97963 Results for: "Molecular+Biology+Reagents"

Supplier: MOLECULAR DIMENSIONS INC MS

WIZARD CLASSIC 3 4 HT-96 96 X 1.7 ML

Supplier: MOLECULAR DIMENSIONS INC MS

PACK VALUE MEMGOLD COMBO HT-96 192X1ML

Supplier: MOLECULAR DIMENSIONS INC MS

LIGAND FRIENDLY SCREEN HT-96 96 X 1 ML

Supplier: MOLECULAR DIMENSIONS INC MS

SODIUM 2HYDROGEN PHOSPHT PH 9.2 1M 200ML

Supplier: Genetex

SIR2, one of the silent information regulator genes, encodes a protein that promotes a compact chromatin structure, thereby preventing or silencing gene transcription at selected loci. SIR2 belongs to a family of proteins that is found in organisms ranging from bacteria to complex eukaryotes. Members of this family contain a 250 amino acid core domain that shares about 25-60% sequence identity. Silencing occurs as a series of events initiated by formation of Sir complexes (Sir2, Sir3, Sir4). The complexes are recruited to their chromosome targets via interactions with DNA-binding proteins, followed by deacetylation of histones H3 and H4. A final step required for telomeric silencing is binding of the complex to the deacetylated histones and recruitment of the telosome to the nuclear periphery. Sir2 protein is an NAD-dependent histone deacetylase, an enzyme that removes acetyl groups from lysine residues of histone proteins and possibly other substrates. Sir2 transfers acetyl groups from its protein substrates to ADP-ribose and synthesizes o-acetyl-ADP-ribose. Through histone deacetylation, Sir2 may silence chromatin. The maintenance or silencing of chromatin may be at the center of processes leading to aging of cells and development of cancer.

Supplier: Genetex

Mu Calpain, and m calpain, also known as Calpain 2, are intracellular, calcium dependent cysteine proteases. Mu calpain has a micromolar sensitivity (thus the mu) as compared to the millimolar calcium sensitivity of m calpain. Both Calpains 1 and 2 are composed of an 80 kD subunit and a 30 kD subunit. Whereas the 30 kDa subunit is shared by both enzymes, the larger catalytic subunits are different and exhibit the distinct Ca++ requirements that are suggested by their names. The calpains have papain like activity, thus the pain nomenclature. Both Calpain 1 and Calpain 2 are ubiquitously expressed, and are countered by the endogenous calpain inhibitor, calpastatin.Other calpain family members (calpain 94, ncl2, ncl3, etc) have more limited tissue distribution, and perhaps different functions. The calpain family members consist of a common small subunit (Calpain 4), and a large variable subunit. It is not clear that all calpains contain a small subunit. Domains in the large subunit include the amino terminal domain I, the proteinase domain II, domain III, and the EF hand domain IV. The calpains appear to serve multiple physiological roles, and ideas concerning the functions of these enzymes are in a state of rapid flux.

Supplier: Genetex

Methylation of DNA at cytosine residues plays an important role in regulation of gene expression, genomic imprinting and is essential for mammalian development. Hypermethylation of CpG islands in tumor suppressor genes or hypomethylation of bulk genomic DNA may be linked with development of cancer. To date, 3 families of mammalian DNA methyltransferase genes have been identified which include Dnmt 1, Dnmt 2 and Dnmt 3. Dnmt 1 is constitutively expressed in proliferating cells and inactivation of this gene causes global demethylation of genomic DNA and embryonic lethality. Dnmt 2 is expressed at low levels in adult tissues and its inactivation does not affect DNA methylation or maintenance of methylation. The Dnmt3 family members, Dnmt 3a and Dnmt 3b, are strongly expressed in ES cells but their expression is down regulated in differentiating ES cells and is low in adult somatic tissue. Dnmt1 co-purifies with the retinoblastoma (Rb) tumour suppressor gene product, E2F 1, and HDAC 1. Dnmt 1 also cooperates with Rb to repress transcription from promoters containing E2F binding sites suggesting a link between DNA methylation, histone deacetylase and sequence-specific DNA binding activity, as well as a growth-regulatory pathway that is disrupted in nearly all cancer cells.

Supplier: Genetex

Adipose cells produce and secrete numerous physiologically important proteins, such as lipoprotein lipase, leptin, and adipocyte complement related protein of 30 kDa (Acrp30). Acrp30 is a circulating protein that is secreted exclusively by differentiated adipocytes. During adipocyte differentiation, mRNA levels of Acrp30 have been shown to be induced over 100-fold. Studies indicate that Acrp30 enhances the ability of sub-physiological levels of insulin to suppress glucose production, thus linking adipose tissue to whole body glucose regulation. Acrp30 function appears to be regulated by phosphatidylinositol 3 kinase (PI3K) since Acrp30 secretion is blocked by pharmacologic inhibitors of this kinase. mRNA levels of Acrp30 have been shown to be significantly reduced in adipose tissue of obese patients with Type 2 diabetes relative to control subjects. Structural similarities to TNF alpha suggests that Acrp30 may play a role in pathogenesis of insulin resistance in Type 2 diabetes. Because Acrp30 is down-regulated in various forms of obesity and its structural similarity to TNF alpha, it is currently being investigated as an important regulator of whole body energy homeostasis.

Supplier: Genetex

The cyclic monophosphate nucleotides (cyclic adenosine monophosphate [cAMP] and cyclic guanosine monophosphate [cGMP]) are found ubiquitously in mammalian cells and act as second messenger transducers to effect the intracellular actions of a variety of G protein coupled receptors (GPCRs) for hormones, cytokines, and neurotransmitters. Cyclic nucleotides are important intracellular second messengers which play important role in a variety of signal transduction process. The cyclic nucleotides are hydrolyzed and compartmentalized by a family of enzymes called phosphodieterases. One of the many phosphodiesterases that compartmentalized and hydrolyze cGMP in various tissues is phosphodiesterase type 5A. The cGMP is involved in nitric oxide signaling as well as cell signaling associated with natriuretic peptides and gulanylins. Some of the intracellular biding cites for the cGMP include cyclic nucleotide gated ion channels, cGMP dependent protein kinases, and cyclic GMP biding phosphodiesterases (cGB PDEs). The cGB PDEs include PDE2, PDE3, PDE5, PDE5 and PDE10; the members of these families contain various structural and functional motifs that are conserved. Most of these proteins contain dimmeric subunits that contain a highly conserved cGMP binding site and a phosphodiesterase catalytic site.

Supplier: MOLTOX Molecular Toxicology

TRYPTIC SOY AGAR SLANT 10 ML/TUBE 10BX

Supplier: GT MOLECULAR, LLC MS

KIT ASAY C.AURIS DIG PCR SYS V2.0 200RXN

Supplier: Genetex

Cyclic nucleotides are hydrolyzed and compartmentalized by a family of enzymes called phosphodieterases. In mammals at least 11 different families of PDEs can be discriminated (PDE1-11) based on their kinetic properties and inhibition to various pharmacological agents. Three different PDE1 genes have been identified (PDE1A, B, and C). PDE1A and PDE1B have higher affinity for cGMP than for cAMP, whereas PDE1C has high affinity for both cAMP and cGMP. The PDE1A gene family includes various proteins that differ from each other at amino and carboxy termini of the protein. There are three novel PDE1A variants so far identified (PDE1A1; PDE1A3 and PD1A5), PDE1A5 encodes a 519 residue protein , which is different from PDE1A1 by insertion of 14 amino acid residues at the carboxy terminal and is also different from PDE1A3 by a divergent at N-terminus. The tissue distribution of PDE1A is different from other PDE1 gene family members. In testis PDE1A is highly expressed but in different stages of developing germ cells.

Supplier: Genetex

Bassoon is a 420 kDa protein that is a localized at the presynaptic nerve terminals and is believed to play a role in the structural and functional organization of the synaptic vesicle cycle. Bassoon does not belong to any known protein families. It has been found in rat and mouse with sequence identity of the two proteins at 96%. The human BASSOON gene has recently been cloned and localized. Bassoon is predicted to contain two double-zinc fingers, three coiled-coil regions, and two polyglutamine domains. The polyglutamine domains in the C-terminus are of interest, since it is known that for some human proteins, such as Huntingtin, abnormal amplification of this region can cause late-onset neurodegeneration. Bassoon is concentrated at sites opposite to postsynaptic densities in synaptic terminals and in cultured neurons, it is found to colocalize with GABA (A) and glutamate (GluR1) receptors.Another presynaptic protein, Piccolo was found to colocalize with Bassoon in cultured hippocampal neurons. These observations suggested that they serve specific functions at synaptic junctions and may be involved in organization of the cytoskeleton at the site of neurotransmitter release.

Supplier: Rockland Immunochemical

MUC1 is a large cell surface mucin glycoprotein expressed by most glandular and ductal epithelial cells and some hematopoietic cell lineages. It is expressed on most secretory epithelium, including mammary gland and some hematopoietic cells. It is expressed abundantly in lactating mammary glands and overexpressed abundantly in >90% breast carcinomas and metastases. Transgenic MUC1 has been shown to associate with all four cebB receptors and localize with erbB1 (EGFR) in lactating glands. The MUC1 gene contains seven exons and produces several different alternatively spliced variants. The major expressed form of MUC1 uses all seven exons and is a type 1 transmembrane protein with a large extracellular tandem repeat domain. The tandem repeat domain is highly O glycosylated and alterations in glycosylation have been shown in epithelial cancer cells. This antibody is suitable for researchers interested in neuroscience research, developmental signaling, and cell adheshion.

Supplier: Genetex

Lysosomal enzymes containing one or two mannose 6-phosphate (man6P) moieties are moved about in the cell by two distinct but interconnected cycles by means of 300 kDa cation-independent mannose 6-phospate receptors (MPR). MPR cycles and transports newly synthesized lysosomal enzymes between the TGN and late endosomes / early lysosomes. It also cycles and transports extracellular lysosomal enzymes between the plasma membrane and early endosomes via clathrin coated vesicles. The bulk of the MPR protein is in the extracellular/lumenal domain. The entire pool of MPRs cycles between these cellular compartments every 3 hours. The steady state distribution of MPR's is predominantly within late endosomes, fewer in the trans Golgi network and ~5-10 % at the cell surface. In addition to its man6P binding activity, the MPR contains a separate binding site for the type II insulin-like growth factor and is capable of binding both man6P and IGF-II simultaneously. An ~240 kDa soluble, truncated form, representing the extracellular domain of the protein, has also been found circulating in serum and is capable of binding both ligands.

Supplier: Genetex

Arginine methylation is an irreversible post translational modification which has only recently been linked to protein activity. At least three types of PRMT enzymes have been identified in mammalian cells. These enzymes have been shown to have essential regulatory functions by methylation of key proteins in several fundamental areas. These protein include nuclear proteins (Histone 2A, 3, 4), IL enhancer binding factor, nuclear factors (NF45, 90, ILF3, Nucleolin, STAT1, Poly(A) binding protein II), cell cycle proteins (phosphoprotein phosphatase 2A), signal transduction proteins (FGF2, Fibrillarin, FN, INFAR1, Jak, MBP, Src-adaptor Sam68), apoptosis proteins (FADD, ICE-like protease), and viral proteins (Hepatitis C NS3 RNA Helicase, HIV TAR). The mammalian PRMT family currently consists of 5 members that share two large domains of homology. Outside of these domains, epitopes were identified and antibodies against all five PRMT members have been developed. These antibodies can be utilized to explore arginine methylation and its regulatory functions.

Supplier: Anaspec

Proinsulin C-peptide is the sequence of C peptide as it exists within proinsulin, the precursor to insulin which consists of insulin A chain, insulin B chain and C peptide (connecting peptide). In proinsulin, C peptide provides a means to ensure correct folding and assembly of the A and B chains. It is eventually cleaved away by proteases PC2, PC1/3 and CPE, at the flanking Arg-Arg and Lys-Arg basic residues (Arg-Arg-C peptide-Lys-Arg). Although C peptide is not present in mature insulin, it is stored in secretory granules, and eventually released into the bloodstream together with insulin in nearly equimolar amounts. Whereas insulin is metabolized quickly from circulation, C-peptide exhibits a slow turnover rate (>30 minutes). The measurement of the C-peptide is an important test for the β-cell function. In the red blood cells of type 2 diabetic patients, Na+,K+, ATPase activity is strongly related to blood C-peptide levels. C-peptide signal transduction in human renal tubular cells involves the activation of phospholipase C and PKC-δ and PKC-varepsilon, as well as RhoA, followed by phosphorylation of ERK1/2 and JNK and a parallel activation of Akt. C-peptide shows specific binding to a G-protein-coupled membrane binding site, resulting in Ca2+ influx, activation of mitogen-activated protein kinase signalling pathways and stimulation of Na+, K+ ATPase and endothelial nitric oxide synthase.
Sequence: RREAEDLQVGQVELGGGPGAGSLQPLALEGSLQKR
MW: 3617 Da
% Peak area by HPLC: 95
Storage condition: -20° C

Supplier: Genetex

Structural Maintenance of Chromosomes (SMC) family proteins play critical roles in various nuclear events that require structural changes of chromosomes, including mitotic chromosome organization, DNA recombination and repair and global transcriptional repression. The chromosome proteins are conserved in eukaryotes lead to mitotic chromosome segregation defects, suggesting a critical function of SMC family proteins in mitotic chromosome dynamics. SMC1 and SMC3 form a heterodimeric complex required for metaphase progression in mitotic cells. Specifically this SMC1/SMC3 complex is responsible for sister chromatid cohesion during metaphase. A number of cellular factors interact with hSMC1/hSMC3 during cell cycle. The major population of hSMC1/hSMC3 is in a compex with hRAD21 forming the human cohesion complex. Human cohesion associates with chromosomes which peaks at S phase and dissociates from chromosomes during G2/M transition. In addition, a subpopulation of hSMC1/hSMC3 associates tightly with nuclear matrix and centrosomes during interphase. A subset of hSMC1/hSMC3 is localized to spindle poles, spindles and kinetochores during mitosis when cohesin is in the cytoplasm. hSMC1/hSMC3 is required for spindle aster formation in vitro and reacts with nuclear mitotic apparatus protein in vivo.

Supplier: Genetex

Peroxisome proliferators are non genotoxic carcinogens which are purported to exert their effect on cells through their interaction with members of the nuclear hormone receptor family termed peroxisome proliferator activated receptors (PPARs). Nuclear hormone receptors are ligand dependent intracellular proteins that stimulate transcription of specific genes by binding to specific DNA sequences following activation by the appropriate ligand. Studies indicate that PPARs are activated by peroxisome proliferators such as clofibric acid, nafenopin, and WY14,643, as well as by some fatty acids. It has also been shown that PPARs can induce transcription of acyl coenzyme A oxidase & cytochrome P450 (CYP450) A6 through interaction with specific response elements. The PPAR gamma 2 isoform appears to be induced very early in the differentiation of several cultured adipocyte cell lines, and has been suggested to be a dominant regulator of the murine P2 (aP2) gene which encodes an intracellular lipid binding protein which is expressed only in adipose cells. PPAR gamma 2, like several other nuclear hormone receptors, heterodimerizes with RXR alpha.

Supplier: Genetex

Superoxide dismutase (SOD) is responsible for the elimination of cytotoxic active oxygen by catalyzing the dismutation of the superoxide radical to oxygen and hydrogen peroxide. There are three SOD isoenzymes in mammalian cells. They are: extracellular SOD (EC SOD), copper and zinc-containing SOD (Cu/Zn SOD) and manganese-containing SOD (Mn SOD). The Cu/Zn form contains Cu and Zn ions and exists as a 32 kDa dimer in the cytosol. Mn SOD is an 80 kDa tetramer that contains Mn ion and resides in the mitochondrial matrix. Mn SOD is a tumor necrosis factor (TNF)-inducible enzyme that protects cells from TNF-mediated apoptosis via superoxide anion detoxification and the subsequent regulation of apoptosis through cytochrome c release and the modulation of the redox state of the mitochondria. Mn SOD has also been shown to be a tumor suppressor in human breast cancer. Overexpression of this enzyme protects neurons from NMDA- and nitric oxide-induced neurotoxicity.

Supplier: Genetex

Caspases are a family of cysteine proteases that are key mediators of programmed cell death or apoptosis. The precursor form of all caspases is composed of a prodomain, and large and small catalytic subunits. The active forms of caspases are generated by several stimuli including ligand-receptor interactions, growth factor deprivation and inhibitors of cellular functions. All known caspases require cleavage adjacent to aspartates to liberate one large and one small subunit, which associate into a2b2 tetramer to form the active enzyme. Gene for Caspase 3 also known as Yama, CPP32, and apopain codes for a 32-kDa protein. Caspase 3 cleaves the death substrate poly(ADP-ribose) polymerase (PARP) to a specific 85 kDa form observed during apoptosis and is inhibitable by the CrmA protein. Other Caspase 3 substrates include DNA-PK, actin, GAS2, and procaspase-6, etc. Caspase 3 is activated by cleavage events at Asp-28/Ser-29 (between N-terminal pro-domain) and Asp-175/Ser-176 (between large and small subunits) to generate a large subunit of 17-kDa and a small subunit of 12-kDa.

Supplier: Genetex

The implication of alpha synuclein in neurodegenerative diseases started after the identification of non A beta component of amyloid (NAC peptide) in Alzheimeris disease (AD) brains.There is now a general group of synucleinopathies which implicates alpha synuclein in Lewy body syndromes, Parkinsonis disease, and Alzheimeris disease. Certain missense mutations in the alpha synuclein gene (A53T, A30P) have been linked to the familial Parkinsonis disease (PD). Alpha synuclein is the major component of Lewy bodies and Lewy neuritis in sporadic PD, dementia with Lewy Bodies and Lewy Body variant of AD. Lewy bodies are composed of truncated and phosphorylated intermediate neurofilament proteins, alpha synuclein, ubiquitin and associated enzymes. The synuclein phosphoproteins (15-20 kD) are small highly conserved proteins in vertebrates. The synuclein family includes alpha and beta synucleins and loosely related gamma synuclein and synoretin.The expression is abundant in neurons and typically localized at presynaptic terminals. Antibodies to alpha synuclein provide a specific method to detect Lewy bodies and associated pathological mechanism of PD and AD.

Supplier: Genetex

Ran (ras-related nuclear protein) is a small GTP binding protein belonging to the RAS superfamily that is essential for the translocation of RNA and proteins through the nuclear pore complex. The Ran protein is also involved in control of DNA synthesis and cell cycle progression. Nuclear localization of Ran requires the presence of regulator of chromosome condensation 1 (RCC1). Mutations in Ran disrupt DNA synthesis. Because of its many functions, it is likely that Ran interacts with several other proteins. Ran regulates formation and organization of the microtubule network independently of its role in the nucleus-cytosol exchange of macromolecules. Ran could be a key signaling molecule regulating microtubule polymerization during mitosis. RCC1 generates a high local concentration of Ran-GTP around chromatin which, in turn, induces the local nucleation of microtubules. Ran is an androgen receptor (AR) coactivator that binds differentially with different lengths of polyglutamine within the androgen receptor. Polyglutamine repeat expansion in the AR is linked to Kennedy's disease (X-linked spinal and bulbar muscular atrophy). Ran coactivation of the AR diminishes with polyglutamine expansion within the AR, and this weak coactivation may lead to partial androgen insensitivity during the development of Kennedy's disease.

Supplier: Genetex

Bcl2 family is a key regulator of apoptosis that functions to either inhibit or promote cell death. Over-expression of members such as Bcl2 and BclxL inhibit the apoptotic process. The Bcl2 family members are also characterized by dimerizing to further modulate apoptosis. Bag1, for example, has been found to form a heterodimer with Bcl2 resulting in the enhancement of the anti-apoptotic effect of Bcl2. Bax and Bak have been shown to play a critical role in cytochrome c release from mitochondria and thus initiate apoptosis. Bax exerts a pro-apoptotic rather than an anti-apoptotic effect on cells. Bax targets mitochondrial membranes, inducing mitochondrial damage and cell death in a caspase-independent manner. Bad plays a critical role in the Bax-mediated apoptosis pathway by dimerizing with BclxL, causing the displacment of Bax. The displacement of Bax allows apoptosis to proceed. BclxS, a shorter version of BclxL (lacking amino acids 126-188), apparently utilizes a different pathway than Bax to induce cell death. Some research suggests that BclxS uses a novel mechanism for regulating caspase or it may use an alternate cell death effector pathway.

Supplier: Genetex

Methylation of DNA at cytosine residues plays an important role in regulation of gene expression, genomic imprinting and is essential for mammalian development. Hypermethylation of CpG islands in tumor suppressor genes or hypomethylation of bulk genomic DNA may be linked with development of cancer. To date, 3 families of mammalian DNA methyltransferase genes have been identified which include Dnmt1, Dnmt2 and Dnmt3. Dnmt1 is constitutively expressed in proliferating cells and inactivation of this gene causes global demethylation of genomic DNA and embryonic lethality. Dnmt2 is expressed at low levels in adult tissues and its inactivation does not affect DNA methylation or maintenance of methylation. The Dnmt3 family members, Dnmt3a and Dnmt3b, are strongly expressed in ES cells but their expression is down regulated in differentiating ES cells and is low in adult somatic tissue. Dnmt 1 co-purifies with the retinoblastoma (Rb) tumour suppressor gene product, E2F1, and HDAC1. Dnmt 1 also cooperates with Rb to repress transcription from promoters containing E2F binding sites suggesting a link between DNA methylation, histone deacetylase and sequence-specific DNA binding activity, as well as a growth-regulatory pathway that is disrupted in nearly all cancer cells.

Supplier: Genetex

Arginine methylation is an irreversible post translational modification which has only recently been linked to protein activity. At least three types of PRMT enzymes have been identified in mammalian cells. These enzymes have been shown to have essential regulatory functions by methylation of key proteins in several fundamental areas. These protein include nuclear proteins (Histone 2A, 3, 4), IL enhancer binding factor, nuclear factors (NF45, 90, ILF3, Nucleolin, STAT1, Poly(A) binding protein II), cell cycle proteins (phosphoprotein phosphatase 2A), signal transduction proteins (FGF2, Fibrillarin, FN, INFAR1, Jak, MBP, Src adaptor Sam68), apoptosis proteins (FADD, ICE like protease), and viral proteins (Hepatitis C NS3 RNA Helicase, HIV TAR). The mammalian PRMT family currently consists of 5 members that share two large domains of homology. Outside of these domains, epitopes were identified and antibodies against all five PRMT members have been developed. These antibodies can be utilized to explore arginine methylation and its regulatory functions.

Supplier: Sedia Biosciences

Sedia’s Asanté™ Dried Blood Specimen Collection Strips (Asanté™ Strips) are intended for the collection, transport, storage, testing, and archiving of blood specimens, including finger-stick blood, venous blood, serum, or plasma.

Supplier: Biosensis

Neurofilaments can be defined as the intermediate or 10nm diameter filaments found in neuronal cells. They are composed a mixture of subunits which often includes the neurofilament triplet proteins, NF-L, NF-M and NF-H. Neurofilaments may also include peripherin, alpha-internexin, nestin and in some cases vimentin. Alpha-internexin is a ~66 kDa Class IV intermediate filament subunit expressed in large amounts early in neuronal development, but is downregulated in many neurons as development procedes. Many classes of mature neurons contain alpha-internexin in addition to NF-L, NF-M and NF-H. In some mature neurons alpha-internexin is the only neurofilament subunit expressed. Antibodies to alpha-internexin are therefore unique probes to study and classify neuronal types and follow their processes in sections and in tissue culture. In addition the very early developmental expression of alpha-internexin means its presence is an early and convenient diagnostic feature of neuronal progenitors cells and other cell committed to the neuronal lineage.

Supplier: 0000014724

GLYCEROL 100% 250ML

Supplier: Anaspec

This GLP-1 (7-36) amide peptide is fluorescently labeled at Tryptophan residue 25 with Fluorescein. This is the same type of fluorescent labeling as in Extendin-4 Flex peptide (Cat# AS-63899). GLP-1 (7-36) amide is an incretin hormone that causes glucose dependent release of insulin by pancreatic beta cells. It is the cleavage product of GLP-1 (1-36) amide peptide (cat# AS-22460). Both GLP-1 (7-36) and GLP-1 (7-37) - Cat# AS-20761, also play roles in gastric motility (gastric emptying), on the suppression of plasma glucagon levels (glucose production) and possibly on the promotion of satiety and stimulation of glucose disposal in peripheral tissues independent of the actions of insulin. GLP-1 (7-36) has a short half life of less than 2 minutes, and like GIP, is rapidly degraded by the enzyme dipeptidyl peptidase IV (DPP-4), which is widely expressed in a number of sites, including the endothelial cells of small gut arterioles. DPP-4 degrades GLP-1 (7-36) into the non insulinotropic GLP-1 (9-36) - Cat# AS-65070 (some studies suggest it may have weak insulinotropic activity). As a result, the majority of GLP-1 (and GIP) is inactivated as an insulinotrope before reaching the systemic circulation.
Sequence: HAEGTFTSDVSSYLEGQAAKEFIA (Trp-S-FAM)-LVKGR-NH2
MW: 3717.5 Da
% Peak area by HPLC: 95
Storage condition: -20° C