Recombinant Human Trypsin-1 (PRSS1) Protein (His)

Name: Recombinant Human Trypsin-1 (PRSS1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06485P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Trypsin-1 (PRSS1) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P07477
Target Symbol	PRSS1
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	C-6His
Target Protein Sequence	IVGGYNCEENSVPYQVSLNSGYHFCGGSLINEQWVVSAGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPQYDRKTLNNDIMLIKLSSRAVINARVSTISLPTAPPATGTKCLISGWGNTASSGADYPDELQCLDAPVLSQAKCEASYPGKITSNMFCVGFLEGGKDSCQGDSGGPVVCNGQLQGVVSWGDGCAQKNKPGVYTKVYNYVKWIKNTIAANS
Expression Range	24-247aa
Protein Length	Full Length of Mature Protein
Mol. Weight	25.6 kDa
Research Area	Metabolism
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	Has activity against the synthetic substrates Boc-Phe-Ser-Arg-Mec, Boc-Leu-Thr-Arg-Mec, Boc-Gln-Ala-Arg-Mec and Boc-Val-Pro-Arg-Mec. The single-chain form is more active than the two-chain form against all of these substrates.
Subcellular Location	Secreted, extracellular space.
Protein Families	Peptidase S1 family
Database References	HGNC: 9475 OMIM: 167800 KEGG: hsa:5644 STRING: 9606.ENSP00000308720 UniGene: PMID: 29870887 report here for the first time a family from India that is positive for R122H mutation in the PRSS1 gene PMID: 29476405 Studied mutations in cationic trypsinogen (PRSS1) and serine protease inhibitor Kazal type 1 (SPINK1) and their association with alcoholic chronic pancreatitis (ACP) and idiopathic chronic pancreatitis. PMID: 29641165 Data indicate association between polymorphism rs10273639 of the PRSS1-PRSS2 locus and pancreatitis development. PMID: 27846138 SNP in the PRSS1-PRSS2-rs10273639 is associated with Chronic pancreatitis. PMID: 28913878 Gene mutations were present in PRSS1 in 26 patients with acute recurrent and chronic pancreatitis, SPINK1 in 23, CTRC in 3, and CPA1 in 5. In the 31 patients with mutations in SPINK1, CTRC, or CPA1, 16 (51.6%) had homozygous or heterozygous mutations with other mutations. PMID: 27409067 Results identified 3 new rare variants in the proximal promoter region of PRSS1 which along the known c.-30_-28delTCC do not seem to be a risk factors for chronic pancreatitis. PMID: 27432637 Early-onset pancreatitis is associated strongly with PRSS1 or CTRC mutations and family history of pancreatitis. PMID: 28502372 PRSS1 variant p.L104P exhibits a variety of phenotypic changes that can increase risk for chronic pancreatitis. Mutation-induced misfolding and associated ER stress are the dominant effects that support a direct pathogenic role in chronic pancreatitis. PMID: 26822915 Mutations in CFTR, SPINK1 or PRSS1 are present in one third of pediatric acute recurrent (ARP) or chronic (CP) pancreatitis with no other cause. PMID: 26692446 Three types of pathogenic PRSS1 variants was identified in 11 patients, including p.N29I (n=1), p.R122H (n=1), and p.G208A (n=9). PMID: 27578509 Mutations were found at the promoter and exon 3 of the PRSS1 in patients with pancreatic cancer. That is, five patients had c.410 C > T mutation causing p.Thr 137 Met, and three patients had c. -338 T >G mutation at the promoter of the PRSS1. In patients with PRSS1 mutations, serum trypsin was significantly higher than that in normal controls PMID: 26546433 These findings suggest that IL-1beta plays a key role in trypsin upregulation and has a pathological role in multiple organ failure in influenza virus infection. PMID: 27714503 Human anionic trypsinogen is controlled by CTRC in a manner that individual natural mutations are unlikely to increase stability enough to promote intra-pancreatic activation. PMID: 27129265 Association of PRSS1 polymorphism with idiopathic recurrent acute pancreatitis and idiopathic chronic pancreatitis. PMID: 26110235 Letter/Case Report: high penetrance of the PRSS1 A16V mutation caused by SPINK1 N34S and CFTR TG11-5T co-mutations associated with pancreatitis. PMID: 26658045 We did not find PRSS1 mutation in any patient. PMID: 25981744 In Israel, pediatric as well as adult recurrent acute pancreatitis and chronic pancreatitis are often associated with PRSS1, serine protease inhibitor Kazal type 1, chymotrypsin C, or Cystic Fibrosis Transmembrane Conductance Regulator mutations. PMID: 25383785 This study shows that PRSS1, SPINK1 and CFTR mutations do not play a role in alcoholic and idiopathic chronic pancreatitis patients. PMID: 25835118 N29T mutation associated with pancreatitis PMID: 26376395 Recombination events between members of the trypsinogen family can generate high-risk PRSS1 alleles. PMID: 25546417 the observations demonstrate that the tyrosyl sulfate in human trypsins interacts with the P2' position of the substrate-like inhibitor and this modification increases P2' selectivity towards basic side chains. PMID: 25010489 PRSS1 single nucleotide polymorphism is associated with alcoholic pancreatitis. PMID: 25253127 PRSS1 variants are associated with less disease relapse in autoimmune pancreatitis. PMID: 24909264 Two novel PRSS1 mutations were identified in Mexican patients with early onset idiopathic recurrent acute pancreatitis. PMID: 25206283 The -409 T/T genotype of PRSS1 gene was revealed to be a marker for predicting neotal sepsis, along with serum trypsin levels. PMID: 24777884 None of the selected 121 pancreatic cancer samples showed a pancreatitis-predisposing mutation in the PRSS1 gene. PMID: 25003218 expression of WT or mutant human PRSS1 in murine acinar cells induces apoptosis and is sufficient to promote spontaneous pancreatitis. PMID: 24722290 Using the optimal cutoffs, the sensitivity of the IRT/PAP strategy would not be inferior to that of IRT/DNA if identification of mild forms is not required. PMID: 24513262 PRSS1: IVS 2 +56_60 del CCCAG is a noval mutant which may contribute to AIP pathogenesis. PMID: 24236450 The p.G208A variant of PRSS1, previously only found in Asian patients, was found in 3 generations of a European family, one of whom had chronic pancreatitis. PMID: 24413785 the p.N43S mutation in the SPINK1 gene, accelerated the onset of HP in the presence of the p.R122H mutation in the CT gene. PMID: 24134754 Rare causative PRSS1 mutations account for 9.1% of the idiopathic chronic pancreatitis study group in 253 young French patients. PMID: 23951356 The trypsinogen to trypsin conformational switch modulates cleavage susceptibility of nick sites by altering both the thermodynamics and kinetics of cleavage to protect human cationic trypsin from premature degradation. PMID: 24403079 PRSS1 hereditary pancreatitis is characterized by progressive lipomatous atrophy of the pancreas. PMID: 24525505 No association of PRSS1 with pancreatic cancer is found. PMID: 23751316 D21A polymorphism in the PRSS1 gene seems to be a risk factor for hereditary chronic pancreatitis. PMID: 23864476 PRSS1 gene was significantly associated with total pancreatitis disease, both totally and separately PMID: 23801884 For pediatric ulcerative colitis patients who require surgery, the immunopositivity of Tryp-1 at diagnosis is lower when compared to that of patients with a more benign disease course. PMID: 23745029 Autoimmune pancreatitis may be related to PRSS1 gene mutations. PMID: 23745036 Trypsin-1 and trypsin-2 appear to have a function in the degradation of vitreous type II collagen. PMID: 23882137 A kindred from Venezuela, South America with the PRSS1 R122H variant. PMID: 23474566 Even in the absence of chymotrypsin C, trypsinogen activation peptide mutants autoactivated at markedly increased rates. PMID: 23601753 Case Report: suggest involvement of PRSS1 mutations in familial solid pseudopapillary pancreatic tumors. PMID: 22722260 Frequencies of CFTR variants p.R75Q, p.I148T, 5T-allele and p.E528E were comparable in patients and controls. We identified 103 CFTR variants, which represents a 2.7-fold risk increase (p<0.0001). PMID: 22427236 Two associations with alcoholic pancreatitis at genome-wide significance were identified and replicated at PRSS1-PRSS2 and X-linked CLDN2 through a two-stage genome-wide study. PMID: 23143602 Data show that among the 2 mutations in the PRSS1 gene, only the N29I mutation was found in 1 (1.7%) of 58 patients with AP, in the heterozygous state. PMID: 22699143 hereditary pancreatitis is caused by CTRC-dependent dysregulation of cationic trypsinogen autoactivation, which results in elevated trypsin levels in the pancreas. PMID: 22539344 All of the heterozygote patients with a combination of CFTR and SPINK1 or PRSS1 mutations had chronic pancreatitis. PMID: 22094894 Mutations of PRSS1 gene may be an important factor of pancreatic cancer. PMID: 22088471

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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.