Recombinant Human Trypsin-2 (PRSS2) Protein (His-SUMO)

Name: Recombinant Human Trypsin-2 (PRSS2) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-07759P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins, Recombinant proteins fall special offers - full-length proteins

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Product Overview

Description	Recombinant Human Trypsin-2 (PRSS2) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P07478
Target Symbol	PRSS2
Synonyms	Anionic trypsinogen;Serine protease 2;Trypsin II
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	IVGGYICEENSVPYQVSLNSGYHFCGGSLISEQWVVSAGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPKYNSRTLDNDILLIKLSSPAVINSRVSAISLPTAPPAAGTESLISGWGNTLSSGADYPDELQCLDAPVLSQAECEASYPGKITNNMFCVGFLEGGKDSCQGDSGGPVVSNGELQGIVSWGYGCAQKNRPGVYTKVYNYVDWIKDTIAANS
Expression Range	24-247aa
Protein Length	Full Length of Mature Protein
Mol. Weight	37.0 kDa
Research Area	Cell Biology
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	In the ileum, may be involved in defensin processing, including DEFA5.
Subcellular Location	Secreted, extracellular space.
Protein Families	Peptidase S1 family
Database References	HGNC: 9483 OMIM: 601564 KEGG: hsa:5645 UniGene: PMID: 26110235 PRSS2 single nucleotide polymorphism associated with the development of alcoholic pancreatitis. PMID: 25253127 Serum trypsinogen-2 is associated with pancreatic cancer and pancreatitis. PMID: 25916077 trypsin-2 over-expression enhanced tongue carcinoma cell invasion by various genetic and proteolytic mechanisms. PMID: 22909050 Elevation of urine trypsinogen 2 is an independent risk factor for pancreatic fistula after pancreaticoduodenectomy. PMID: 22357509 Report a simple, rapid, easy, and noninvasive urinary trypsinogen-2 test can diagnose or rule out most cases of acute pancreatitis. PMID: 22481290 Data show that urinary trypsinogen-2 dipstick test is a useful test for early diagnosis of post-endoscopic retrograde cholangiopancreatography (ERCP) pancreatitis. PMID: 21946810 results suggest that trypsinogen-2 is a more sensitive marker than amylase, and it can be useful in early diagnosis of post-endoscopic retrograde cholangiopancreatography (ERCP) pancreatitis. PMID: 21792081 A genetic variant of PRSS2 may contribute to the low prevalence of pancreatitis in primary hyperparathyroidism patients. PMID: 20625975 Hyperexpression of the PRSS2 gene is associated with pancreatic cancer. PMID: 20428826 there was a borderline statistically significant association between pancreatic cancer and HAT/HCT but no association between pancreatic cancer and HAT, HCT. PMID: 20484960 Urine trypsinogen-2 test may be an important diagnostic tool in excluding the diagnosis of acute pancreatitis; it has a negative predictive value. PMID: 20517765 Results do not support the urinary trypsinogen-2 dipstick test (UTDT) to replace standard plasma amylase for the diagnosis of AP, however, the test demonstrated an adequate sensitivity to be used for rapid early screening of AP in daily clinics. PMID: 19752771 Results indicate that up-regulation of anionic trypsinogen in pancreatic diseases does not affect physiological trypsinogen activation, but significantly limits trypsin generation under potential pathological conditions. PMID: 12709065 High levels of pulmonary trypsin-2 may be associated with the development of bronchopulmonary dysplasia in preterm infants. PMID: 12949286 G191R variant of PRSS2 mitigates intrapancreatic trypsin activity and thereby protects against chronic pancreatitis PMID: 16699518 Our results suggest that serum trypsinogen-2 is a most useful marker for diagnosing patients with cholangiocarcinoma, and it is superior to serum CA19-9 and CEA. PMID: 17640760 Co-localization of trypsin-2 and MMP-9 resulted in intracellular proMMP-9 processing that represented fully or partially activated MMP-9. PMID: 18062964 A loss of function polymorphism (G191R) of anionic trypsinogen (PRSS2) confers protection against chronic pancreatitis. PMID: 18362849 A fusion with PRSS1 is associated with hereditary pancreatitis. PMID: 18461367 primary role of trypsinogen sulfation in humans is to stimulate autoactivation of PRSS1 PMID: 18986305 The p.G191R variant protected against alcoholic and idiopathic chronic pancreatitis as well as alcoholic acute pancreatitis in Japan. PMID: 19052022 G191R PRSS2 is a rare allele in the Indian population and the data suggest a nonsignificant trend towards a protective effect from tropical calcific pancreatitis in Indians. PMID: 19077465

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.