLTTGNGLF LSEGLKLVDK FLEDVKKLYH SEAFTVNFGD TEEAKKQIND YVEKGTQGKI VDLVKELDRD TVFALVNYIF FKGKWERPFE VKDTEEEDFH VDQVTTVKVP MMKRLGMFNI QHCKKLSSWV LLMKYLGNAT AIFFLPDEGK LQHLENELTH DIITKFLENE DRRSASLHLP KLSITGTYDL KSVLGQLGIT KVFSNGADLS GVTEEAPLKL SKAVHKAVLT IDEKGTEAAG AMFLEAIPMS IPPEVKFNKP FVFLMIDQNT KSPLFMGKVV NPTQK |
SERPINA1 is secreted and is a serine protease inhibitor which its targets include elastase, plasmin, collagenase, thrombin, leucocytic proteases, trypsin, chymotrypsin, and plasminogen activator. Defects in SERPINA1 gene can cause emphysema or liver disease. Antral SERPINA1 expression is particularly induced by H. pylori infection. lung and prostate cancers have shown a significant increase in SERPINA1 serum levels compared with healthy controls though breast cancers did not show a significant change. SERPINA1 is an endogenous inhibitor of serine proteases and inhibits the catalytic domain of human recombinant matriptase in vitro. Rise in SERPINA1 occurs as an acute phase response to tissue necrosis and inflammation. mutations in SERPINA1 and SLC11A1 genes change the balance between elastase produced by leukocytes during phagocytosis.
SERPINA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 395 amino acids (25-418) and having a molecular mass of 44.4 kDa. The SERPINA1 protein is purified by proprietary chromatographic techniques.
| UniProt Protein Function: | 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. Ref.17 Ref.18 Ref.24Short peptide from AAT (SPAAT) is a 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). Ref.17 Ref.18 Ref.24 |
| UniProt Protein Details: | Subcellular location: Secreted Ref.24. Short peptide from AAT: Secreted › extracellular space › extracellular matrix Ref.24. Tissue specificity: Plasma. Domain: 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 modification: Several 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. Polymorphism: The sequence shown is that of the M1V allele which is the most common form of PI (44 to 49%). Other frequent alleles are: M1A 20 to 23%; M2 10 to 11%; M3 14 to 19%. Involvement in Disease: Defects in SERPINA1 are the cause of alpha-1-antitrypsin deficiency (A1ATD) [ MIM:613490]. 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. Ref.58 Ref.60 Ref.62 Miscellaneous: 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 similarities: Belongs to the serpin family. Sequence caution: The sequence CAD62334.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.The sequence CAD62585.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. |
| NCBI Summary: | 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. [provided by RefSeq] |
| UniProt Code: | P01009 |
| NCBI GenInfo Identifier: | 1703025 |
| NCBI Gene ID: | 5265 |
| NCBI Accession: | P01009.3 |
| UniProt Secondary Accession: | P01009,Q0PVP5, Q13672, Q53XB8, Q5U0M1, Q7M4R2, Q86U18 Q86U19, Q96BF9, Q96ES1, A6PX14, B2RDQ8, |
| UniProt Related Accession: | P01009,Q13747,Q2L9S7,Q3I0J7,Q9P173 |
| Molecular Weight: | 46,737 Da |
| NCBI Full Name: | Alpha-1-antitrypsin |
| NCBI Synonym Full Names: | serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1 |
| NCBI Official Symbol: | SERPINA1 |
| NCBI Official Synonym Symbols: | PI; A1A; AAT; PI1; A1AT; MGC9222; PRO2275; MGC23330; alpha1AT |
| NCBI Protein Information: | alpha-1-antitrypsin; serpin A1; OTTHUMP00000197150; OTTHUMP00000197151; OTTHUMP00000197152; OTTHUMP00000197153; OTTHUMP00000197154; alpha-1-antiproteinase; alpha-1 protease inhibitor; protease inhibitor 1 (anti-elastase), alpha-1-antitrypsin; serine (or cysteine) proteinase inhibitor, clade A, member 1 |
| UniProt Protein Name: | Alpha-1-antitrypsin |
| UniProt Synonym Protein Names: | Alpha-1 protease inhibitor; Alpha-1-antiproteinase; Serpin A1 |
| Protein Family: | Alpha-1-antitrypsin |
| UniProt Gene Name: | SERPINA1 |
| UniProt Entry Name: | A1AT_HUMAN |
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