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1000 results found for “Serpin”
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Name :
HSV-2 gBDescription:
Herpes Simplex Virus-2 gB Recombinant
Product # :
HSV-226Price :
Quantity :
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Description
The E.Coli derived HSV-2 gB recombinant protein is fused to a Six histidine tag at C-terminus and has a MW of 82kDa (pI 8.35).
Source
Escherichia Coli.
Formulation
10mM Phosphate buffer pH 7.6 and 75mM NaCl.
Purity
Protein is >90% pure as determined by SDS PAGE.
More Info
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Introduction
Entry of HSV into the host cell involves interactions of several viral glycoproteins with cell surface receptors. The virus particle is covered by an envelope which, when bound to specific receptors on the cell surface, will fuse with the cell membrane and create an opening, or pore, through which the virus enters the host cell. The sequential stages of HSV entry are analagous to those of other viruses. At first, complementary receptors on the virus and cell surface bring the two membranes into proximity. In an intermediate state, the two membranes begin to merge, forming a hemifusion state. Finally, a stable entry pore is formed through which the viral envelope contents are introduced to the host cell.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
HSV-2 gB although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MIAPYKFKATMYYKDVTVSQVWFGHRYSQFMGIFEDRAPVPFEEVIDKINAKGVCRST AKYVRNNLETTAFHRDDHETDMELKPANAATRTSRGWHTTDLKYNPSRVEAFHRYGT
TVNCIVEEVDARSVYPYDEFVLATGDFVYMSPFYGYREGSHTEHTSYAADRFKQVDGF
YARDLTTKARATAPTTRNLLTTPKFTVAWDWVPKRPSVCTHHHHHH. -
Applications
ELISA, WB, Flow-Through.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Soybean P34 GSTDescription:
Soybean P34 Protein Recombinant, GST Tag
Product # :
ALR-005Price :
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Description
The E.Coli derived GST Tag recombinant protein, 36kDa, contains Soybean P34 Protein epitopes 214-261, 351-379 amino acids.
Source
Escherichia Coli.
Formulation
50mM Tris-HCl, pH 8.0, 60mM NaCl, 10mM glutathione and 50% glycerol.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
The P34 protein is the main allergen for soybean sensitive humans. Soybean protein P34, a thiol protease belonging to the papain family, is a monomeric allergen having an N-terminal amino acid sequence and amino acid composition identical to that of the seed 34kDa protein. It is an insoluble glycoprotein having a pI of 4.5 and a calculated mass of 28.643 Dalton, representing 2–3% of total soybean protein. Upon glycosylation, the mass will be somewhat larger, resulting in a ~32kDa band in non-reduced SDS PAGE gels. It exhibits no enzymatic function due to an absence of the catalytic cysteine. P34 is stored in storage vacuoles of soybean cotyledons.
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Stability
Soybean P34 His although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Purification Method
Purified by proprietary chromatographic technique
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SNRPC HumanDescription:
Small Nuclear Ribonucleoprotein Polypeptide C Human Recombinant
U1 small nuclear ribonucleoprotein C, U1 snRNP C, U1-C, U1C, SNRPC, Yhc1.
Product # :
PRO-1004Price :
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Description
SNRPC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-159 a.a.) and having a molecular mass of 19.8kDa (Molecular weight on SDS-PAGE will appear higher).SNRPC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SNRPC protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.3M NaCl, 5mM DTT and 2mM EDTA.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
SNRPC is a member of the U1 small nuclear ribonucleoprotein C family. The SNRPC protein component of the U1 small nuclear ribonucleoprotein (snRNP) particle required for the formation of the spliceosome. SNRPC participates in the processing of nuclear precursor messenger RNA splicing. snRNP particles are tackled by autoantibodies frequently produced by patients with connective tissue diseases.
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Synonyms
U1 small nuclear ribonucleoprotein C, U1 snRNP C, U1-C, U1C, SNRPC, Yhc1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPKFYCD YCDTYLTHDS PSVRKTHCSG RKHKENVKDY YQKWMEEQAQ SLIDKTTAAF QQGKIPPTPF SAPPPAGAMI PPPPSLPGPP RPGMMPAPHM GGPPMMPMMG PPPPGMMPVG PAPGMRPPMG GHMPMMPGPP MMRPPARPMM VPTRPGMTRP DR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NPEPPS HumanDescription:
Aminopeptidase Puromycin Sensitive Human Recombinant
PSA, MP100, AAP-S, Puromycin-sensitive aminopeptidase, Cytosol alanyl aminopeptidase, aminopeptidase puromycin sensitive.
Product # :
ENZ-1196Price :
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Description
NPEPPS Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 925 amino acids (1-919 a.a.) and having a molecular mass of 104kDa. NPEPPS is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
NPEPPS protein solution (0.25mg/ml) containing 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 85.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 800 pmol/min/ug and is defined as the amount of enzyme that cleaves 1 pmole of H-Leu[1]AMC per minute at pH7.0 at 37°C.
More Info
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Synonyms
PSA, MP100, AAP-S, Puromycin-sensitive aminopeptidase, Cytosol alanyl aminopeptidase, aminopeptidase puromycin sensitive.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MWLAAAAPSL ARRLLFLGPP PPPLLLLVFS RSSRRRLHSL GLAAMPEKRP FERLPADVSP INYSLCLKPD LLDFTFEGKL EAAAQVRQAT NQIVMNCADI DIITASYAPE GDEEIHATGF NYQNEDEKVT LSFPSTLQTG TGTLKIDFVG ELNDKMKGFY RSKYTTPSGE VRYAAVTQFE ATDARRAFPC WDEPAIKATF DISLVVPKDR VALSNMNVID RKPYPDDENL VEVKFARTPV MSTYLVAFVV GEYDFVETRS KDGVCVRVYT PVGKAEQGKF ALEVAAKTLP FYKDYFNVPY PLPKIDLIAI ADFAAGAMEN GLVTYRETA LLIDPKNSCS SSRQWVALVV GHELAHQWFG NLVTMEWWTH LWLNEGFASW IEYLCVDHCF PEYDIWTQFV SADYTRAQEL DALDNSHPIE VSVGHPSEVD EIFDAISYSK GASVIRMLHD YIGDKDFKKG MNMYLTKFQQ KNAATEDLWE SLENASGKPI AAVMNTWTKQ MGFPLIYVEA EQVEDDRLLR LSQKKFCAGG SYVGEDCPQW MVPITISTSE DPNQAKLKIL MDKPEMNVVL KNVKPDQWVK LNLGTVGFYR TQYSSAMLES LLPGIRDLSL PPVDRLGLQN DLFSLARAGI ISTVEVLKVM EAFVNEPNYT VWSDLSCNLG ILSTLLSHTD FYEEIQEFVK DVFSPIGERL GWDPKPGEGH LDALLRGLVL GKLGKAGHKA TLEEARRRFK DHVEGKQILS ADLRSPVYLT VLKHGDGTTL DIMLKLHKQA DMQEEKNRIE RVLGATLLPD LIQKVLTFAL SEEVRPQDTV SVIGGVAGGS KHGRKAAWKF IKDNWEELYN RYQGGFLISR LIKLSVEGFA VDKMAGEVKA FFESHPAPSA ERTIQQCCEN ILLNAAWLKR DAESIHQYLL QRKASPPTVH HHHHH.
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Background
NPEPPS is involved in the proteolytic degradation of misfolded or damaged proteins, contributing to the maintenance of protein homeostasis within the cell. It specifically removes N-terminal amino acids from peptides, thereby regulating their activity and facilitating their further degradation by other proteases.
This enzyme is particularly important in the nervous system, where it degrades neuropeptides and helps regulate synaptic signaling and neuronal communication.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
FBLIM1 HumanDescription:
Filamin Binding LIM Protein 1 Human Recombinant
Filamin binding LIM protein 1, CAL, FBLP-1, FBLP1, RP11-169K16.5, Migfilin, Mitogen-inducible 2-interacting protein, MIG2-interacting protein.
Product # :
PRO-1473Price :
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Description
FBLIM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 396 amino acids (1-373) and having a molecular mass of 43.1 kDa. FBLIM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FBLIM1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Filamin binding LIM protein 1 (FBLIM1) plays a role as an anchoring site for cell-ECM adhesion proteins and filamin-containing actin filaments. FBLIM1 is involved in cell shape spreading and motility. FBLIM1 participates in the regulation of filamin-mediated cross-linking and stabilization of actin filaments. FBLIM1 promotes stimulation of integrins and regulates integrin-mediated cell-cell adhesion.
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Synonyms
Filamin binding LIM protein 1, CAL, FBLP-1, FBLP1, RP11-169K16.5, Migfilin, Mitogen-inducible 2-interacting protein, MIG2-interacting protein.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMASKPEK RVASSVFITL APPRRDVAVA EEVRQAVCEA RRGRPWEAPA PMKTPEAGLA GRPSPWTTPG RAAATVPAAP MQLFNGGCPP PPPVLDGEDV LPDLDLLPPP PPPPPVLLPS EEEAPAPMGA SLIADLEQLH LSPPPPPPQA PAEGPSVQPG PLRPMEEELP PPPAEPVEKG ASTDICAFCH KTVSPRELAV EAMKRQYHAQ CFTCRTCRRQ LAGQSFYQKD GRPLCEPCYQ DTLERCGKCG EVVRDHIIRA LGQAFHPSCF TCVTCARCIG DESFALGSQN EVYCLDDFYR KFAPVCSICE NPIIPRDGKD AFKIECMGRN FHENCYRCED CRILLSVEPT DQGCYPLNNH LFCKPCHVKR SAAGCC.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
POR (43-677) HumanDescription:
P450 Oxidoreductase Human Recombinant
P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.
Product # :
ENZ-1186Price :
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Description
POR Human Recombinant produced in Sf9 Insect cells is a single, glycosylated, polypeptide chain (43-677 a.a) containing a total of 642 amino acids, having a molecular mass of 73.0 kDa. POR is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
POR protein solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 1,500 pmol/min/mg. Defined by the amount of enzyme that reduction of 1 pmole cytochrome-C by NADPH/min. at pH-8 25C.
More Info
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Synonyms
P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MLFRKKKEEV PEFTKIQTLT SSVRESSFVE KMKKTGRNII VFYGSQTGTA EEFANRLSKD AHRYGMRGMS ADPEEYDLAD LSSLPEIDNA LVVFCMATYG EGDPTDNAQD FYDWLQETDV DLSGVKFAVF GLGNKTYEHF NAMGKYVDKR LEQLGAQRIF ELGLGDDDGN LEEDFITWRE QFWPAVCEHF GVEATGEESS IRQYELVVHT DIDAAKVYMG EMGRLKSYEN QKPPFDAKNP FLAAVTTNRK LNQGTERHLM HLELDISDSK IRYESGDHVA VYPANDSALV NQLGKILGAD LDVVMSLNNL DEESNKKHPF PCPTSYRTAL TYYLDITNPP RTNVLYELAQ YASEPSEQEL LRKMASSSGE GKELYLSWVV EARRHILAIL QDCPSLRPPI DHLCELLPRL QARYYSIASS SKVHPNSVHI CAVVVEYETK AGRINKGVAT NWLRAKEPAG ENGGRALVPM FVRKSQFRLP FKATTPVIMV GPGTGVAPFI GFIQERAWLR QQGKEVGETL LYYGCRRSDE DYLYREELAQ FHRDGALTQL NVAFSREQSH KVYVQHLLKQ DREHLWKLIE GGAHIYVCGD ARNMARDVQN TFYDIVAELG AMEHAQAVDY IKKLMTKGRY SLDVWSHHHH HH.
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Background
P450 Oxidoreductase (POR) is a vital enzyme that plays a crucial role in the electron transfer system, specifically in the cytochrome P450 (CYP) enzyme family. POR acts as an electron donor for various CYP enzymes involved in drug metabolism, steroid biosynthesis, and detoxification processes. This research aims to explore the function, regulation, and significance of POR protein in human cells, shedding light on its role in maintaining cellular homeostasis and drug metabolism.
Function of POR Protein:
POR protein serves as an essential component in the redox reactions of the CYP enzymes. It transfers electrons from NADPH to the CYP enzymes, allowing them to catalyze a wide range of reactions involved in the metabolism of endogenous compounds, drugs, and toxins. Through its electron transfer function, POR enables the activation or inactivation of substrates, contributing to the regulation of cellular processes such as hormone synthesis, drug clearance, and xenobiotic detoxification.
Regulation of POR Protein:
The expression and activity of POR protein are tightly regulated to ensure proper functioning of the CYP enzymes. Several factors influence POR expression, including genetic variations, environmental stimuli, and hormonal signals. Transcriptional regulation of POR involves binding of specific transcription factors to its promoter region. Additionally, post-translational modifications, such as phosphorylation and protein-protein interactions, modulate POR activity, influencing its electron transfer efficiency and interaction with CYP enzymes.
Role of POR Protein in Drug Metabolism:
One of the prominent functions of POR protein is its involvement in drug metabolism. POR collaborates with CYP enzymes in the biotransformation of a wide array of drugs, converting them into more soluble and easily excretable forms. The interplay between POR and CYP enzymes determines the pharmacokinetics and therapeutic efficacy of numerous drugs. Understanding the role of POR in drug metabolism is crucial for predicting drug-drug interactions, optimizing drug dosing, and minimizing the risk of adverse reactions.
Significance of POR Protein in Disease States:
Emerging evidence suggests that POR protein dysregulation can contribute to various disease states. Mutations in the POR gene have been linked to disorders such as Antley-Bixler syndrome and disordered steroidogenesis, highlighting the critical role of POR in development and endocrine function. Moreover, altered POR expression and activity have been implicated in drug resistance and toxicity, as well as in the pathogenesis of certain cancers.
Conclusion:
The investigation of P450 Oxidoreductase (POR) protein in human cells provides valuable insights into its function, regulation, and significance in various physiological and pathological processes. Understanding the interplay between POR and CYP enzymes is essential for deciphering drug metabolism pathways, predicting drug interactions, and developing personalized therapeutic strategies. Further research is warranted to unravel the intricate mechanisms governing POR activity and its potential as a therapeutic target.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TRAPPC4 HumanDescription:
Trafficking Protein Particle Complex 4 Human Recombinant
Trafficking protein particle complex subunit 4, TRS23 homolog, Synbindin, Hematopoietic stem/progenitor cell protein 172.
Product # :
PRO-1273Price :
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Description
TRAPPC4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 242 amino acids (1-219) and having a molecular mass of 26.7kDa. TRAPPC4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TRAPPC4 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Trafficking protein particle complex 4 (TRAPPC4) is part of the multisubunit TRAPP (transport protein particle) complex and interacts with SDC2. TRAPPC4 has a role in vesicular transport from endoplasmic reticulum to Golgi.
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Synonyms
Trafficking protein particle complex subunit 4, TRS23 homolog, Synbindin, Hematopoietic stem/progenitor cell protein 172.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAIFSVY VVNKAGGLIY QLDSYAPRAE AEKTFSYPLD LLLKLHDERV LVAFGQRDGI RVGHAVLAIN GMDVNGRYTA DGKEVLEYLG NPANYPVSIR FGRPRLTSNE KLMLASMFHS LFAIGSQLSP EQGSSGIEML ETDTFKLHCY QTLTGIKFVV LADPRQAGID SLLRKIYEIY SDFALKNPFY SLEMPIRCEL FDQNLKLALE VAEKAGTFGP GS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Bet v 2.0101Description:
Profilin-1 Recombinant
Profilin-1, Allergen Bet v II, Pollen allergen Bet v 2, Bet v 2, BETVII, Bet v 2.0101.
Product # :
PRO-2283Price :
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Description
Recombinant Profilin-1 produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 15,625 Dalton. Bet v 2.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Bet v 2.0101 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Profilin-1 (Bet v 2.0101) binds to actin and affects the structure of the cytoskeleton. At high concentrations, profiling-1 averts the polymerization of actin, whereas it augments it at low concentrations. By binding to PIP2, Profilin-1 inhibits the creation of IP3 and DG.
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Synonyms
Profilin-1, Allergen Bet v II, Pollen allergen Bet v 2, Bet v 2, BETVII, Bet v 2.0101.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HCV NS5, BiotinDescription:
Hepatitis C Virus NS5, Biotin Recombinant
Product # :
HCV-236Price :
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Description
The E.coli derived Biotin Labeled recombinant protein contains the HCV NS5 immunodominant regions. HCV NS5 antigen (recombinant) a.a 2061 to a.a 2302 of HCV polyprotein. The protein is fused to a GST tag at N-terminus.
Formulation
1.5M urea, 25mM Tris-HCl pH 8.0, 0.2% Triton-X and 50% Glycerol.
Purity
HCV NS5 Biotin protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6). -
Stability
HCV NS5 Biotin although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
HCV NS5 Biotin antigen is suitable for ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.
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Specificity
Immunoreactive with sera of HCV-infected individuals.
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Purification Method
HCV NS5 Biotin protein was purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NCL HumanDescription:
Nucleolin Human Recombinant
Nucleolin, Protein C23, NCL, C23.
Product # :
PRO-1508Price :
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Description
Nucleolin Human Recombinant produced in SF9 is a glycosylated, polypeptide chain containing the C-terminal section of the human nucleolin and missing the N-terminal histone-binding part of nucleolin, having a calculated molecular mass of 55,162 Dalton. NCL is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 Insect Cells.
Formulation
NCL is supplied in 20mM HEPES pH-7.3, 600mM NaCl, 0.3mM Tris(2-carboxyethyl)phosphine (TCEP) and 25% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Nucleolin (NCL) which is a eukaryotic nucleolar phosphoprotein, involved in the synthesis and maturation of ribosomes. Nucleolin is the key nucleolar protein of growing eukaryotic cells. NCL is found linked with intranucleolar chromatin and pre-ribosomal particles. NCL induces chromatin decondensation by binding to histone H1. Nucleolin is assumed to have a role in pre-rRNA transcription and ribosome compilation. Nucleolin may also have a role in the process of transcriptional elongation. Nucleolin is located primarily in the dense fibrillar regions of the nucleolus. The Human NCL gene consists of 14 exons with 13 introns and spans approximately 11kb.
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Synonyms
Nucleolin, Protein C23, NCL, C23.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CTSD MouseDescription:
Cathepsin-D Mouse Recombinant
Ctsd, CatD, CD, Cathepsin D.
Product # :
ENZ-1017Price :
Quantity :
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Description
CTSD produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 398 amino acids (21-410 a.a.) and having a molecular mass of 44.0kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CTSD is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CTSD protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 1,000 pmol/min/ug in which one unit will convert 1.0 pmole of Mca-PLGL-Dpa-AR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25C.More Info
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Introduction
Cathepsin D is synthesized as a 54kDa precursor, which is proteolytically processed to an intermediate 48kDa single chain, which matures into more stable 34kDa and 14kDa two chain form. It is an estrogen-regulated lysosomal protease that has been suggested to facilitate cancer cell migration and invasion by digesting the basement membrane, extracellular matrix, and xonnective tissue. Because of its mitogenic and proteolytic activities, it has been implicated as a prognostic marker in many tumor types. Cathepsin D is expressed in epithelial cells as well as in macrophages.
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Synonyms
Ctsd, CatD, CD, Cathepsin D.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
IIRIPLRKFT SIRRTMTEVG GSVEDLILKG PITKYSMQSS PKTTEPVSEL LKNYLDAQYY GDIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KILDIACWVH HKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC KSDQSKARGI KVEKQIFGEA TKQPGIVFVA AKFDGILGMG YPHISVNNVL PVFDNLMQQK LVDKNIFSFY LNRDPEGQPG GELMLGGTDS KYYHGELSYL NVTRKAYWQV HMDQLEVGNE LTLCKGGCEA IVDTGTSLLV GPVEEVKELQ KAIGAVPLIQ GEYMIPCEKV SSLPTVYLKL GGKNYELHPD KYILKVSQGG KTICLSGFMG MDIPPPSGPL WILGDVFIGS YYTVFDRDNN RVGFANAVVL LEHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
C3 RatDescription:
Complement C3 Rat
Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.
Product # :
PRO-2706Price :
Quantity :
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Shipped with Ice Packs
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Description
Rat Complement C3 produced in Rat plasma having a molecular weight of 187kDa.
Source
Rat Plasma.
Formulation
C3 solution contains phosphate buffer saline.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
C3 is central to the activation of all 3 pathways of complement activation. Initiation of each pathway generates proteolytic enzyme complexes which binds the target surface. These enzymes cleave a peptide bond in C3 releasing the anaphylatoxin C3a and activating C3b. Most of the C3 activated during complement activation never attaches to the surface due to its thioester reaction with water forming fluid phase C3b which is rapidly inactivated by factors H and I forming iC3b. Surface-bound C3b is necessary in all 3 pathways for efficient activation of C5 and formation of C5b-9 complexes that lyse the target cell membrane.
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Synonyms
Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.
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Physical Appearance
Sterile filtered solution.
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Stability
C3 Mouse is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
BivalirudinDescription:
Bivalirudin
Product # :
PRO-357Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The active of Bivalirudin substance is a synthetic 20 amino acid peptide. The amino acid sequence is Phe-Pro-Arg-Pro-Gly-Gly-Gly-Gly- Asn-Gly-Asp-Phe-Glu-Glu-Ile- Pro-Glu-Glu-Tyr-Leu. The Mw is 2180 dalton.
Formulation
The protein (1mg/ml) was lyophilized with 0.5mg Manntiol and sodium hydroxide 50µg pH-5.5.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Bivalirudin directly inhibits thrombin by specifically binding as well to the catalytic site and to the anion-binding exosite of circulating and clot-bound thrombin. Bivalirudin is a specific and reversible direct thrombin inhibitor.
Thrombin, which is a serine protease, plays a central role in the thrombotic process; it cleaves fibrinogen into fibrin monomers and activates Factor XIII to Factor XIIIa, allowing fibrin to develop a covalently cross-linked structure which stabilizes the thrombus. Thrombin also activates Factors V and VIII, which promotes further thrombin generation, activates platelets, stimulating aggregation and granule release. -
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bivalirudin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bivalirudin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Bivalirudin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CALB2 MouseDescription:
Calbindin-2 Mouse Recombinant
Calretinin, CR, Calb2, calbindin 2.
Product # :
PRO-290Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Calretinin Mouse Recombinant full length protein expressed in E.coli, shows a 57 kDa band on SDS-PAGE.The Calretinin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Calretinin protein at 100µg/ml in 50mM Tris-HCl, pH7.5 and 10mM L-glutathione (reduced).
More Info
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Introduction
Calretinin is an intracellular calcium-binding protein belonging to the troponin C superfamily characterized by a structural motif described as the EF-hand domain. The immunohistochemical detection of calretinin in developing cerebellum is restricted to the later stages indicated by weak staining from week 21 of gestation, in Purkinje and basket cells and in neurons of the dentate nucleus. The intensity of staining increases as the cerebellum matures. In tumors, calretinin has been detected in mesotheliomas and some pulmonary adenocarcinomas.
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Synonyms
Calretinin, CR, Calb2, calbindin 2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Benzonase Nuclease, 99%Description:
Benzonase Nuclease Serratia Marcescens Recombinant, 99%
Product # :
ENZ-1112Price :
Quantity :
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Shipped with Ice Packs
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Description
Benzonase Nuclease Serratia Marcescens Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 245 amino acids and having a molecular mass of 30kDa with 2 essential disulfide bonds. Benzonase Nuclease is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Benzonase Nuclease solution contains 50% glycerol, 50 mM Tris-HCl pH 8.0, 20 mM NaCl and 2 mM MgCl2.
Purity
Greater than 99.0% as determined by SDS-PAGE.
More Info
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Introduction
Serratia marcescens secretes an endonuclease that has exceptionally high specific activity to the medium that surrounds it. The Benzonase Nuclease is mainly used for elimination of nucleic acid contamination from purified proteins, downstream processing, reduction of viscosity etc. Nucleic acid contaminants are caused by nuclease released to the medium. The DNA is being destroyed by the release of the S. marcescens nuclease and it acts as the killer gene for the auto destruction of microorganisms.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Specificity
Unspecific (DNA, RNA) attacks all nucleic acids (single strand, double strand, circular, supercoiled) with no apparent sequence preference. Final reaction product: 5’-mono-phosphate terminated oligonucleotides (3-5 bases). Protease Activity: Not detectable
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Unit Definition
1U Benzonase Nuclease is defined as the amount of enzyme that causes a ΔA260 of 1 in 30 min, which corresponds to complete digestion of 37μg DNA. Standard reaction conditions are 1mg/ml sonicated DNA substrate in 50mM Tris-HCl pH 8.0, 0.1mg/ml BSA, 1mM MgCl2, incubated at 37°C.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
AITR HumanDescription:
AITR Human Recombinant
TNFRSF18, AITR, CD357, GITR, GITR-D, Tumor necrosis factor receptor superfamily member 18, Activation-inducible TNFR family receptor, Glucocorticoid-induced TNFR-related protein, CD357, UNQ319/PRO364.
Product # :
CYT-925Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
AITR Human Recombinant produced in Sf9 Baculovirus is a single, glycosylated polypeptide chain containing 145 amino acids (26-162a.a.) and having a molecular mass of 15.6kDa (Migrates at 18-28kDa on SDS-PAGE under reducing conditions).AITR is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AITR protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
More Info
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Synonyms
TNFRSF18, AITR, CD357, GITR, GITR-D, Tumor necrosis factor receptor superfamily member 18, Activation-inducible TNFR family receptor, Glucocorticoid-induced TNFR-related protein, CD357, UNQ319/PRO364.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
QRPTGGPGCG PGRLLLGTGT DARCCRVHTT RCCRDYPGEE CCSEWDCMCV QPEFHCGDPC CTTCRHHPCP PGQGVQSQGK FSFGFQCIDC ASGTFSGGHE GHCKPWTDCT QFGFLTVFPG NKTHNAVCVP GSPPAEPLEH HHHHH.
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Background
AITR Human Recombinant: Unveiling its Role in Immune Regulation and Therapeutic Potential
1. Abstract
This research paper aims to provide a comprehensive exploration of the AITR Human Recombinant, a crucial receptor involved in immune regulation. By examining its structure, signaling pathways, biological functions, and implications in disease, we unravel the potential therapeutic applications of AITR in immune-related disorders.
2. Introduction
AITR, also known as TNFRSF18, is a receptor protein that plays a vital role in immune regulation. With its involvement in T-cell responses and immune tolerance, AITR has emerged as an intriguing target for therapeutic interventions in various immune-mediated conditions.
3. Structure and Signaling of AITR
AITR is a transmembrane receptor protein belonging to the tumor necrosis factor receptor superfamily. Its extracellular domain interacts with its ligand, glucocorticoid-induced TNFR-related protein (GITR) ligand, leading to downstream signaling events that modulate immune cell function.
4. Biological Functions of AITR
AITR activation influences T-cell responses by regulating T-cell activation, proliferation, and cytokine production. Additionally, AITR signaling can modulate the balance between effector and regulatory T-cell populations, thereby playing a role in immune tolerance and immune homeostasis.
5. AITR in Disease Pathology
AITR dysregulation has been associated with various immune-related disorders, including autoimmune diseases, cancer, and transplant rejection. Understanding the role of AITR in these pathologies may provide insights into potential therapeutic strategies targeting AITR signaling.
6. Therapeutic Potential of AITR
The unique role of AITR in immune regulation makes it an appealing target for therapeutic interventions. Modulation of AITR signaling holds promise for manipulating immune responses in the context of autoimmune diseases, cancer immunotherapy, and transplantation.
7. Conclusion and Future Perspectives
While our understanding of AITR and its functions has advanced significantly, further research is warranted to unravel its complex signaling pathways and therapeutic potential. Continued investigations into AITR biology will enhance our ability to develop targeted therapies for immune-related disorders.
What is the molecular weight/Mw of AITR Protein?
AITR Protein has a total Mw of 15.6kDa.
What is the source or expression system of AITR Protein?
Escherichia Coli.
What is the Purity of AITR Protein?
AITR Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of AITR Protein?
The biological functionality of AITR Protein will be determined in the future.
What is the amino acid sequence of AITR Protein?
QRPTGGPGCG PGRLLLGTGT DARCCRVHTT RCCRDYPGEE CCSEWDCMCV QPEFHCGDPC CTTCRHHPCP PGQGVQSQGK FSFGFQCIDC ASGTFSGGHE GHCKPWTDCT QFGFLTVFPG NKTHNAVCVP GSPPAEPLEH HHHHH.
What applications can AITR Protein be used in?
AITR Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for AITR Protein?
The endotoxin level is minimal, AITR Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MYBPC3 HumanDescription:
Myosin Binding Protein C, Cardiac Human Recombinant
Myosin Binding Protein C Cardiac, C-Protein Cardiac Muscle Isoform, Myosin-Binding Protein C Cardiac, Cardiac MyBP-C, CMD1MM, LVNC10, MYBP-C, CMH4, FHC, MYBPC3.
Product # :
PRO-2292Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
MYBPC3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Phe271) containing 281 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 29.6kDa.
Source
Escherichia Coli.
Formulation
MYBPC3 was filtered (0.4µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Myosin Binding Protein C, Cardiac (MYBPC3) is the cardiac isoform of myosin-binding protein C expressed exclusively in heart muscle. Myosin-binding protein C is a myosin-associated protein found in the cross-bridge-bearing zone (C region) of A bands in striated muscle. Regulatory phosphorylation of the cardiac isoform in vivo by cAMP-dependent protein kinase upon adrenergic stimulation may be associated with modulation of cardiac contraction. MYBPC3 gene mutations are one of the causes of familial hypertrophic cardiomyopathy. In vitro MYBPC3 binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. MYBPC3 may modulate muscle contraction or it may have a more structural role.
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Synonyms
Myosin Binding Protein C Cardiac, C-Protein Cardiac Muscle Isoform, Myosin-Binding Protein C Cardiac, Cardiac MyBP-C, CMD1MM, LVNC10, MYBP-C, CMH4, FHC, MYBPC3.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. MYBPC3 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASMPEPGKKPVS AFSKKPRSVE VAAGSPAVFE AETERAGVKV RWQRGGSDIS ASNKYGLATE GTRHTLTVRE VGPADQGSYA VIAGSSKVKF DLKVIEAEKA EPMLAPAPAP AEATGAPGEA PAPAAELGES APSPKGSSSA ALNGPTPGAP DDPIGLFVMR PQDGEVTVGG SITFSARVAG ASLLKPPVVK WFKGKWVDLS SKVGQHLQLH DSYDRASKVY LFELHITDAQ PAFTGSYRCE VSTKDKFDCS NFNLTVHEAM GTGDLDLLSA F.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Apo D HumanDescription:
Apolipoprotein-D Human Recombinant
Apolipoprotein D, Apo-D, ApoD.
Product # :
CYT-547Price :
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Shipping Method :
Shipped at Room temp
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Description
Apolipoprotein-D Human Recombinant His Tag fusion protein at C-terminus (7 highlighted a.a.) produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 174 amino acids and having a molecular mass of 19.82kDa. The protein a.a sequence corresponds to the UniProtKB/Swiss-Prot entry P05090.The Following gene modifications were made:Trp99His, Cys116Ser, Ile118Ser, Leu120Ser amino acids exchanges were introduced at the surface of Apolipoprotein-D to enhance the protein’s solubility and another three Leu23Pro, Pro133Val, Asn134Ala amino acids exchanges which facilitate its genetic manipulation. The Apolipoprotein-D is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 1mg/ml in 4mM KH2PO4, 16mM Na2HPO4 and 115mM NaCl pH 7.5.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Apolipoprotein-D is mainly associated with high density lipoproteins in human plasma. Apolipoprotein-D is an atypical apolipoprotein and, based on its primary structure, Apolipoprotein-D is a member of the lipocalin family. Lipocalins adopt a beta-barrel tertiary structure and transport small hydrophobic ligands. Apolipoprotein-D binds cholesterol, progesterone, pregnenolone, bilirubin and arachidonic acid.
Apolipoprotein-D is expressed in numerous tissues having high levels of expression in spleen, testes and brain. Apolipoprotein-D is present at high concentrations in the cyst fluid of women with gross cystic disease of the breast, a condition associated with increased risk of breast cancer. Apolipoprotein-D accumulates in regenerating peripheral nerves and in the cerebrospinal fluid of patients with neurodegenerative conditions, such as Alzheimer's disease. Apolipoprotein-D participates in maintenance and repair within the central and peripheral nervous systems. Apolipoprotein-D is a multi-ligand, multi-functional transporter and transports a ligand from 1 cell to another within an organ, scavenge a ligand within an organ for transport to the blood or could transport a ligand from the circulation to specific cells within a tissue. -
Synonyms
Apolipoprotein D, Apo-D, ApoD.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized H2O to a working volume of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter this product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
FHLGKCPNPP VQENFDVNKY PGRWYEIEKI PTTFENGRCI QANYSLMENG KIKVLNQELR ADGTVNQIEG EATPVNLTEP AKLEVKFSWF MPSAPYHILA TDYENYALVY SCTSISQSFH VDFAWILARN VALPPETVDS LKNILTSNNI DVKKMTVTDQ VNCPKLSAHHHHHH.
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Background
Apolipoprotein-D Human Recombinant: Illuminating the Role of a Multifaceted Lipid-Binding Protein
Abstract:
Apolipoprotein-D (ApoD), a multifunctional lipid-binding protein, has emerged as a fascinating player in lipid metabolism and neuroprotection. This research paper aims to provide an insightful overview of ApoD human recombinant, exploring its physiological functions, production methods, and potential therapeutic applications. By unraveling the complexities of ApoD, we gain valuable insights into its role in lipid homeostasis and its potential as a therapeutic target for neurodegenerative diseases. This article presents a concise yet comprehensive analysis of ApoD, humanizing its significance in the context of human health.Introduction:
Understanding the intricate mechanisms underlying lipid metabolism and neuroprotection is crucial for the development of novel therapeutic strategies. ApoD, a versatile protein expressed in various tissues, offers unique insights into these areas. This paper delves into the multifaceted nature of ApoD, shedding light on its significance in lipid homeostasis and neuronal health.Structure and Function of Apolipoprotein-D:
ApoD exhibits a complex molecular structure, comprising distinct domains that facilitate its binding to lipids and other biomolecules. It engages in diverse functions, including lipid transport, antioxidant defense, and modulation of neuroinflammatory responses. The versatility of ApoD underscores its pivotal role in maintaining cellular and tissue integrity.Regulation of Apolipoprotein-D Expression:
The expression of ApoD is subject to intricate regulatory mechanisms influenced by hormonal and environmental cues. Understanding the factors governing ApoD expression provides valuable insights into its physiological roles and potential therapeutic applications.Apolipoprotein-D and Neurodegenerative Diseases:
Growing evidence implicates ApoD in neuroprotection, particularly in the context of neurodegenerative diseases. ApoD exhibits neuroprotective properties by modulating oxidative stress, lipid peroxidation, and inflammatory responses, making it an intriguing target for therapeutic interventions.Production of Apolipoprotein-D Human Recombinant:
Advanced biotechnological approaches, including recombinant DNA technology and protein expression systems, enable the production of ApoD human recombinant. These methods facilitate large-scale production, purification, and characterization of ApoD, paving the way for potential therapeutic applications.Therapeutic Potential of Apolipoprotein-D Human Recombinant:
Targeting ApoD holds promise for the development of therapeutics aimed at neurodegenerative diseases. Modulating ApoD expression or function may provide neuroprotection, enhance neuronal survival, and mitigate the progression of neurodegenerative disorders.Conclusion:
Apolipoprotein-D human recombinant represents a captivating area of research, bridging the fields of lipid metabolism and neurodegeneration. Understanding the intricate interplay between ApoD, lipid homeostasis, and neuroprotection is crucial for unraveling its full therapeutic potential. Continued investigation into the functions and mechanisms of ApoD will likely lead to novel therapeutic strategies for neurodegenerative diseases.What is the molecular weight/Mw of APO D Protein?
APO D Protein has a total Mw of 19.82kDa.
What is the source or expression system of APO D Protein?
Escherichia Coli.
What is the Purity of APO D Protein?
APO D Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of APO D Protein?
The biological functionality of APO D Protein will be determined in the future.
What is the amino acid sequence of APO D Protein?
FHLGKCPNPP VQENFDVNKY PGRWYEIEKI PTTFENGRCI QANYSLMENG KIKVLNQELR ADGTVNQIEG EATPVNLTEP AKLEVKFSWF MPSAPYHILA TDYENYALVY SCTSISQSFH VDFAWILARN VALPPETVDS LKNILTSNNI DVKKMTVTDQ VNCPKLSAHHHHHH.
What applications can APO D Protein be used in?
APO D Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for APO D Protein?
The endotoxin level is minimal, APO D Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SOCS3 HumanDescription:
Suppressor Of Cytokine Signaling 3 Human Recombinant
Suppressor Of Cytokine Signaling 3, CIS3, SSI3, Cytokine-Inducible SH2 Protein 3, STAT-Induced STAT Inhibitor 3, ATOD4, Cish3, MGC71791, CIS-3.
Product # :
PRO-1891Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SOCS3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 262 amino acids (1-225 a.a) and having a molecular mass of 29kDa.SOCS3 is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SOCS3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Suppressor of Cytokine Signaling 3, also known as SOCS3 belongs to the SOCS family; in addition SOCS3 is a member of the STAT-induced STAT inhibitor (SSI). The SSI family members are cytokine-inducible negative regulators of cytokine signaling. The expression of SOCS3 is induced by different cytokines, including IL6 and IL10. SOCS3 can bind to JAK2 kinase, and inhibit the activity of JAK2 kinase. Studies of the mouse counterpart of SOCS3 have shown the roles of SOCS3 in the negative regulation of fetal liver hematopoiesis, and placental development.
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Synonyms
Suppressor Of Cytokine Signaling 3, CIS3, SSI3, Cytokine-Inducible SH2 Protein 3, STAT-Induced STAT Inhibitor 3, ATOD4, Cish3, MGC71791, CIS-3.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMVT HSKFPAAGMS RPLDTSLRLK TFSSKSEYQL VVNAVRKLQE SGFYWSAVTG GEANLLLSAE PAGTFLIRDS SDQRHFFTLS VKTQSGTKNL RIQCEGGSFS LQSDPRSTQP VPRFDCVLKL VHHYMPPPGA PSFPSPPTEP SSEVPEQPSA QPLPGSPPRR AYYIYSGGEK IPLVLSRPLS SNVATLQHLC RKTVNGHLDS YEKVTQLPGP IREFLDQYDA PL
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
STIP1 Human, HisDescription:
Stress-Induced-Phosphoprotein 1 Human Recombinant, His Tag
HOP, P60, STI1, STI1L, IEF-SSP-3521, STIP1, Stress-induced-phosphoprotein 1, Hsc70/Hsp90-organizing protein, Transformation-sensitive protein IEF SSP 3521, Renal carcinoma antigen NY-REN-11.
Product # :
PRO-753Price :
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Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human STIP1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 563 amino acids (1-543 a.a) and having a molecular mass of 64.8kDa. STIP1 is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The STIP1 protein solution (1mg/ml) contains 20mM Tris-HCl, pH-8, 1mM DTT, 1mM EDTA, 0.2mM PMSF and 20% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
STIP1 is an adaptor protein that mediates the functions of HSP70 & HSP90 in protein folding. STIP1 supports the transfer of proteins from HSP70 to HSP90 by binding together HSP90 and substrate-bound HSP70. STIP1 stimulates the ATPase activity of HSP70 and inhibits the ATPase activity of HSP90, suggesting that it regulates both the conformations and ATPase cycles of these chaperones. STIP1 genetic variations are involved in regulating corticosteroid response in asthmatic subjects with reduced lung function.
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Synonyms
HOP, P60, STI1, STI1L, IEF-SSP-3521, STIP1, Stress-induced-phosphoprotein 1, Hsc70/Hsp90-organizing protein, Transformation-sensitive protein IEF SSP 3521, Renal carcinoma antigen NY-REN-11.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEQVNELKEK GNKALSVGNI DDALQCYSEA IKLDPHNHVL YSNRSAAYAK KGDYQKAYED GCKTVDLKPDWGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNPQLKE GLQNMEARLA ERKFMNPFNM PNLYQKLESD PRTRTLLSDP TYRELIEQLRNKPSDLGTKL QDPRIMTTLS VLLGVDLGSM DEEEEIATPP PPPPPKKETK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD FDTALKHYDKAKELDPTNMT YITNQAAVYF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA KAYARIGNSY FKEEKYKDAI HFYNKSLAEH TPDVLKKCQQAEKILKEQE RLAYINPDLA LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PKDAKLYSNR AACYTKLLEF QLALKDCEEC QLEPTFIKGYTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI AIR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CRHBP HumanDescription:
Corticotropin Releasing Hormone Binding Protein Human Recombinant
Corticotropin releasing hormone binding protein, CRF-BP, CRH-BP, CRF-binding protein.
Product # :
HOR-267Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
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Description
CRHBP Human Recombinant is a 34.58 kDa protein containing 308 aa and fused to a 10 aa N-Terminal His-tag. CRHBP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CRHBP Human was filtered (0.4µm) and lyophilized from 0.5mg/ml supplied in 20mM TRIS and 20mM NaCl, pH 7.5.
More Info
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Introduction
CRH is a powerful stimulator of synthesis and secretion of preopiomelanocortin-derived peptides. CRH concentration in the human peripheral circulation is usually low. The concentration rises during pregnancy and fall back quickly after parturition. Maternal plasma CRH most likely originates from the placenta. Human plasma has a CRH-binding protein that inactivates CRH and can inhibit inappropriate pituitary-adrenal stimulation in pregnancy.
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Synonyms
Corticotropin releasing hormone binding protein, CRF-BP, CRH-BP, CRF-binding protein.
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Physical Appearance
Filtered white lyophilized powder.
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Stability
Store lyophilized protein at -20°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at -80°C for long term storage. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after one week at 4°C.
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Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS YLELREAADY DPFLLFSANL KRELAGEQPY RRALRCLDML SLQGQFTFTA DRPQLHCAAF FISEPEEFIT IHYDQVSIDC QGGDFLKVFD GWILKGEKFP SSQDHPLPSA ERYIDFCESG LSRRSIRSSQ NVAMIFFRVH EPGNGFTLTI KTDPNLFPCN VISQTPNGKF TLVVPHQHRN CSFSIIYPVV IKISDLTLGH VNGLQLKKSS AGCEGIGDFV ELLGGTGLDP SKMTPLADLC YPFHGPAQMK VGCDNTVVRM VSSGKHVNRV TFEYRQLEPY ELENPNGNSI GEFCLSGL YLELREAADY DPFLLFSANL KRELAGEQPY RRALRCLDML SLQGQFTFTA DRPQLHCAAF FISEPEEFIT IHYDQVSIDC QGGDFLKVFD GWILKGEKFP SSQDHPLPSA ERYIDFCESG LSRRSIRSSQ NVAMIFFRVH EPGNGFTLTI KTDPNLFPCN VISQTPNGKF TLVVPHQHRN CSFSIIYPVV IKISDLTLGH VNGLQLKKSS AGCEGIGDFV ELLGGTGLDP SKMTPLADLC YPFHGPAQMK VGCDNTVVRM VSSGKHVNRV TFEYRQLEPY ELENPNGNSI GEFCLSGL
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Applications
ELISA, Western blotting
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
APP HumanDescription:
Amyloid beta (A4) Precursor Protein Human Recombinant
Amyloid beta A4 protein, ABPP, APPI, APP, Alzheimer disease amyloid protein, Cerebral vascular amyloid peptide, CVAP, PreA4, Protease nexin-II, PN-II, APP, A4, AD1, AAA, PN2, ABETA, CTFgamma.
Product # :
PRO-1080Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
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Description
APP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (18-289 a.a) and having a molecular mass of 34.7kDa (Molecular size on SDS-PAGE will appear higher).APP is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
APP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Amyloid beta A4 protein (APP) functions as a cell surface receptor and transmembrane precursor protein which is cleaved by secretases to form a number of peptides. A number of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to stimulate transcriptional activation, whereas others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. APP gene mutations are implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy).
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Synonyms
Amyloid beta A4 protein, ABPP, APPI, APP, Alzheimer disease amyloid protein, Cerebral vascular amyloid peptide, CVAP, PreA4, Protease nexin-II, PN-II, APP, A4, AD1, AAA, PN2, ABETA, CTFgamma.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSLEVP TDGNAGLLAE PQIAMFCGRL NMHMNVQNGK WDSDPSGTKT CIDTKEGILQ YCQEVYPELQ ITNVVEANQP VTIQNWCKRG RKQCKTHPHF VIPYRCLVGE FVSDALLVPD KCKFLHQERM DVCETHLHWH TVAKETCSEK STNLHDYGML LPCGIDKFRG VEFVCCPLAE ESDNVDSADA EEDDSDVWWG GADTDYADGS EDKVVEVAEE EEVAEVEEEE ADDDEDDEDG DEVEEEAEEP YEEATERTTS IATTTTTTTE SVEEVVRE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NEK7 HumanDescription:
NIMA-related kinase 7 Human Recombinant
NIMA (never in mitosis gene a)-related kinase 7, Serine/threonine-protein kinase Nek7.
Product # :
PKA-044Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NEK7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 326 amino acids (1-302 a.a) and having a molecular mass of 37kDa.NEK7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NEK7 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) , 0.15M NaCl and 20% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
NEK7, protein kinase, has a vital role in mitotic cell cycle progression. It is essential for microtubule nucleation activity of the centrosome, robust mitotic spindle formation and cytokinesis. NEK7 is greatly expressed in lung, muscle, testis, brain, heart, liver, leukocyte and spleen.
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Synonyms
NIMA (never in mitosis gene a)-related kinase 7, Serine/threonine-protein kinase Nek7.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMDEQSQ GMQGPPVPQF QPQKALRPDM GYNTLANFRI EKKIGRGQFS EVYRAACLLD GVPVALKKVQ IFDLMDAKAR ADCIKEIDLL KQLNHPNVIK YYASFIEDNE LNIVLELADA GDLSRMIKHF KKQKRLIPER TVWKYFVQLC SALEHMHSRR VMHRDIKPAN VFITATGVVK LGDLGLGRFF SSKTTAAHSL VGTPYYMSPE RIHENGYNFK SDIWSLGCLL YEMAALQSPF YGDKMNLYSL CKKIEQCDYP PLPSDHYSEE LRQLVNMCIN PDPEKRPDVT YVYDVAKRMH ACTASS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SNPH HumanDescription:
Syntaphilin Human Recombinant
KIAA0374, MGC46096, bA314N13.5, SNPH, Syntaphilin.
Product # :
PRO-545Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
SNPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 444 amino acids (1-424) and having a molecular mass of 48.2 kDa.The SNPH is fused to 20 amino acid His-Tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The Syntaphilin protein solution contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Syntaxin-1, synaptobrevin, and SNAP25 cooperate to form the SNARE complex, which is needed for synaptic vesicle docking and fusion SNPH is a neuron-specific protein originally characterized as a binding partner of syntaxin-1. SNPH participates with SNAP25 for the binding to Syntaxin-1 and prevents the construction of the SNARE core complex, thus manageling free syntaxin-1 availability for the assembly of the SNARE complex and potentially regulating synaptic vesicle exocytosis. Expression Syntaphilin appears to be brain-specific. SNPH is an inhibitor of both SNARE-based fusion and dynamin-mediated endocytosis.
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Synonyms
KIAA0374, MGC46096, bA314N13.5, SNPH, Syntaphilin.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAMSLPGSRR TSAGSRRRTS PPVSVRDAYG TSSLSSSSNS GSYKGSDSSP TPRRSMKYTL CSDNHGIKPPTPEQYLTPLQ QKEVCIRHLK ARLKDTQDRL QDRDTEIDDL KTQLSRMQED WIEEECHRVE AQLALKEARK EIKQLKQVID TVKNNLIDKDKGLQKYFVDI NIQNKKLETL LHSMEVAQNG MAKEDGTGES AGGSPARSLT RSSTYTKLSD PAVCGDRQPG DPSSGSAEDG ADSGFAAADD
TLSRTDALEA SSLLSSGVDC GTEETSLHSS FGLGPRFPAS NTYEKLLCGM EAGVQASCMQ ERAIQTDFVQ YQPDLDTILE KVTQAQVCGTDPESGDRCPE LDAHPSGPRD PNSAVVVTVG DELEAPEPIT RGPTPQRPGA NPNPGQSVSV VCPMEEEEEA AVAEKEPKSY WSRH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.