Recombinant Human Islet Amyloid Polypeptide Protein (IAPP) Protein (GST)

Name: Recombinant Human Islet Amyloid Polypeptide Protein (IAPP) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-02268P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human Islet Amyloid Polypeptide Protein (IAPP) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P10997
Target Symbol	IAPP
Synonyms	Amylin; DAP; Diabetes associated peptide; Diabetes-associated peptide; IAP; IAPP; IAPP_HUMAN; Insulinoma amyloid peptide; Islet amyloid polypeptide (diabetes associated peptide, amylin); Islet amyloid polypeptide
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY
Expression Range	34-70aa
Protein Length	partial
Mol. Weight	31.4kDa
Research Area	Signal Transduction
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	Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.
Subcellular Location	Secreted.
Protein Families	Calcitonin family
Database References	HGNC: 5329 OMIM: 147940 KEGG: hsa:3375 STRING: 9606.ENSP00000240652 UniGene: PMID: 30014749 These findings suggest that increased membrane permeation induced by oligomeratization of amylin peptide in cell sarcolemma contributes to Ca(2+) dysregulation in pre-diabetes. PMID: 29604965 down-regulation of IAPP expression induces the death of human annulus fibrosus cells via mitochondrial and death receptor pathways, potentially offering a novel therapeutic target for the treatment of intervertebral disc degeneration. PMID: 28433710 This study highlights that with positional scanning of the split-tetracysteine motif (Cys-Cys), the fluorogenic probe fluorescein arsenical hairpin detection method offers unique time-dependent conformational insights on the proteospecies assembled throughout the amyloidogenic pathway of IAPP. PMID: 29360346 Bri2 BRICHOS domain is a potent inhibitor of IAPP fibril formation.IAPP colocalizes with Bri2 both intracellularly and in islet amyloid deposits. PMID: 29507232 Insulin resistance in rheumatoid arthritis does not appear to be mediated by amylin. This would imply that the mechanisms associated with IR in RA patients differ from those at work in type 2 diabetes. PMID: 29352842 During aggregation, the nucleating NFGAIL region remains flexible and accessible within this isolated intermediate, suggesting a mechanism by which membrane-associated aggregation may be propagated. PMID: 29148426 Study presents a new Zn(2+) binding site in the N-terminus of fibrillary amylin with three different coordination modes. Simulations showed that Zn(2+) ions bind to polymorphic amylin fibrils with a preference to bind to four Cys residues rather than two Cys residues of two neighboring amylin monomers. PMID: 28692245 The IAPP beta-hairpin can serve as a molecular recognition motif enabling control of IAPP aggregation. PMID: 27641459 cholesterol significantly modulates the ability of model membranes to induce IAPP amyloid formation and IAPP-mediated membrane damage. PMID: 29373018 point mutations within the central aggregation-prone regions contribute to the reduction of the overall amyloidogenic potential of IAPP but do not completely abolish the formation of IAPP amyloid fibrils. PMID: 28602716 Using the Tg2576 AD mouse model, a single intraperitoneal injection of amylin significantly increased Abeta serum levels, and the effect was abolished by AC253, an amylin receptor antagonist, suggesting that amylin effect could be mediated by its receptor. Subsequent mechanistic studies showed amylin enhanced Abeta transport across a cell-based model of the blood-brain barrier. PMID: 28059785 These results suggest that protein segment structures represent polymorphs of their parent protein and that segment 19-29 S20G may serve as a model for the toxic spine of human IAPP. PMID: 28045370 All-atom explicit-water molecular dynamics (MD) simulations studying adsorption, orientation, and surface interaction of hIAPP aggregates with different sizes (monomer to tetramer) and conformations (monomer with alpha-helix and tetramer with beta-sheet-rich U-turn) upon adsorption. hIAPP monomer with alpha-helical conformation and hIAPP pentamer with beta-sheet conformation can adsorb on both POPC and POPC/POPE bilayers. PMID: 28585804 The aggregation of rhIAPP also occurred significantly faster when compared with that of the chemically synthesized peptide. PMID: 29046394 Data (including data from studies using tissues from transgenic mice) suggest that IL1B plays dual roles by (1) mediating islet amyloid-induced FAS up-regulation and apoptosis in pancreatic beta-cells and (2) down-regulating IAPP precursor processing thereby potentiating islet amyloid formation. (IL1B = interleukin-1beta; FAS = FAS cell surface death receptor; IAPP = islet amyloid polypeptide) PMID: 28058779 Data suggest that single aromatic/hydrophobic amino acid residues within IAPP (islet amyloid polypeptide) amyloid core region are able to control its interaction with amyloid-beta(1-40) or amyloid-beta(1-42) but not IAPP self-assembly; four aromatic/hydrophobic residues are able to control both IAPP amyloid self-assembly and its cross-interaction with amyloid-beta(1-40) or amyloid-beta(1-42). PMID: 28684415 Data show that aluminum (Al3+) could inhibit islet amyloid polypeptide hIAPP(11-28) fibrillogenesis. PMID: 28338927 The absence of BACE2 ameliorates glucose tolerance defects induced by IAPP overexpression in the beta-cell and promotes beta-cell survival. PMID: 28337562 This study supports the elucidation of the structural basis of IAPP amyloid formation and highlights the extent of amyloid fibril polymorphism. PMID: 27607147 Data suggest that a single GlcNAc residue at CTR N130 (asparagine 130) is responsible for enhanced affinity of calcitonin for CTR ECD; the same appears to apply for enhanced affinity of amylin for RAMP2-CTR ECD. [GlcNAc = N-acetylglucosamine; CTR = calcitonin receptor; ECD = extracellular domain; RAMP2 = receptor (calcitonin) activity modifying protein 2]. PMID: 28614667 The kinetics of human amylin amyloid formation can be monitored by SYPRO-orange fluorescence and match the time course determined with thioflavin-T assays. PMID: 27479186 effect of cholesterol on the amyloidogenicity of IAPP PMID: 27410742 Together, our preclinical results suggest that AT406 could be further evaluated as a promising anti-pancreatic cancer agent. PMID: 27387230 Al(III) could promote fibrillation and aggregation of hIAPP, while EGCG could inhibit the fibrillation of hIAPP and lead to the formation of hIAPP amorphous aggregates instead of the ordered fibrils PMID: 28074190 Chondroitin sulfate A has an intensive promotion effect on the fibrillation of human IAPP at the palmitoyloleoylphosphatidylcholine (POPC) membrane, which is larger than the total effect of Chondroitin sulfate A alone and POPC alone. PMID: 27067251 C4BP protects beta-cells from IAPP cytotoxicity by modulating IAPP fibril formation extracellularly and also, after uptake by the cells, by enhancing cholesterol synthesis. PMID: 27566545 beta-hairpin peptide inhibitor of IAPP aggregation that are stabilized in that conformation, or even forced to remain in the hairpin conformation by a backbone cyclization constraint, display superior activity as inhibitors. PMID: 27317951 hA17-29 aggregate toxicity seems to be mediated by RAGE and p75-NGFR receptors PMID: 27804051 Serum levels of preptin and amylin were significantly lower in patients with psoriasis and Behcet's disease. PMID: 25545917 These data suggest participation by both soluble and fibrillar aggregates in IAPP-induced islet inflammation. IAPP-induced activation of TLR2 and secretion of IL-1 may be important therapeutic targets to prevent amyloid-associated beta cell dysfunction. PMID: 26786104 the effect of the endoplasmic reticulum chaperone protein disulfide isomerase (PDI) on beta-cell dysfunction, was examined. PMID: 26607804 Data suggest that IAPP/membrane interaction strongly depends on protonation state of His18; at neutral pH, N-terminal domain is stabilized/anchored to membrane, while C-terminal domain is disordered as if in solution. PMID: 26953503 Surface molecular structure and amino acid residue composition of hIAPP fibrils are specifically probed with nanoscale resolution using tip-enhanced Raman spectroscopy. PMID: 25952953 Structural studies and cytotoxicity assays of "aggregation-prone" IAPP(8-16) and its non-amyloidogenic variants suggest its important role in fibrillogenesis and cytotoxicity of human amylin. PMID: 25913357 structural and dynamical information of amylin and CGRP PMID: 26331261 The computational models support the cross-sequence interactions between ABETA and IAPP pentamers, which would lead to the complex hybrid ABETA-IAPP assemblies. PMID: 26173078 Study focused on human islet amyloid polypeptide aggregates and a de novo designed short polypeptide at lipid/water and air/glass interfaces; found that parallel beta-sheets adopt distinct orientations at various interfaces and exhibit characteristic chiroptical responses in the amide I and N-H stretch regions. PMID: 26263128 Secondary Structure of Rat and Human Amylin PMID: 26221949 The intramolecular hydrogen bond formation by His(18) and the possibility of His(18) participating in the formation of alpha-helical structures greatly modulated the manner of hIAPP amyloid formation. PMID: 26777153 Matrix Metalloproteinase-9 Protects Islets from Amyloid-induced Toxicity. PMID: 26483547 cross-seeding assemblies between hIAPP and rIAPP oligomers PMID: 25706385 combined computational and experimental study offers detailed mechanistic insight into the complex role of zinc on IAPP aggregation and T2D development PMID: 26603575 When copper(II) was present in the solution, no dimers were detected. Thus, the copper(II) ions disrupt the association pathway to the formation of beta-sheet rich amylin fibrils. PMID: 26352401 Computational studies identified new IAPP mutations that have stronger amyloid fibrils destabilizing potential that the currently known. PMID: 25903685 The effect of a single proline mutant at position 26 in an amylin polypeptide on its binding to a lipid bilayer was studied. PMID: 25427619 Inhibition of IAPP aggregation by insulin depends on the insulin oligomeric state regulated by zinc ion concentration PMID: 25649462 Introducing the porcine insulin promoter-hIAPP expression vector into PK15 cells combined with exogenous Pdx-1, MafA and NeuroD1 resulted in the efficient expression of hIAPP at the gene level, but not the protein. PMID: 24825179 There was abundant amylin aggregates in lysates of cardiac myocytes from obese patients, but not in controls. amylin aggregation at the sarcolemma induces oxidative stress and Ca(2+) dysregulation. PMID: 25146704 interaction between HS and IAPP or the subsequent effects represent a possible therapeutic target whose blockage can lead to a prolonged survival of beta cells PMID: 25922077

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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.