Recombinant Human Leukocyte Elastase Inhibitor (SERPINB1) Protein (His-SUMO)

Name: Recombinant Human Leukocyte Elastase Inhibitor (SERPINB1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09883P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Leukocyte Elastase Inhibitor (SERPINB1) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P30740
Target Symbol	SERPINB1
Synonyms	Anti elastase ; EI; ELANH2 ; Epididymis luminal protein 57; HEL57; ILEU_HUMAN; LEI; Leukocyte elastase inhibitor; M/NEI; MNEI ; Monocyte/neutrophil elastase inhibitor; Peptidase inhibitor 2; Pi-2; PI2 ; Serine (or cysteine) proteinase inhibitor clade B (ovalbumin) member 1; Serpin B1; Serpin peptidase inhibitor clade B (ovalbumin) member 1; serpinb1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MEQLSSANTRFALDLFLALSENNPAGNIFISPFSISSAMAMVFLGTRGNTAAQLSKTFHFNTVEEVHSRFQSLNADINKRGASYILKLANRLYGEKTYNFLPEFLVSTQKTYGADLASVDFQHASEDARKTINQWVKGQTEGKIPELLASGMVDNMTKLVLVNAIYFKGNWKDKFMKEATTNAPFRLNKKDRKTVKMMYQKKKFAYGYIEDLKCRVLELPYQGEELSMVILLPDDIEDESTGLKKIEEQLTLEKLHEWTKPENLDFIEVNVSLPRFKLEESYTLNSDLARLGVQDLFNSSKADLSGMSGARDIFISKIVHKSFVEVNEEGTEAAAATAGIATFCMLMPEENFTADHPFLFFIRHNSSGSILFLGRFSSP
Expression Range	1-379aa
Protein Length	Full Length
Mol. Weight	58.7kDa
Research Area	Cardiovascular
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	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.