Recombinant Human Serpin B9 Protein (C-6His)

Name: Recombinant Human Serpin B9 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-0954NP
Availability: InStock

BL-0954NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Serine Protease Inhibitor-clade B9 is produced by our Mammalian expression system and the target gene encoding Met1-Pro376 is expressed with a 6His tag at the C-terminus.
Accession	P50453
Synonym	Cytoplasmic antiproteinase 3;Peptidase inhibitor 9;CAP3;PI-9;Serpin B9
Gene Background	Serpin B9, also known as Cytoplasmic antiproteinase 3(CAP-3), is a cytoplasm protein which belongs to the large superfamily of serine proteinase inhibitors (serpins), which bind to and inactivate serine proteinases. Serpin B9 is an inhibitor of the granzyme B/perforin lytic pathway. It is expressed in normal mammary epithelial cells but not in most mammary carcinoma cell lines. These interactions are involved in many cellular processes, including coagulation, fibrinolysis, complement fixation, matrix remodeling, and apoptosis. Serpin-B9 expression in immune-privileged cells, APCs, and CTLs protects these cells against the actions of granzyme B, and when expressed in tumor cells or virally infected hepatocytes, confers resistance to killing by CTL and NK cells. Expression of increasing levels of Serpin-B9 in target cells may progressively inhibit immune surveillance by blocking NK and CTL-induced cytotoxicity through the perforin / granzyme pathway and then through the Fas / FasL pathway.
Molecular Mass	43.4 KDa
Apmol Mass	35-40 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Granzyme B inhibitor.
Subcellular Location	Cytoplasm.
Protein Families	Serpin family, Ov-serpin subfamily
Database References	HGNC: 8955 OMIM: 601799 KEGG: hsa:5272 STRING: 9606.ENSP00000370074 UniGene: PMID: 26992230 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 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 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 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 Increased intracellular PI-9 activity in mononuclear phagocytes from HIV-infected patients contributes to successful intracellular infection by virulent Mycobacterium tuberculosis. PMID: 24445365 The GrB-Sb9 nexus may therefore represent an additional mechanism of limiting lymphocyte lifespan and populations. PMID: 24488096 Suppression of granzyme B initiated apoptosis in protease inhibitor-9-expressing leukemia cells. PMID: 23892923 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 lung cancer cells utilise their increased PI-9 expression to protect from granzyme B-mediated cytotoxicity as an immune evasion mechanism PMID: 22387007 Inhibition of Granzyme B by PI-9 protects prostate cancer cells from apoptosis. PMID: 21919028 Reduced proteinase inhibitor 9 expression in human vascular smooth muscle cells is associated with atherosclerotic disease progression. PMID: 21296596 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 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 upregulated expression of PI-9 in NSCLC cells may serve to protect them from apoptosis induced by GrB PMID: 19956856 Expression levels of apoptosis-related proteins caspase 3, Bcl-2, and PI9 predict clinical outcome in anaplastic large cell lymphoma. PMID: 12036886 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 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 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 Since PI-9 considerably alters GrzB and killer cell sensitivity, it may strongly influence the efficacy of GvL(graft-versus-leukemia) effects PMID: 15531453 Over expression of SERPINB9 is associated with metastatic melanoma PMID: 16144945 Soluble SERPINB9 circulates in blood and increases on primary Cytomegalovirus infection in post renal transplantation patients PMID: 16267761 Estrogen induction of PI-9 may reduce the ability of cytolytic lymphocytes-mediated immune surveillance to destroy newly transformed cells PMID: 16306080 up-regulated expression of PI-9 in gestational trophoblastic diseases contributes to disease pathogenesis via immune evasion PMID: 16310039 loss of PI9 expression in tumor cells may reflect some mechanism associated with progression PMID: 17077322 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 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 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

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.