Recombinant Rat Dipeptidyl Peptidase 4 (DPP4) Protein (His-SUMO)

Name: Recombinant Rat Dipeptidyl Peptidase 4 (DPP4) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-04031P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Rat Dipeptidyl Peptidase 4 (DPP4) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P14740
Target Symbol	DPP4
Synonyms	Dpp4; Cd26; Dipeptidyl peptidase 4; Bile canaliculus domain-specific membrane glycoprotein; Dipeptidyl peptidase IV; DPP IV; GP110 glycoprotein; T-cell activation antigen CD26; CD antigen CD26
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	SMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQISKALVDAGVDFQAMWYTDEDHGIASSTAHQHIYSHMSHFLQQCFSLR
Expression Range	638-767aa
Protein Length	Partial
Mol. Weight	30.7kDa
Research Area	Immunology
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	Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
Subcellular Location	[Dipeptidyl peptidase 4 soluble form]: Secreted.; Cell membrane; Single-pass type II membrane protein. Apical cell membrane; Single-pass type II membrane protein. Cell projection, invadopodium membrane; Single-pass type II membrane protein. Cell projection, lamellipodium membrane; Single-pass type II membrane protein. Cell junction. Membrane raft.
Protein Families	Peptidase S9B family, DPPIV subfamily
Database References	KEGG: rno:25253 STRING: 10116.ENSRNOP00000045536 UniGene: PMID: 29677638 Proteome profile array screening further revealed that DPPIV decreases matrix metalloproteinase-9, a key downstream effector of ERK-AKT signaling pathways PMID: 27525674 results suggest that long-term exposure to DPPIV inhibitors looks compatible with an overall balanced metabolism PMID: 28895067 Bis-Pyrano Prenyl Isoflavone Improves Glucose Homeostasis by Inhibiting Dipeptidyl Peptidase-4 in Hyperglycemic Rats PMID: 27238050 The study demonstrates that the DPP4 inhibitor has a neuroprotective effect against hyperthermia-induced seizures by reducing the astrocyte-mediated inflammatory response by an NF-kappaB-dependent pathway. These properties are of significant clinical value and help explain the increasing evidence that DPP4 is involved in the incidence and progression of febrile seizures. PMID: 28372289 DPP-4 inhibition with linagliptin may represent a novel treatment for chronic kidney disease. PMID: 27083282 DPP4 inhibition protects against ventricular arrhythmias by attenuating NGF-induced sympathetic innervation via cAMP/PKA/CREB-dependent antioxidant pathway in non-diabetic infarcted rats. PMID: 26399925 Dipeptidyl peptidase-4 inhibition by gemigliptin exerts a preventative effect on the proliferation and migration of VSMCs via Nrf2. PMID: 26187356 Differences in Expression of DPP4 in Steatotic Rat Liver Are Not Related to Differences in the Methylation of its Gene Promoter PMID: 26359413 The inhibition of the renal DPP-4 activity induced by saxagliptin may contribute to ameliorating renal injury in hypertension-related renal injury. PMID: 25936515 Inhibition of DPP-4 reduces T2DM-induced increase in post-MI acute mortality possibly by restoring the autophagic response through attenuation of Bcl-2-Beclin-1 interaction. PMID: 26259714 DPP4 inhibitor vildagliptin attenuates oxidative stress and cardiac fibrosis and improving cardiac function in rats with chronic myocardial infarction. PMID: 25823534 Findings indicate a positive correlation between reduced stress-responsiveness and increased central NPY, in DPP4mut rats. PMID: 25635612 DPP-4 inhibitors reduced macrophage infiltration via glucagon-like peptide-1-dependent signaling in nephritis model and suggest that the control of inflammation by DPP-4 inhibitors is useful for the treatment of nondiabetic kidney disease models. PMID: 25656369 bone marrow derived cells but not the kidney represent at least one source of sDPP4. And leukocyte or macrophage subpopulations could be potential candidates. PMID: 24874705 DPP4 regulates the expression of the hemoglobin genes, and might play a role in the preservation of renal function. PMID: 25122001 Maternal deprivation as a model for postnatal stress experience influences remarkably postnatal lung development of rats, which is significantly modulated by the DPP4-system. PMID: 24357522 Long term deficiency of DPP4 activity improved cardiac performance against pressure overload in rat. PMID: 24416433 a low level of DPPIV activity contributed to maintaining intestinal homeostasis PMID: 23832365 Circulating DPPIV activity is associated with poorer cardiovascular outcomes in heart failure. PMID: 23894014 High fat and high cholesterol diets increased DPP-IV expression in intestinal lymph. PMID: 23535306 DPP-IV is a promising in situ marker of biliary functionality not only of normal but also of fatty rats. PMID: 23361237 Long term loss of DPP4 activity increased the capability against ROS stress, which was more than GLP-1 dependent pathway PMID: 23359639 DPP-4 deficiency restored ischemia (but not G-CSF)-induced stem cell mobilization and improved vascular recovery in diabetic animals PMID: 23184393 These data suggest that GLP-1 analogs may serve as a novel therapeutic drug to alleviate obesity-induced liver injury by reducing bile acid synthesis and improving liver bile secretory function. PMID: 22918684 Dipeptidyl peptidase IV regulates proliferation of preglomerular vascular smooth muscle and mesangial cells. PMID: 22802229 novel evidence shows the regulatory roles of DPP4 in chronic heart failure. PMID: 23035207 Seven days post artery occlusion, dipeptidyl peptidase IV immunoreactivity was found in the perikarya of surviving cortical neurons of the ipsilateral hemisphere. PMID: 22373413 APN and DPPIV activity levels are related to the development of arthritis, being protective or inducer of the susceptibility PMID: 21982785 This study demonstrates a reduction of anabolic effects on the energy homeostasis and a centrally enhanced NPY-expression in DPP4-deficient rats under high caloric food intake. DPP4-deficiency altered intracorporal fat distribution. PMID: 20887754 plasma DPP4 activity changes in accordance with the progression of hyperinsulinemic obesity and pancreatic islet atrophy PMID: 21139073 Monosodium glutamate and/or food deprivation decreased the activity of dipeptidyl peptidase 4 in the soluble and membrane fraction from the hypothalamus, and in the membrane fraction from the hippocampus. PMID: 20153005 Reduced airway inflammation in CD26-deficient F344 rats appear to be mediated by differences in the recruitment and activity of Tregs. PMID: 20560982 APM and DPPIV-DI are respectively related to the downregulation of somatostatin in food-deprived rats, and to the recovery of energy balance in monosodium glutamate obese rats during food deprivation PMID: 19876009 These findings demonstrate a negative regulatory role of the bronchus-associated lymphatic tissue -specific expression of CD26 in T-cell adhesion during an asthma-like inflammation. PMID: 19501934 The 6A3 epitope was stably exposed in both native and denatured rDPP IV. Data mapped the 6A3 epitope to a surface-exposed Thr331-dependent motif D329KTTLVWN, only 11 amino acids away from L311QWLRRI on the same plane as the fifth beta-propeller blade. PMID: 19804410 Immunoreactive endomorphin 2 was generated extracellularly by a membrane-bound DPP-IV, which was switched to "synthase" mode by the hydrolase inhibitor Ile-Pro-Ile PMID: 19540879 Clustered charged amino acids of human adenosine deaminase comprise a functional epitope for binding the adenosine deaminase complexing protein CD26/dipeptidyl peptidase IV. PMID: 11901152 DPPIV deficiency results in improved glucose tolerance and ameliorated insulin resistance PMID: 12031691 kinetics of this enzyme and insights into its dimerization and gelatinase activity PMID: 12675219 An increase in this enzyme is associated with graft rejection. Inhibition of this enzyme prevents heart graft rejection. PMID: 12675233 The three-dimensional structure of DPPIV as determined by cryo-TEM and single particle analysis. PMID: 12705886 identification of DPPIV-binding sites in fibronectin and the effect of binding site peptides on DPPIV/poly-fibronectin adhesion and metastasis PMID: 12716896 The behavioral repertoire and response to ethanol was characterized in dipeptidyl peptidase IV (DPPIV/CD26)-deficient, mutant Japanese, German, and wild-type-like F344 rat substrains. PMID: 14568317 presence of a yet to be characterized signalling mechanism whereby DPP IV has access to c-Src-containing signalling platforms PMID: 16478473 short-term DP IV inhibition does not eliminate the satiety actions of exogenously administered peptide YY at the doses tested. PMID: 16802131 results extend earlier findings and illustrate the role of CD26/DPP IV in alloantigen-mediated immune responses PMID: 16962474 The X-ray structure confirms that the binding mode of rat DPPIV is similar to the parent xanthines. PMID: 17010607 Inhibition of intragraft DPP IV activity significantly reduced ischemia/reperfusion-associated pulmonary injury, allowing for successful transplantation after 18 hours of ischemia. PMID: 17175274 Rats with a high fat diet significantly increased DPP-IV's expression and activity about 142-152% in the intestine and 153-240% in kidneys, but there was no change in the liver. PMID: 17583752

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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.

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