Recombinant Human Alpha-2-antiplasmin (SERPINF2)

Code CSB-YP021085HU
MSDS
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Source Yeast
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Code CSB-EP021085HU
MSDS
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Source E.coli
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Code CSB-EP021085HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP021085HU
MSDS
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Source Baculovirus
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Code CSB-MP021085HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
SERPINF2
Uniprot No.
Alternative Names
A2AP; A2AP_HUMAN; AAP; Alpha 2 antiplasmin; Alpha 2 antiplasmin pigment epithelium derived factor; Alpha 2 AP; ALPHA 2 PI; Alpha 2 plasmin inhibitor; Alpha 2 plasmin inhibitor deficiency; Alpha-2-antiplasmin; Alpha-2-AP; Alpha-2-PI; Alpha-2-plasmin inhibitor; Antiplasmin deficiency; API; Plasmin inhibitor deficiency; PLI; Serine (or cysteine) peptidase inhibitor; clade F; member 2; Serine (Or cysteine) peptidase inhibitor; clade F; member 2; isoform CRA_c; Serine (or cysteine) proteinase inhibitor; clade F (alpha 2 antiplasmin pigment epithelium derived factor) member 2; Serine (Or cysteine) proteinase inhibitor; clade F; member 2; Serine or cysteine peptidase inhibitor clade F member 2; Serpin F2; Serpin peptidase inhibitor clade F; Serpin peptidase inhibitor; clade F (alpha 2 antiplasmin pigment epithelium derived factor) member 2; SERPINF2
Species
Homo sapiens (Human)
Expression Region
40-491
Target Protein Sequence
N QEQVSPLTLL KLGNQEPGGQ TALKSPPGVC SRDPTPEQTH RLARAMMAFT ADLFSLVAQT STCPNLILSP LSVALALSHL ALGAQNHTLQ RLQQVLHAGS GPCLPHLLSR LCQDLGPGAF RLAARMYLQK GFPIKEDFLE QSEQLFGAKP VSLTGKQEDD LANINQWVKE ATEGKIQEFL SGLPEDTVLL LLNAIHFQGF WRNKFDPSLT QRDSFHLDEQ FTVPVEMMQA RTYPLRWFLL EQPEIQVAHF PFKNNMSFVV LVPTHFEWNV SQVLANLSWD TLHPPLVWER PTKVRLPKLY LKHQMDLVAT LSQLGLQELF QAPDLRGISE QSLVVSGVQH QSTLELSEVG VEAAAATSIA MSRMSLSSFS VNRPFLFFIF EDTTGLPLFV GSVRNPNPSA PRELKEQQDS PGNKDFLQSL KGFPRGDKLF GPDLKLVPPM EEDYPQFGSP K
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Serine protease inhibitor. The major targets of this inhibitor are plasmin and trypsin, but it also inactivates matriptase-3/TMPRSS7 and chymotrypsin.
Gene References into Functions
  1. alpha2AP has a profibrotic effect probably not by the action as a plasmin inhibitor, and the blocking of alpha2AP exerts an antifibrotic effect in humans and mice with systemic sclerosis PMID: 26743600
  2. This review presents recent findings regarding the main aspects of the natural heterogeneity of A2AP with particular focus on the functional and possible clinical implications. [review] PMID: 26626994
  3. Possession of the alpha2AP 407Lys allele was negatively associated with AAA, and thus changes in alpha2AP may affect aneurysm growth and development. PMID: 25065555
  4. Changes in plasma A2AP are associated with cardiovascular disease event presentation. PMID: 26088309
  5. A significant correlation was found between soluble fibroblast activation protein levels and alpha2-antiplasmin cleavage in coronary thrombosis. PMID: 25464232
  6. increased N-terminal cleavage of alpha2AP may have a role in liver cirrhosis PMID: 24034420
  7. FXIII-A has a functional role through exposure on the activated platelet membrane where it exerts antifibrinolytic function by cross-linking alpha2AP to fibrin PMID: 25331118
  8. Data suggest serum A2AP (SERPINF2) level can serve as biomarker for diabetic retinopathy; levels of A2AP (but not fibrinogen, plasminogen, or plasminogen activator inhibitor 1) are up-regulated in hyperglycemic type 1 diabetes with retinopathy. PMID: 24818165
  9. protective mediator during gram-negative (pneumo)sepsis, limiting bacterial growth, inflammation, tissue injury, and coagulation PMID: 23992406
  10. Study revealed that plasmin was present in tumor tissue, and that it was responsible for processing progalanin to galanin(1-20) in the extracellular environment. PMID: 21707521
  11. Data suggest that decreased amounts of alpha2-plasmin inhibitor in plasma vs serum ex vivo may reflect reduced factor XIII (FXIII) in vivo; thus, plasma vs serum alpha2-plasmin inhibitor may be useful diagnostic marker for severe FXIII deficiency. PMID: 22205503
  12. fibrinolysis is enhanced by inhibiting enzymatic cleavage of precursor alpha2-antiplasmin PMID: 21251197
  13. Truncation of monocyte chemoattractant protein 1 by plasmin promotes blood-brain barrier disruption. PMID: 21486949
  14. Levels of free full-length alpha2AP were decreased in myocardial infarction (MI); the percentage of C-terminally cleaved alpha2AP was unaltered, and Arg407Lys did not influence alpha2AP levels or MI risk. PMID: 21505192
  15. the antifibrinolytic function of FXIII is independent of fibrin-fibrin cross-linking and is expressed exclusively through alphaAP. PMID: 21471521
  16. ADAMTS13 inactivation by plasmin as a potential cause of thrombotic thrombocytopenic purpura PMID: 20553378
  17. deficiency in patients with Philadelphia chromosome-positive haematologic cancer receiving imatinib mesylate PMID: 19492163
  18. OPN is highly susceptible to cleavage near its integrin-binding motifs, and the protein is a novel substrate for plasmin and cathepsin D PMID: 20071328
  19. FXIIIa substrate, A2AP, sequences suggests that the residue located two positions beyond the reactive glutamine is not conserved. this position makes important contributions to effective FXIIIa-A2AP interactions PMID: 19691486
  20. Multiple Lys residues within alpha 2-antiplasmin contribute, perhaps in a zipper-like fashion, to its binding to the in-tandem, multikringle array that configures the plasmin heavy chain. PMID: 12549929
  21. Alpha2-antiplasmin has an important role in acute pulmonary embolism PMID: 12911586
  22. the Arg6Trp polymorphism may play a significant role in governing the long-term deposition/removal of intravascular fibrin PMID: 17317851
  23. Fibrinolysis is amplified by converting alpha-antiplasmin from a plasmin inhibitor to a substrate PMID: 17883703
  24. Hydroxyethyl starch (HES) dilution enhances fibrinolysis by diminishing alpha2-antiplasmin-plasmin interactions. PMID: 17890952
  25. Sequencing analysis revealed the presence of two alpha2-PI gene variations, both in the second half of exon 10: a frameshift mutation and a G to A transition at nucleotide 11337 in codon 407. PMID: 17961166
  26. Thrombin activatable fibrinolysis inhibitor and alpha(2)-antiplasmin are not markers for recanalization in patients with ischemic stroke treated with recombinant tissue-type plasminogen activator. PMID: 18048863
  27. Plasmin in nephrotic urine activates the epithelial sodium channel PMID: 19073825

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Involvement in disease
Alpha-2-plasmin inhibitor deficiency (APLID)
Subcellular Location
Secreted.
Protein Families
Serpin family
Tissue Specificity
Expressed by the liver and secreted in plasma.
Database Links

HGNC: 9075

OMIM: 262850

KEGG: hsa:5345

STRING: 9606.ENSP00000321853

UniGene: Hs.159509

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