Biotinylated Recombinant Human Serpin B9 (SERPINB9) Protein (MBP&His-Avi)

Beta LifeScience SKU/CAT #: BLC-06829P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Biotinylated Recombinant Human Serpin B9 (SERPINB9) Protein (MBP&His-Avi)

Beta LifeScience SKU/CAT #: BLC-06829P
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Product Overview

Description Biotinylated Recombinant Human Serpin B9 (SERPINB9) Protein (MBP&His-Avi) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P50453
Target Symbol SERPINB9
Species Homo sapiens (Human)
Expression System E.coli
Tag N-MBP&C-6His-Avi
Target Protein Sequence METLSNASGTFAIRLLKILCQDNPSHNVFCSPVSISSALAMVLLGAKGNTATQMAQALSLNTEEDIHRAFQSLLTEVNKAGTQYLLRTANRLFGEKTCQFLSTFKESCLQFYHAELKELSFIRAAEESRKHINTWVSKKTEGKIEELLPGSSIDAETRLVLVNAIYFKGKWNEPFDETYTREMPFKINQEEQRPVQMMYQEATFKLAHVGEVRAQLLELPYARKELSLLVLLPDDGVELSTVEKSLTFEKLTAWTKPDCMKSTEVEVLLPKFKLQEDYDMESVLRHLGIVDAFQQGKADLSAMSAERDLCLSKFVHKSFVEVNEEGTEAAAASSCFVVAECCMESGPRFCADHPFLFFIRHNRANSILFCGRFSSP
Expression Range 1-376aa
Protein Length Full Length
Mol. Weight 90.2 kDa
Research Area Immunology
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Granzyme B inhibitor.
Subcellular Location Cytoplasm.
Protein Families Serpin family, Ov-serpin subfamily
Database References

Gene Functions References

  1. Data show that the serine protease inhibitor B9 (serpinB9) mediated caspase-1 inhibition regulates IL-1beta release in monocytes. PMID: 26992230
  2. Treatment with estrogens further increased PI-9 level while decreased that of ERalpha66 isoform thus excluding the involvement of this receptor isoform in the event. Moreover, our studies also provided evidence that tertiary tumorspheres express elevated levels of CXCR4 and phospho-p38, suggesting that the high PI-9 content might be ascribed to the activation of the proliferative CXCR4/phospho-p38 axis. PMID: 27121069
  3. Data show that oropharyngeal squamous cell carcinomas (OPSCCs) express granzyme inhibitors SERPINB1, SERPINB4 and SERPINB9 for cytotoxicity and the expression was not different between human papillomavirus (HPV)-positive and HPV-negative tumors. PMID: 26993499
  4. Pediatric CNS-PNETs evade immune recognition by downregulating cell surface MHC-I and CD1d expression. Intriguingly, expression of SERPINB9, SERPINB1, and SERPINB4 is acquired during tumorigenesis in 29%, 29%, and 57% of the tumors PMID: 26963506
  5. Data suggest that reactive oxygen species (ROS) generated within cytotoxic lymphocytes by receptor stimulation are required for lysosomal permeabilization and release of GzmB (granzyme B) into the cytosol and for inactivation of serpin B9. PMID: 26670609
  6. Increased intracellular PI-9 activity in mononuclear phagocytes from HIV-infected patients contributes to successful intracellular infection by virulent Mycobacterium tuberculosis. PMID: 24445365
  7. The GrB-Sb9 nexus may therefore represent an additional mechanism of limiting lymphocyte lifespan and populations. PMID: 24488096
  8. Suppression of granzyme B initiated apoptosis in protease inhibitor-9-expressing leukemia cells. PMID: 23892923
  9. SerpinB9 expression in human renal tubular epithelial cells is induced by triggering of the viral dsRNA sensors TLR3, MDA5 and RIG-I during subclinical rejection. PMID: 22167597
  10. lung cancer cells utilise their increased PI-9 expression to protect from granzyme B-mediated cytotoxicity as an immune evasion mechanism PMID: 22387007
  11. Inhibition of Granzyme B by PI-9 protects prostate cancer cells from apoptosis. PMID: 21919028
  12. Reduced proteinase inhibitor 9 expression in human vascular smooth muscle cells is associated with atherosclerotic disease progression. PMID: 21296596
  13. PI-9 induction within human mononuclear phagocytes by virulent Mycobacterium tuberculosis serves to protect these primary targets of infection from elimination by apoptosis and thereby promotes intracellular survival of the organism. PMID: 22090449
  14. constitutive expression of serine protease inhibitor 9 (PI-9) on human peripheral blood-and bone marrow-derived mesenchymal stem cells is a major defense mechanism against granzyme B-mediated destruction by NK cells PMID: 21795594
  15. upregulated expression of PI-9 in NSCLC cells may serve to protect them from apoptosis induced by GrB PMID: 19956856
  16. Expression levels of apoptosis-related proteins caspase 3, Bcl-2, and PI9 predict clinical outcome in anaplastic large cell lymphoma. PMID: 12036886
  17. The presence and subcellular localization of proteinase inhibitor 9 in leukocytes and dendritic cells are consistent with a protective role against ectopic or misdirected granzyme B during an immune response. PMID: 12517944
  18. a high expression of PI-9 by tubular epithelial cells can serve as one of the factors protecting renal allografts from rejection in spite of the presence of inflammatory cell infiltrates. PMID: 15458434
  19. proteinase inhibitor 9 was effectively hydrolyzed and inactivated by human granzyme M, raising the possibility that this orphan granzyme bypasses proteinase inhibitor 9 inhibition of granzyme B PMID: 15494398
  20. Since PI-9 considerably alters GrzB and killer cell sensitivity, it may strongly influence the efficacy of GvL(graft-versus-leukemia) effects PMID: 15531453
  21. Over expression of SERPINB9 is associated with metastatic melanoma PMID: 16144945
  22. Soluble SERPINB9 circulates in blood and increases on primary Cytomegalovirus infection in post renal transplantation patients PMID: 16267761
  23. Estrogen induction of PI-9 may reduce the ability of cytolytic lymphocytes-mediated immune surveillance to destroy newly transformed cells PMID: 16306080
  24. up-regulated expression of PI-9 in gestational trophoblastic diseases contributes to disease pathogenesis via immune evasion PMID: 16310039
  25. loss of PI9 expression in tumor cells may reflect some mechanism associated with progression PMID: 17077322
  26. PI9 inhibited apoptotic death by directly interacting with the intermediate active forms of caspase-8 and -10. This indicates that PI9 can regulate pro-apoptotic apical caspases. PMID: 17479112
  27. The data suggest that PI-9 is tightly linked to maturation and may allow dendritic cells to exert their function in a potentially hostile environment. PMID: 18191723
  28. A significant population consumes levels of genistein in soy products that may be high enough to induce PI-9, perhaps potentiating the survival of some preexisting breast cancers by enabling them to evade immunosurveillance. PMID: 18669594

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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