Recombinant Human Serpin B1 Protein (C-6His)

Name: Recombinant Human Serpin B1 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-0937NP
Availability: InStock

BL-0937NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Serine Protease Inhibitor-clade B1 is produced by our Mammalian expression system and the target gene encoding Met1-Pro379 is expressed with a 6His tag at the C-terminus.
Accession	P30740
Synonym	Leukocyte elastase inhibitor;SERPINB1; Monocyte/neutrophil elastase inhibitor; M/NEI; Peptidase inhibitor 2; PI-2
Gene Background	SERPINB1 is a member of the serpin family and Ov-serpin subfamily. As protease inhibitors, serpins have an array of functions including regulating blood coagulation, fibrinolysis, the complement pathway, angiogenesis, inflammation, tumor suppression, extracellular matrix remodeling, and cell motility. SERPINB1 regulates the activity of the neutrophil proteases elastase, cathepsin G, proteinase-3, chymase, chymotrypsin, and kallikrein-3. Reactive bond 1 of SerpinB1 is specific for reaction with chymotrypsin-like protease such as cathepsin G, chymotrypsin or chymase. Reactive bond 2 of SerpinB1 is specific for reaction with elastase-like protease such as neutrophyl elastase, proteinase-3, pancreatic elastase or PSA. In addition, SERPINB1 also functions as a potent intracellular inhibitor of granzyme H.
Molecular Mass	43.8 KDa
Apmol Mass	40-56 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	Neutrophil serine protease inhibitor that plays an essential role in the regulation of the innate immune response, inflammation and cellular homeostasis. Acts primarily to protect the cell from proteases released in the cytoplasm during stress or infection. These proteases are important in killing microbes but when released from granules, these potent enzymes also destroy host proteins and contribute to mortality. Regulates the activity of the neutrophil proteases elastase, cathepsin G, proteinase-3, chymase, chymotrypsin, and kallikrein-3. Acts also as a potent intracellular inhibitor of GZMH by directly blocking its proteolytic activity. During inflammation, limits the activity of inflammatory caspases CASP1, CASP4 and CASP5 by suppressing their caspase-recruitment domain (CARD) oligomerization and enzymatic activation. When secreted, promotes the proliferation of beta-cells via its protease inhibitory function.
Subcellular Location	Secreted. Cytoplasm. Cytolytic granule. Early endosome.
Protein Families	Serpin family, Ov-serpin subfamily
Database References	HGNC: 3311 OMIM: 130135 KEGG: hsa:1992 STRING: 9606.ENSP00000370115 UniGene: Hs.381167
Tissue Specificity	In human bone marrow, present in all CD45+ populations. Expression levels are highest in the neutrophil lineage, intermediate in monocytic, and lowest in lymphocytic lineage. Within the neutrophil lineage, expression is highest in promyelocytes.

Gene Functions References

The expression of SERPINB1 was approximately 2-fold higher in apical periodontitis. SERPINB1 expression was noted in neutrophils and epithelial cells. PMID: 28673495
SERPINB1 decreased inflammation, ameliorated oxidative stress in the lung, and attenuated acute lung injury in rats with orthotopic autologous liver transplantation by activating HO-1 and it does so through STAT3 PMID: 28427999
a relatively low Serpinb1a protein threshold in neutrophils that is required for sustained survival PMID: 27107834
SERPINB1 expression is significantly upregulated in human masticatory mucosa during wound healing PMID: 28005267
Data show that high serpin B1 protein (SERPINB1) gene expression was associated with favorable tumor response and prolonged survival under cisplatin-based chemotherapy. PMID: 26799424
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
is not expressed in neutrophils of both sulfur mustard-exposed and chronic obstructive pulmonary disease patients PMID: 24852194
Data suggest that serine protease inhibitor (SERPIN) B1 negatively regulates glioma cell migration and invasion probably by abrogating the expression of matrix metalloproteinase-2 and the activation of focal adhesion kinase. PMID: 24968089
Decreased expression of SERPINB1 correlates with tumor invasion and poor prognosis in hepatocellular carcinoma. PMID: 24105272
Apoptosis-inducing factor and leukocyte elastase inhibitor derived DNase II interact and can cooperate to induce cell death. PMID: 23673989
Upon reactive center loop cleavage at Phe-343,SERPINB1 covalently complexes with GzmH. SERPINB1 overexpression suppresses GzmH- or LAK cell-mediated cytotoxicity. Crystal structures show possible conformational changes in GzmH for the suicide inhibition. PMID: 23269243
In the resting state during human neutrophil extracellar trap generation, SerpinB1 is exclusively in the cytoplasm, consistent with the current understanding of clade B serpins, and it may migrate and regulate events in the cell nucleus. PMID: 23002442
These results suggest that serpin B1 may be a novel marker of active ulcerative colitis and may play an important role in the pathogenesis of inflammatory bowel disease. PMID: 22421620
serpinB1 sustains a healthy neutrophil reserve that is required in acute immune responses. PMID: 21248149
The findings define an innate role for SerpinB1 in cystic fibrosis airways. PMID: 20817705
M/NEI is a dual specificity inhibitor with two adjacent reactive sites that support rapid efficient inhibitory reactions with cellular proteases, including the three neutrophil granule proteases. PMID: 11747453

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.