Recombinant Human Dipeptidyl Peptidase 9 (DPP9) Protein (His)

Name: Recombinant Human Dipeptidyl Peptidase 9 (DPP9) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06288P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human Dipeptidyl Peptidase 9 (DPP9) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Activity	Not tested.
Uniprotkb	Q86TI2
Target Symbol	DPP9
Synonyms	(DP9)(Dipeptidyl peptidase IV-related protein 2)(DPRP-2)(Dipeptidyl peptidase IX)(DPP IX)(Dipeptidyl peptidase-like protein 9)(DPLP9)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	C-6His
Target Protein Sequence	LHKQPRFWASMMEAASCPPDYVPPEIFHFHTRSDVRLYGMIYKPHALQPGKKHPTVLFVYGGPQVQLVNNSFKGIKYLRLNTLASLGYAVVVIDGRGSCQRGLRFEGALKNQMGQVEIEDQVEGLQFVAEKYGFIDLSRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDTGYTERYMDVPENNQHGYEAGSVAL
Expression Range	585-788aa
Protein Length	Partial
Mol. Weight	29.7 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	Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. Acts as an inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis: inhibits pyroptosis by preventing activation of NLRP1 and CARD8 via an unknown mechanism.
Subcellular Location	[Isoform 1]: Cytoplasm, cytosol.; [Isoform 2]: Nucleus.
Protein Families	Peptidase S9B family, DPPIV subfamily
Database References	HGNC: 18648 OMIM: 608258 KEGG: hsa:91039 STRING: 9606.ENSP00000262960 UniGene: PMID: 27682012 DPP9 has a role in promoting tumorgenicity, metastasis and the prediction of poor prognosis in non-small cell lung cancer PMID: 27943262 The DPP9 expressing cell model system is a very useful and promising system for investigating the selectivity and associated toxicity of DPP4 inhibitors on DPP9. PMID: 25464020 There was a concomitant decrease in the phosphorylation of focal adhesion kinase and paxillin, indicating that DPP9 knockdown or enzyme inhibition suppressed the associated adhesion signaling pathway, causing impaired cell movement. PMID: 25486458 Whereas DPP9-short is present in the cytosol, DPP9-long localizes preferentially to the nucleus. PMID: 24562348 DPP9 was found in macrophages of carotid atherosclerotic plaque and may play a role in disease progression. PMID: 23608773 DPP9 binds to SUMO1 through a novel SUMO1 interacting motif. PMID: 23152501 residues important for dimer formation and enzymatic activity PMID: 22001206 These findings suggest an important signaling role of DPP9 in the regulation of survival and proliferation pathways. PMID: 21622624 This is the first study to demonstrate the presence of DP9 in chronic lymphocytic leukemia. PMID: 20534982 identification of two forms, their tissue distribution, cytoplasmic localization PMID: 15245913 cells overexpressing DP9 exhibit behavioral changesin the presence of ECM components; these effects were independent of enzyme activity PMID: 16700509 The DPP9 gene is not associated with the occurrence or curve severity of AIS. It is neither a disease-predisposition nor a disease-modifying gene of AIS. PMID: 18940951 results indicate that the biochemical property of DPP9 is very similar to that of DPP8, its homologous protease. DPP9 and DPP8 are likely redundant proteins carrying out overlapping functions in vivo PMID: 19268648 DPP9, a poorly characterized cytoplasmic prolyl-peptidase, is rate-limiting for destruction of proline-containing substrates both in cell extracts and in intact cells PMID: 19667070

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.