Recombinant Human Protein Z-dependent protease inhibitor (SERPINA10)

Code CSB-YP891944HU
MSDS
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Source Yeast
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Code CSB-EP891944HU
MSDS
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Source E.coli
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Code CSB-EP891944HU-B
MSDS
Size Pls inquire
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-BP891944HU
MSDS
Size Pls inquire
Source Baculovirus
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Code CSB-MP891944HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
SERPINA10
Uniprot No.
Alternative Names
Protein Z dependent protease inhibitor; Protein Z dependent protease inhibitor precursor; Protein Z-dependent protease inhibitor; PZ dependent protease inhibitor; PZ-dependent protease inhibitor; PZI; serine (or cysteine) proteinase inhibitor clade A (alpha 1 antiproteinase antitrypsin) member 10; Serpin A10; Serpin peptidase inhibitor clade A (alpha 1 antiproteinase antitrypsin) member 10; SERPINA 10; SERPINA10; ZPI; ZPI_HUMAN
Species
Homo sapiens (Human)
Expression Region
22-444
Target Protein Sequence
LAPSPQSPE TPAPQNQTSR VVQAPKEEEE DEQEASEEKA SEEEKAWLMA SRQQLAKETS NFGFSLLRKI SMRHDGNMVF SPFGMSLAMT GLMLGATGPT ETQIKRGLHL QALKPTKPGL LPSLFKGLRE TLSRNLELGL TQGSFAFIHK DFDVKETFFN LSKRYFDTEC VPMNFRNASQ AKRLMNHYIN KETRGKIPKL FDEINPETKL ILVDYILFKG KWLTPFDPVF TEVDTFHLDK YKTIKVPMMY GAGKFASTFD KNFRCHVLKL PYQGNATMLV VLMEKMGDHL ALEDYLTTDL VETWLRNMKT RNMEVFFPKF KLDQKYEMHE LLRQMGIRRI FSPFADLSEL SATGRNLQVS RVLQRTVIEV DERGTEAVAG ILSEITAYSM PPVIKVDRPF HFMIYEETSG MLLFLGRVVN PTLL
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
Inhibits activity of the coagulation protease factor Xa in the presence of PROZ, calcium and phospholipids. Also inhibits factor XIa in the absence of cofactors.
Gene References into Functions
  1. PZ/ZPI polymorphisms do not appear to play an active role in the development of prosthesis heart valve thrombosis. PMID: 29302946
  2. Data suggest oxidized lipid vesicles with phosphatidylserine/polyunsaturated fatty acids promote inactivation of ZPI-PZ complex or free ZPI; binding of PZ-complexed or free ZPI to oxidized vesicles mediates inactivation of ZPI (an inhibitor of FXa); blocking heparin- (anticoagulant-)binding site on ZPI interferes with binding to lipid or PZ. (ZPI = protein Z-dependent protease inhibitor; PZ = protein Z; FXa = factor Xa) PMID: 28717005
  3. rs2232710 SNV showed no association with DVT in two Dutch replication cohorts the LETS study and the MEGA study, indicating that the rs2232710 variant is not a risk factor for DVT PMID: 26982741
  4. Results show the energetic basis of the Z-dependent protease inhibitor (ZPI)-protein Z (PZ) interaction and suggest an important role for ZPI Lys-239 in PZ catalytic action. PMID: 25713144
  5. The unbalance between PZ and ZPI in plasma samples from patients with Colorectal Cancer or Pancreatic Cancer is not only related to an inflammatory state but could also results from an ectopic synthesis of these proteins by the cancer cells. PMID: 24315319
  6. Protein Z EGF2 subdomain constitutes an interactive-site for ZPI protein. PMID: 24960590
  7. Protein Z/protein Z-dependent protease inhibitor and Fxa expression in human gastric cancer cells indicate that these proteins may play a role in anticoagulant events at the tumor tissue. PMID: 24158387
  8. the PZ/ZPI complex may play some modulating role in hemophilia A PMID: 23269381
  9. structural features within residues of the 39-loop contribute to the resistance of FIXa to inhibition by plasma inhibitors ZPI and TFPI. PMID: 23530052
  10. The study shows by Ala-scanning mutagenesis of the ZPI-binding interface, together with native PAGE and kinetic analyses of PZ binding to ZPI, that Tyr240 and Asp293 of ZPI are crucial hot spots for PZ binding. PMID: 22786881
  11. Report two missense mutations identified in venous thrombosis patients impair the inhibitory function of the ZPI were not convincingly associted with thrombosis risk. PMID: 22399118
  12. heparin-binding site of ZPI was mapped: basic residues of both helices C and D of ZPI interact with heparin to modulate the inhibitory function of the serpin. PMID: 22540147
  13. Plasma ZPI levels were unchanged in non-pregnant recurrent miscarriage women, while the plasma PZ level was slightly reduced, a finding consistent with existing reports. PMID: 22274138
  14. Medium expression of ZPI(IRS=6.5), together with weak expression of PZ(IRS=4), was observed in cancer cells. PMID: 21975032
  15. localization of PZ/ZPI and FX in colon cancer cells indicates that PZ/ZPI may contribute to anticoagulant events at the tumor site. PMID: 22424030
  16. The results demonstrate that both ZPI R67X and W303X non-sense variants and specific ZPI haplotypes are significantly associated with recurrent spontaneous miscarriage. PMID: 22039093
  17. heparin activates ZPI to inhibit free factor Xa as well as factor XIa and therefore may play a physiologically and pharmacologically important role in ZPI anticoagulant function. PMID: 21220417
  18. present in loco in human breast cancer tissue PMID: 20458435
  19. Data show that mutation of four ZPI contact residues eliminated PZ binding and membrane-dependent PZ acceleration of fXa inhibition. PMID: 20427285
  20. PROTEIN A AND PZI WERE FOUND IN KIDNEY TUBULES BY IMMUNOHISTOCHEMISTRY PMID: 20024489
  21. the catalytic residue of fXa is required for interaction with ZPI PMID: 16079143
  22. protein Z-dependent protease inhibitor may be an unusual physiologic regulator of both the intrinsic factor x-ase and the prothrombinase complexes. PMID: 16093243
  23. Our study supports that the ZPI Arg67Stop nonsense polymorphism might be an independent genetic risk factor for venous thrombosis. This polymorphism has slightly lower prevalence but similar thrombotic risk than the FV Leiden or prothrombin 20210A. PMID: 16527896
  24. a new R67Q mutation is found PMID: 17582153
  25. ZPI functions like other serpins to regulate the activity of FXa but in a manner uniquely dependent on protein Z, procoagulant membranes, and pH PMID: 18768472
  26. Data show that the structural model of ZPI/FXa is compatible with available experimental information regarding the importance for the inhibitory action of certain basic residues in FXa. PMID: 19172319

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Subcellular Location
Secreted.
Protein Families
Serpin family
Tissue Specificity
Expressed by the liver and secreted in plasma.
Database Links

HGNC: 15996

OMIM: 602455

KEGG: hsa:51156

STRING: 9606.ENSP00000261994

UniGene: Hs.118620

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