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1000 results found for “hbsag”
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Name :
IDE Human, ActiveDescription:
Insulin-Degrading Enzyme Human Recombinant
Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulysin, EC 3.4.24.56, Insulinase, Insulin Protease, INSULYSIN, EC 3.4.24, IDE, insulin-degrading enzyme isoform 1.
Product # :
ENZ-1192Price :
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Description
IDE Human, Active Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (42-1019 a.a) containing a total of 984 amino acids, having a molecular mass of 114 kDa. IDE is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IDE solution (0.5mg/ml) contains 10% Glycerol, 100mM NaCl, 0.05% Brij35 and 20mM Tris-HCl buffer (pH 7.5).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is greater than 3,000 pmol/min/ug in which 1 unit will convert 1.0 pmole of Mca-RPPGFSAFK(Dnp)-OH to MCA-Pro-Leu-OH per minute at pH 7.5 at 25°C.
Citations
More Info
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Synonyms
Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulysin, EC 3.4.24.56, Insulinase, Insulin Protease, INSULYSIN, EC 3.4.24, IDE, insulin-degrading enzyme isoform 1.
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Physical Appearance
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
MNNPAIKRIG NHITKSPEDK REYRGLELAN GIKVLLISDP TTDKSSAALD VHIGSLSDPP NIAGLSHFCE HMLFLGTKKY PKENEYSQFL SEHAGSSNAF TSGEHTNYYF DVSHEHLEGA LDRFAQFFLC PLFDESCKDR EVNAVDSEHE KNVMNDAWRL FQLEKATGNP KHPFSKFGTG NKYTLETRPN QEGIDVRQEL LKFHSAYYSS NLMAVCVLGR ESLDDLTNLV VKLFSEVENK NVPLPEFPEH PFQEEHLKQL YKIVPIKDIR NLYVTFPIPD LQKYYKSNPG HYLGHLIGHE GPGSLLSELK SKGWVNTLVG GQKEGARGFM FFIINVDLTE EGLLHVEDII LHMFQYIQKL RAEGPQEWVF QECKDLNAVA FRFKDKERPR GYTSKIAGIL HYYPLEEVLT AEYLLEEFRP DLIEMVLDKL RPENVRVAIV SKSFEGKTDR TEEWYGTQYK QEAIPDEVIK KWQNADLNGK FKLPTKNEFI PTNFEILPLE KEATPYPALI KDTAMSKLWF KQDDKFFLPK ACLNFEFFSP FAYVDPLHCN MAYLYLELLK DSLNEYAYAA ELAGLSYDLQ NTIYGMYLSV KGYNDKQPIL LKKIIEKMAT FEIDEKRFEI IKEAYMRSLN NFRAEQPHQH AMYYLRLLMT EVAWTKDELK EALDDVTLPR LKAFIPQLLS RLHIEALLHG NITKQAALGI MQMVEDTLIE HAHTKPLLPS
QLVRYREVQL PDRGWFVYQQ RNEVHNNCGI EIYYQTDMQS TSENMFLELF CQIISEPCFN TLRTKEQLGY IVFSGPRRAN GIQGLRFIIQ SEKPPHYLES RVEAFLITME KSIEDMTEEA FQKHIQALAI RRLDKPKKLS AECAKYWGEI ISQQYNFDRD NTEVAYLKTL TKEDIIKFYK EMLAVDAPRR HKVSVHVLAR EMDSCPVVGE FPCQNDINLS QAPALPQPEV IQNMTEFKRG LPLFPLVKPH INFMAAKLHH HHHH. -
Background
Insulin-degrading enzyme (IDE) is a crucial protease that plays a significant role in maintaining glucose homeostasis by degrading insulin and other bioactive peptides. Dysregulation of IDE has been implicated in various metabolic disorders, particularly type 2 diabetes mellitus. IDE is also associated with the clearance of amyloid-beta peptides in the brain, making it relevant to Alzheimer's disease pathology. Studying the recombinant form of IDE is fundamental to understanding its functional mechanisms and exploring potential avenues for therapeutic interventions.
The primary goal of this research is to express and purify recombinant IDE using diverse expression systems. Recombinant DNA techniques will be employed to construct expression vectors containing the IDE gene, followed by expression in bacterial, yeast, or mammalian cell-based systems. The recombinant IDE will be purified using affinity chromatography or other appropriate methods, facilitating subsequent biochemical and biophysical characterization.
The second objective is to investigate the substrate specificity and catalytic activity of the purified IDE. In vitro enzymatic assays will be conducted to analyse the ability of the recombinant IDE to degrade insulin and other potential substrates. The effects of various factors, such as pH, temperature, and potential modulators, on IDE activity will be evaluated. Additionally, the interactions between IDE and its substrates will be explored using binding assays.
The third objective is to elucidate the three-dimensional structure of the IDE recombinant using techniques like X-ray crystallography or nuclear magnetic resonance (NMR) spectroscopy. Structural insights into the active site and binding pockets of IDE will provide valuable information for understanding its substrate recognition and catalytic mechanisms. This knowledge could be instrumental in designing targeted therapeutic compounds.
By characterizing the IDE recombinant, this research aims to contribute to our understanding of its role in insulin metabolism, glucose regulation, and potential therapeutic applications. The findings from this study may have implications for the development of novel treatments for diabetes and other related disorders.
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 :
TBEV gE middleDescription:
Tick-Borne Encephalitis Virus gE Middle Recombinant
Product # :
TBE-283Price :
Quantity :
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Shipped at Room temp
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Description
The E.coli derived recombinant protein contains the Tick-borne Encephalitis Virus glycoprotein E middle regions, 50-250 amino acids.
Source
Escherichia Coli.
Formulation
20mM MES pH 6.5, 8M urea, 200mM NaCl and 0.05% Tween-20.
Purity
Encephalitis protein is >95% pure as determined by 10% PAGE (coomassie staining).
Citations
More Info
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Introduction
TBE is caused by tick-borne encephalitis virus (TBEV), a member of the family Flaviviridae.
A closely related virus in Far Eastern Eurasia, Russian spring-summer encephalitis virus (RSSEV).
The family Flaviviridae includes other tick-borne viruses are closely related to TBEV and RSSEV, such as Omsk hemorrhagic fever virus & Kyasanur Forest virus.
Louping ill virus is also a member of this family. -
Physical Appearance
Sterile Filtered clear solution.
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Stability
Encephalitis protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
Encephalitis antigen is suitable for ELISA and Western blots, excellent antigen for detection of Tick-borne encephalitis virus with minimal specificity problems.
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Specificity
Immunoreactive with sera of encephalitis virus infected individuals.
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Purification Method
Encephalitis 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 :
ABHD10 HumanDescription:
Abhydrolase Domain Containing 10 Human Recombinant
Abhydrolase domain containing 10 mitochondrial2, FLJ11342, EC 3.4.-.-.
Product # :
ENZ-612Price :
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Description
ABHD10 Human Recombinant produced in E. coli is a single polypeptide chain containing 279 amino acids (53-306) and having a molecular mass of 30.9kDa.ABHD10 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ABHD10 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 100mM NaCl and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Abhydrolase domain-containing protein 10 (ABHD10) is a member of the AB hydrolase superfamily.
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Synonyms
Abhydrolase domain containing 10 mitochondrial2, FLJ11342, EC 3.4.-.-.
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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 MGSHMTSLSF LNRPDLPNLA YKKLKGKSPG IIFIPGYLSY MNGTKALAIE EFCKSLGHAC IRFDYSGVGS SDGNSEESTL GKWRKDVLSI IDDLADGPQI LVGSSLGGWL MLHAAIARPE KVVALIGVAT AADTLVTKFN QLPVELKKEV EMKGVWSMPS KYSEEGVYNV QYSFIKEAEH HCLLHSPIPV NCPIRLLHGM KDDIVPWHTS MQVADRVLST DVDVILRKHS DHRMREKADI QLLVYTIDDL IDKLSTIVN
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 :
SCGB1A1 MouseDescription:
Uteroglobin Mouse Recombinant
Uteroglobin, Clara cell 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.
Product # :
CYT-746Price :
Quantity :
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Shipped at Room temp
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Description
Uteroglobin Mouse Recombinant produced in E.coli is a non-glycosylated disulfide-linked homodimeric protein containing 2x75 amino acids chains and having a molecular mass of 16.7kDa.The SCGB1A1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Uteroglobin protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the ability of the immobilized protein to support the adhesion of the A549 human lung carcinoma cells is less than 5.0µg/ml, corresponding to a specific activity of > 200 IU/mg.Citations
More Info
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Introduction
Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.
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Synonyms
Uteroglobin, Clara cell 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Uteroglobin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCGB1A1 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 SCGB1A1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
DICPGFLQVL EALLMESESG YVASLKPFNP GSDLQNAGTQ LKRLVDTLPQ ETRINIMKLT EKILTSPLCK QDLRF.
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 :
UBE2R2 HumanDescription:
Ubiquitin Conjugating Enzyme E2R 2 Human Recombinant
CDC34B, E2-CDC34B, UBC3B, Ubiquitin carrier protein R2, Ubiquitin-conjugating enzyme E2-CDC34B, Ubiquitin-protein ligase R2, Ubiquitin-conjugating enzyme E2 R2, EC 6.3.2.19.
Product # :
ENZ-511Price :
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Shipped with Ice Packs
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Description
UBE2R2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 261 amino acids (1-238 a.a) and having a molecular mass of 29.6kDa (Molecular size on SDS-PAGE will appear higher).UBE2R2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UBE2R2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Ubiquitin-conjugating enzyme E2 R2 (UBE2R2) is a member of the ubiquitin-conjugating enzyme family. Protein kinase CK2 is a ubiquitous and pleiotropic Ser/Thr protein kinase implicated in cell growth andtransformation. This protein is a protein similar to the E2 ubiquitin conjugating enzyme UBC3/CDC34. Studies propose that CK2-dependent phosphorylation of this ubiquitin-conjugating enzyme functions by regulating beta-TrCP substrate recognition and induces its interaction with beta-TrCP, enhancing beta-catenin degradation. UBE2R2 receives ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes monoubiquitination and 'Lys-48'-linked polyubiquitination. UBE2R2 may be implicated in degradation of katenin. Among the diseases associated with UBE2R2 are cblc, and herpes simplex.
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Synonyms
CDC34B, E2-CDC34B, UBC3B, Ubiquitin carrier protein R2, Ubiquitin-conjugating enzyme E2-CDC34B, Ubiquitin-protein ligase R2, Ubiquitin-conjugating enzyme E2 R2, EC 6.3.2.19.
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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 MGSMAQQQMT SSQKALMLEL KSLQEEPVEG FRITLVDESD LYNWEVAIFG PPNTLYEGGY FKAHIKFPID YPYSPPTFRF LTKMWHPNIY ENGDVCISIL HPPVDDPQSG ELPSERWNPT QNVRTILLSV ISLLNEPNTF SPANVDASVM FRKWRDSKGK DKEYAEIIRK QVSATKAEAE KDGVKVPTTL AEYCIKTKVP SNDNSSDLLY DDLYDDDIDD EDEEEEDADC YDDDDSGNEE S
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 :
ADH1C Human, sf9Description:
Alcohol Dehydrogenase 1C, Human Recombinant, sf9
ADH1, ADH1C, ADH3, Alcohol dehydrogenase 1C, Alcohol dehydrogenase subunit gamma.
Product # :
ENZ-1010Price :
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Description
ADH1C Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 381 amino acids (1-375) and having a molecular mass of 40.6kDa. ADH1C is fused to a 6 amino acid IgG His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ADH1C protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Citations
More Info
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Introduction
ADH1C is a member of the zinc-containing alcohol dehydrogenase family which metabolizes a large assortment of substrates, such as ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH1 is a monomorphic and a key factor in fetal and infant livers, becoming less active in gestation and only weakly active during adulthood.
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Synonyms
ADH1, ADH1C, ADH3, Alcohol dehydrogenase 1C, Alcohol dehydrogenase subunit gamma.
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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
MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAAGICRSD EHVVSGNLVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLFTPQCGK CRICKNPESN YCLKNDLGNP RGTLQDGTRR FTCSGKPIHH FVGVSTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG YGSAVKVAKV TPGSTCAVFG LGGVGLSVVM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ NLSINPMLLL TGRTWKGAIF GGFKSKESVP KLVADFMAKK FSLDALITNI LPFEKINEGF DLLRSGKSIR
TVLTFHHHHH H.
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 :
HEPACAM2 HumanDescription:
HEPACAM2 Human Recombinant
HEPACAM family member 2 isoform 1, MIKI, HEPACAM family member 2, Mitotic kinetics regulator, HEPACAM2, UNQ305/PRO346.
Product # :
PRO-1672Price :
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Description
HEPACAM2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (32-351) and having a molecular mass of 37.9 kDa.HEPACAM2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HEPACAM2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HEPACAM2 is necessary during prometaphase for centrosome maturation. Following poly-ADP-ribosylation (PARsylation) by TNKS, HEPACAM2 translocates from the Golgi apparatus to mitotic centrosomes and takes a significant part in the formation of robust microtubules for quick movement of chromosomes.
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Synonyms
HEPACAM family member 2 isoform 1, MIKI, HEPACAM family member 2, Mitotic kinetics regulator, HEPACAM2, UNQ305/PRO346.
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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 MGSLKVTVPS HTVHGVRGQA LYLPVHYGFH TPASDIQIIW LFERPHTMPK YLLGSVNKSV VPDLEYQHKF TMMPPNASLL INPLQFPDEG NYIVKVNIQG NGTLSASQKI QVTVDDPVTK PVVQIHPPSG AVEYVGNMTL TCHVEGGTRL AYQWLKNGRP VHTSSTYSFS PQNNTLHIAP VTKEDIGNYS CLVRNPVSEM ESDIIMPIIY YGPYGLQVNS DKGLKVGEVF TVDLGEAILF DCSADSHPPN TYSWIRRTDN TTYIIKHGPR LEVASEKVAQ KTMDYVCCAY NNITGRQDET HFTVIITSVG LEKLAQKGKS LSP.
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 :
HP-NAPDescription:
Neutrophil-activating protein A Helicobacter Pylori Recombinant
DNA protection during starvation protein, Bacterioferritin, HP-NAP, Neutrophil-activating protein A, NAP A, dps, napA.
Product # :
PRO-2035Price :
Quantity :
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Shipped at Room temp
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Description
HP-NAP Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Ala144) containing 154 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 18.2kDa.
Source
Escherichia Coli.
Formulation
HP-NAP was filtered (0.4 µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HP-NAP protects DNA from oxidative damage by sequestering intracellular Fe2+ ion and storing it in the form of Fe3+ oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe2+ ions, thus preventing hydroxyl radical production by the Fenton reaction. HP-NAP is necessary for the survival in the presence of oxidative stress. Dps is also a virulence factor which activates neutrophils, mast cells and monocytes. HP-NAP binds to neutrophil-glycosphingolipids and to sulfated carbohydrates on mucin. HP-NAP might play a part in the accumulation of neutrophils and monocytes at the site of infection. HP-NAP induces superoxide anion generation, adhesion and chemotaxis of neutrophils, via a pertussis toxin-sensitive pathway involving MAP kinases.
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Synonyms
DNA protection during starvation protein, Bacterioferritin, HP-NAP, Neutrophil-activating protein A, NAP A, dps, napA.
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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. HP-NAP 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
MKHHHHHHASMKTFEILKHL QADAIVLFMK VHNFHWNVKG TDFFNVHKAT EEIYEEFADM FDDLAERIVQ LGHHPLVTLS EAIKLTRVKE ETKTSFHSKD IFKEILEDYK YLEKEFKELS NTAEKEGDKV TVTYADDQLA KLQKSIWMLQ AHLA.
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 :
IBSP Human, HEKDescription:
Integrin Binding Sialoprotein Human Recombinant, HEK
Integrin Binding Sialoprotein, Integrin-Binding Sialoprotein, Bone Sialoprotein II, Cell-Binding Sialoprotein, BSP II , BNSP, Bone Sialoprotein, BSP-II, SP-II, BSP.
Product # :
PRO-2793Price :
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Description
IBSP Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain (17-317 a.a) containing a total of 307 amino acids and having a molecular mass of 34.3 kDa. IBSP is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The IBSP solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
>40%, measured by the ability of the immobilized protein to support the adhesion of MCF7 human breast cancer cells. When cells are added to Human IBSP coated plates 3 ug/ml.
Citations
More Info
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Synonyms
Integrin Binding Sialoprotein, Integrin-Binding Sialoprotein, Bone Sialoprotein II, Cell-Binding Sialoprotein, BSP II , BNSP, Bone Sialoprotein, BSP-II, SP-II, BSP.
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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
FSMKNLHRRV KIEDSEENGV FKYRPRYYLY KHAYFYPHLK RFPVQGSSDS SEENGDDSSE EEEEEEETSN EGENNEESNE DEDSEAENTT LSATTLGYGE DATPGTGYTG LAAIQLPKKA GDITNKATKE KESDEEEEEE EEGNENEESE AEVDENEQGI NGTSTNSTEA ENGNGSSGGD NGEEGEEESV TGANAEDTTE TGRQGKGTSK TTTSPNGGFE PTTPPQVYRT TSPPFGKTTT
VEYEGEYEYT GANEYDNGYE IYESENGEPR GDNYRAYEDE YSYFKGQGYD GYDGQNYYHH QHHHHHH. -
Background
1. Structural Diversity: Research on IBSP often delves into its structural characteristics. IBSP is known for its rich sialic acid content and multiple functional domains, including an RGD cell-binding domain and polyglutamic acid stretches. These structural features enable IBSP to interact with various cells, affecting adhesion and migration.
2. Mineralization Regulator: A significant focus of research is IBSP's role in mineralization. It acts as a nucleator for calcium phosphate crystals, providing a scaffold for bone formation. Understanding how IBSP influences mineralization is crucial for insights into bone health and diseases like osteoporosis.
3. Cell Signaling: Research papers explore IBSP's involvement in cell signaling pathways. IBSP has been linked to angiogenesis, inflammation, and cellular differentiation. Investigating these signaling pathways sheds light on its broader physiological roles.
4. Biomedical Implications: Studies often discuss the biomedical implications of IBSP. Researchers investigate its potential roles in bone disorders such as osteoporosis and periodontal disease. Additionally, IBSP's involvement in tumor metastasis and dental tissue regeneration is a subject of interest.
5. Recombinant IBSP: The use of recombinant IBSP in research is a significant topic. Researchers utilize recombinant IBSP to explore its functions, interactions, and potential therapeutic applications. This allows for controlled experiments and insights into IBSP's behavior.
6. Diagnostics and Therapeutics: Research papers may discuss the diagnostic and therapeutic potential of IBSP. Understanding its roles in health and disease can lead to the development of diagnostic markers and therapeutic interventions, particularly in the context of bone and dental health.
7. Clinical Relevance: Some research may focus on the clinical relevance of IBSP. This could include studies on patient populations with IBSP mutations or alterations, aiming to understand how variations in IBSP may contribute to specific medical conditions.
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 :
BCAT2 HumanDescription:
Branched Chain Amino-Acid Transaminase 2 Human Recombinant
Branched-chain-amino-acid aminotransferase mitochondrial, BCAT(m), Placental protein 18, PP18, BCAT2, BCATM, BCT2, ECA40, BCAM.
Product # :
ENZ-606Price :
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Shipped with Ice Packs
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Description
BCAT2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (28-392) and having a molecular mass of 43.9kDa.BCAT2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BCAT2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 10% glycerol, 0.2M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Branched Chain Amino-Acid Transaminase 2 (BCAT2) is a member of the class-IV pyridoxal-phosphate-dependent aminotransferase family. BCAT2 is a branched chain aminotransferase found in mitochondria. BCAT2 forms a dimer which catalyzes the first step in the production of the branched chain amino acids leucine, isoleucine, and valine. In addition, BCAT2 may actn as a transporter of branched chain alpha-keto acids.
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Synonyms
Branched-chain-amino-acid aminotransferase mitochondrial, BCAT(m), Placental protein 18, PP18, BCAT2, BCATM, BCT2, ECA40, BCAM.
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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 MGSHMASSSF KAADLQLEMT QKPHKKPGPG EPLVFGKTFT DHMLMVEWND KGWGQPRIQP FQNLTLHPAS SSLHYSLQLF EGMKAFKGKD QQVRLFRPWL NMDRMLRSAM RLCLPSFDKL ELLECIRRLI EVDKDWVPDA AGTSLYVRPV LIGNEPSLGV SQPTRALLFV ILCPVGAYFP GGSVTPVSLL ADPAFIRAWV GGVGNYKLGG NYGPTVLVQQ EALKRGCEQV LWLYGPDHQL TEVGTMNIFV YWTHEDGVLE LVTPPLNGVI LPGVVRQSLL DMAQTWGEFR VVERTITMKQ LLRALEEGRV REVFGSGTAC QVCPVHRILY KDRNLHIPTM ENGPELILRF QKELKEIQYG IRAHEWMFPV.
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 :
BTC Human, HEKDescription:
Betacellulin Human Recombinant, HEK
Betacellulin isoform 1, Probetacellulin, Betacellulin, BTC
Product # :
CYT-1188Price :
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Description
BTC Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (32-111 a.a) containing 86 amino acids and having a molecular mass of 9.8kDa.BTC is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
BTC protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
ED50 range is ≤ 0.5ng/ml. It is measured by cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells.
Citations
More Info
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Introduction
BTC is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are mediated by the EGF receptor and other related receptors.
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Synonyms
Betacellulin isoform 1, Probetacellulin, Betacellulin, BTC
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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
DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY HHHHHH
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Background
What is the molecular weight/Mw of BETACELLULIN Protein?
BETACELLULIN Protein has a total Mw of 9.8kDa.
What is the source or expression system of BETACELLULIN Protein?
HEK293 cells.
What is the Purity of BETACELLULIN Protein?
BETACELLULIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BETACELLULIN Protein?
ED50 range is ≤ 0.5ng/ml. It is measured by cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells.
What is the amino acid sequence of BETACELLULIN Protein?
DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY HHHHHH
What applications can BETACELLULIN Protein be used in?
BETACELLULIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BETACELLULIN Protein?
The endotoxin level is minimal, BETACELLULIN 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 :
CHGA Human, HisDescription:
Chromogranin-A Human Recombinant, His Tag
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
Product # :
PRO-699Price :
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Description
Recombinant Human CHGA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 460 amino acids (19-457 a.a) and having a molecular mass of 51.2kDa (Molecular weight on SDS-PAGE will appear higher). Chromgranin-A is fused to 21 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CHGA protein (0.5mg/ml) contains 20mM Tris-HCl buffer pH-7.5, 2mM EDTA, 0.1mM PMSF and 10% glycerol.
Purity
Greater than 80.0% as determined by Analysis by SDS-PAGE.
Citations
More Info
-
Introduction
Chromgranin-A is part of the neuroendocrine secretory protein family. CHGA is located in secretory vesicles of neurons and endocrine cells. Chromgranin-A is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Other peptides, including chromostatin, beta-granin, WE-14 and GE-25, are also derived from the full-length protein. Chromgranin-A has numerous biological activities on some tissues and organs and exerts a large spectrum of homeostatic actions, including antifungal and antimicrobial effect, modulation of cell adhesion, and inhibition of parathyroid hormone secretion.
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Synonyms
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
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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 MLPVNSPMNK GDTEVMKCIV EVISDTLSKP SPMPVSQECF ETLRGDERIL SILRHQNLLK ELQDLALQGA KERAHQQKKH SGFEDELSEV LENQSSQAEL KEAVEEPSSK DVMEKREDSK EAEKSGEATD GARPQALPEP MQESKAEGNN QAPGEEEEEE EEATNTHPPA SLPSQKYPGP QAEGDSEGLS QGLVDREKGL SAEPGWQAKR EEEEEEEEEA EAGEEAVPEE EGPTVVLNPH PSLGYKEIRK GESRSEALAV DGAGKPGAEE AQDPEGKGEQ EHSQQKEEEE EMAVVPQGLF RGGKSGELEQ EEERLSKEWE DSKRWSKMDQ LAKELTAEKR LEGQEEEEDN RDSSMKLSFR ARAYGFRGPG PQLRRGWRPS SREDSLEAGL PLQVRGYPEE KKEEEGSANR RPEDQELESL SAIEAELEKV AHQLQALRRG.
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 :
PRSS3 Human, HEKDescription:
Protease Serine 3 Human Recombinant, HEK
Protease, Serine, 3, Protease, Serine, 4 (Trypsin 4, Brain), Brain Trypsinogen, Mesotrypsinogen, Mesotrypsin, Trypsin III, EC 3.4.21.4 4, Trypsin IV, PRSS4, TRY3, TRY4 Protease, Serine, 3 (Mesotrypsin), Pancreatic Trypsinogen III, Serine Protease 3, Serine Protease 4, Trypsinogen IV, Trypsinogen 4, Trypsinogen 5, EC 3.4.21, MTG, T9.
Product # :
ENZ-1194Price :
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Description
PRSS3 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 238 amino acids (16-247 a.a.) and having a molecular mass of 26kDa. PRSS3 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
PRSS3 protein solution (1mg/ml) containing 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 10,000pmol/min/ug, and is defined as the amount of enzyme that cleaves 1pmol of McaRPKPVE-Nval-WRK(Dnp)-NH2 per minute at pH 8.0 at 37℃.
Citations
More Info
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Synonyms
Protease, Serine, 3, Protease, Serine, 4 (Trypsin 4, Brain), Brain Trypsinogen, Mesotrypsinogen, Mesotrypsin, Trypsin III, EC 3.4.21.4 4, Trypsin IV, PRSS4, TRY3, TRY4 Protease, Serine, 3 (Mesotrypsin), Pancreatic Trypsinogen III, Serine Protease 3, Serine Protease 4, Trypsinogen IV, Trypsinogen 4, Trypsinogen 5, EC 3.4.21, MTG, T9.
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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
VPFDDDDKIV GGYTCEENSL PYQVSLNSGS HFCGGSLISE QWVVSAAHCY KTRIQVRLGE HNIKVLEGNE QFINAAKIIR HPKYNRDTLD NDIMLIKLSS PAVINARVST ISLPTAPPAA GTECLISGWG NTLSFGADYP DELKCLDAPV LTQAECKASY PGKITNSMFC VGFLEGGKDS CQRDSGGPVV CNGQLQGVVS WGHGCAWKNR PGVYTKVYNY VDWIKDTIAA NSHHHHHH.
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Background
PRSS3 is a member of the serine protease family, characterized by its specific enzymatic activity mediated by the serine residue in the catalytic triad. PRSS3's structure consists of a catalytic domain, a substrate-binding site, and disulfide bridges that help maintain its stability. Understanding the molecular characteristics of PRSS3 is crucial for elucidating its functions.
Physiological Functions: PRSS3 is primarily expressed in the pancreas, where it plays a vital role in the digestion of dietary proteins. It contributes to the breakdown of proteins into smaller peptides, facilitating their absorption in the small intestine. PRSS3 is part of a complex enzymatic network that ensures proper digestion and nutrient absorption.
Pathological Implications: Research has shown that abnormal PRSS3 activity or expression can be associated with various diseases. For example, alterations in PRSS3 have been linked to pancreatic diseases, including pancreatitis and pancreatic cancer. Investigating PRSS3's role in disease pathogenesis can provide valuable insights into the development and progression of these conditions.
Biomedical Research: PRSS3 human recombinant proteins are valuable tools in biomedical research. Researchers use these recombinant proteins to study PRSS3's enzymatic properties, interactions with other molecules, and potential therapeutic applications. They can perform controlled experiments to gain a deeper understanding of PRSS3's functions.
Therapeutic Potential: PRSS3's involvement in diseases like pancreatitis and pancreatic cancer has raised interest in its therapeutic potential. Researchers explore the development of inhibitors or modulators targeting PRSS3 as potential treatments for these diseases. Additionally, PRSS3's role in protein digestion has implications for digestive disorders and enzyme replacement therapies.
Diagnostic Markers: PRSS3 levels or activity may serve as diagnostic markers for certain diseases. Changes in PRSS3 expression in pancreatic tissue or serum may be indicative of pancreatic disorders. Research in this area aims to establish PRSS3 as a diagnostic tool for early disease detection.
Future Directions: Continued research on PRSS3 human recombinant and its roles in health and disease is essential. This includes investigating its regulation, substrate specificity, and potential interactions with other proteins. Such studies may uncover novel therapeutic targets and diagnostic strategies.
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 :
PSG1 Human, Sf9Description:
Pregnancy Specific Beta-1-Glycoprotein 1 Human Recombinant, Sf9
Pregnancy Specific Beta-1-Glycoprotein 1, PSBG1, B1G1, Fetal Liver Non-Specific Cross-Reactive Antigen 1/2, Pregnancy-Specific Beta-1 Glycoprotein C/D, CD66 Antigen-Like Family Member F, PS-Beta-C/D, PS-Beta-G-1, FL-NCA-1/2, PSBG-1, PSGGA, PSG95, SP1, Pregnancy-Specific Beta-1-Glycoprotein 1, Pregnancy-Specific B-1 Glycoprotein, Pregnancy-Specific Glycoprotein 1, CD66f Antigen, DHFRP2, PSGIIA, CD66f, PBG1, PSG1.
Product # :
PRO-2452Price :
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Description
PSG1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 394 amino acids (35-419a.a.) and having a molecular mass of 44.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). PSG1 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
PSG1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Pregnancy Specific Beta-1-Glycoprotein 1 (PSG1) is a member of a subgroup of transcription factors which are phosphorylated upon binding to promoter sequences. PSGs belong to the carcinoembryonic antigen (CEA) family and function as early biochemical markers of syncytiotrophoblast formation. Furthermore, PSG1 is assumed to mediate placental vascular morphogenesis by enhancing VEGF-A production and endothelial tube formation. PSG1 is a major product of the syncytiotrophoblast, reaching concentrations of 100- 290 mg/l at term in the serum of pregnant women.
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Synonyms
Pregnancy Specific Beta-1-Glycoprotein 1, PSBG1, B1G1, Fetal Liver Non-Specific Cross-Reactive Antigen 1/2, Pregnancy-Specific Beta-1 Glycoprotein C/D, CD66 Antigen-Like Family Member F, PS-Beta-C/D, PS-Beta-G-1, FL-NCA-1/2, PSBG-1, PSGGA, PSG95, SP1, Pregnancy-Specific Beta-1-Glycoprotein 1, Pregnancy-Specific B-1 Glycoprotein, Pregnancy-Specific Glycoprotein 1, CD66f Antigen, DHFRP2, PSGIIA, CD66f, PBG1, PSG1.
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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
ADLQVTIEAE PTKVSEGKDV LLLVHNLPQN LTGYIWYKGQ MRDLYHYITS YVVDGEIIIY GPAYSGRETA YSNASLLIQN VTREDAGSYT LHIIKGDDGT RGVTGRFTFT LHLETPKPSI SSSNLNPRET MEAVSLTCDP ETPDASYLWW MNGQSLPMTH SLKLSETNRT LFLLGVTKYT AGPYECEIRN PVSASRSDPV TLNLLPKLPK PYITINNLNP RENKDVLNFT CEPKSENYTY IWWLNGQSLP VSPRVKRPIE NRILILPSVT RNETGPYQCE IRDRYGGIRS DPVTLNVLYG PDLPRIYPSF TYYRSGEVLY LSCSADSNPP AQYSWTINEK FQLPGQKLFI RHITTKHSGL YVCSVRNSAT GKESSKSMTV EVSGKWIPHH HHHH.
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 :
GPT2 HumanDescription:
Glutamic-Pyruvate Transaminase 2 Human Recombinant
ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 2.
Product # :
ENZ-680Price :
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Description
GPT2 Human Recombinant produced in E. coli is a single polypeptide chain containing 546 amino acids (1-523) and having a molecular mass of 60.3 kDa. GPT2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GPT2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 7.5), 30% glycerol, 0.2M NaCl and 2mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Alanine aminotransferase 2 (GPT2), catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids. Multiple transcript variants encoding various isoforms have been found for GPT2.
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Synonyms
ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 2.
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Physical Appearance
Sterile Filtered colorless solution.
-
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 MGSMQRAAAL VRRGCGPRTP SSWGRSQSSA AAEASAVLKV RPERSRRERI LTLESMNPQV KAVEYAVRGP IVLKAGEIEL ELQRGIKKPF TEVIRANIGD AQAMGQQPIT FLRQVMALCT YPNLLDSPSF PEDAKKRARR ILQACGGNSL GSYSASQGVN CIREDVAAYI TRRDGGVPAD PDNIYLTTGA SDGISTILKI LVSGGGKSRT GVMIPIPQYP LYSAVISELD AIQVNYYLDE ENCWALNVNE LRRAVQEAKD HCDPKVLCII NPGNPTGQVQ SRKCIEDVIH FAWEEKLFLL ADEVYQDNVY SPDCRFHSFK KVLYEMGPEY SSNVELASFH STSKGYMGEC GYRGGYMEVI NLHPEIKGQL VKLLSVRLCP PVSGQAAMDI VVNPPVAGEE SFEQFSREKE SVLGNLAKKA KLTEDLFNQV PGIHCNPLQG AMYAFPRIFI PAKAVEAAQA HQMAPDMFYC MKLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPVEKLKTV LQKVKDFHIN FLEKYA.
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 :
RAGE Human, Sf9Description:
Advanced Glycosylation End Product-Specific Receptor Human Recombinant, Sf9
Advanced Glycosylation End-Product Specific Receptor, Advanced Glycosylation End Product-Specific Receptor, RAGE, Receptor for Advanced Glycation End-Products Variant 20, Receptor for Advanced Glycosylation End Products, Receptor for Advanced Glycation End-Products, RAGE Isoform NtRAGE-Delta, RAGE Isoform SRAGE-Delta, SCARJ1.
Product # :
PRO-2645Price :
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Description
RAGE Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 561 amino acids (24-342 a.a) and having a molecular mass of 61.2kDa. RAGE is fused to a 242 amino acid hIgG-His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The RAGE solution (0.25mg/1ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by the ability of the binding activity in a functional ELISA. The ED50 range ≤15ug/ml.
Citations
More Info
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Introduction
Advanced Glycosylation End Product-Specific Receptor or RAGE is an immunoglobulin, part of the immunoglobulin transmembrane proteins family. RAGE moderates interactions between advanced glycosylation end products, also known as AGE. These signaling has a crucial part in the regulation of TNFalpha,oxidative stress, endothelial dysfunction in type 2 diabetesproduction and expression. RAGE helps the translocation of ABPP (amyloid-beta peptide) through the membrane of cells to the intracellular area in the cortical neurons.
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Synonyms
Advanced Glycosylation End-Product Specific Receptor, Advanced Glycosylation End Product-Specific Receptor, RAGE, Receptor for Advanced Glycation End-Products Variant 20, Receptor for Advanced Glycosylation End Products, Receptor for Advanced Glycation End-Products, RAGE Isoform NtRAGE-Delta, RAGE Isoform SRAGE-Delta, SCARJ1.
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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
ADLQNITARI GEPLVLKCKG APKKPPQRLE WKLNTGRTEA WKVLSPQGGG PWDSVARVLP NGSLFLPAVG IQDEGIFRCQ AMNRNGKETK SNYRVRVYQI PGKPEIVDSA SELTAGVPNK VGTCVSEGSY PAGTLSWHLD GKPLVPNEKG VSVKEQTRRH PETGLFTLQS ELMVTPARGG DPRPTFSCSF SPGLPRHRAL RTAPIQPRVW EPVPLEEVQL VVEPEGGAVA PGGTVTLTCE VPAQPSPQIH WMKDGVPLPL PPSPVLILPE IGPQDQGTYS CVATHSSHGP QESRAVSISI IEPGEEGPTA GSVGGSGLGT LALEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEA HNHYTQKSLS LSPGKHHHHH H.
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 :
WHSC2 HumanDescription:
Wolf-Hirschhorn Syndrome Candidate 2 Human Recombinant
Negative elongation factor A, NELF-A, Wolf-Hirschhorn syndrome candidate 2 protein, WHSC2, NELFA, FLJ10442, FLJ25112, P/OKcl.15.
Product # :
PRO-062Price :
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Description
WHSC2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 559 amino acids (1-539 a.a.) and having a molecular mass of 60.6kDa. The WHSC2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The WHSC2 solution (0.25 mg/ml) 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT, 1mM EDTA and 20% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
WHSC2 (NELF-A) is a protein factor required for DRB-sensitive transcription. WHSC2 is one of the 5 components of the multisubunit NELF complex which cooperates with DSIF to repress RNA polymerase II elongation. The Wolf-Hirschhorn syndrome is a multiple malformation syndrome characterized by mental and developmental defects resulting from a hemizygous deletion of the distal short arm of chromosome 4 (4p16.3).
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Synonyms
Negative elongation factor A, NELF-A, Wolf-Hirschhorn syndrome candidate 2 protein, WHSC2, NELFA, FLJ10442, FLJ25112, P/OKcl.15.
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Physical Appearance
Sterile Filtered colorless solution.
-
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 MPGQRRALSP KMASMRESDT GLWLHNKLGA TDELWAPPSI ASLLTAAVID NIRLCFHGLS SAVKLKLLLG TLHLPRRTVD EMKGALMEII QLASLDSDPW VLMVADILKS FPDTGSLNLE LEEQNPNVQD ILGELREKVG ECEASAMLPL ECQYLNKNAL TTLAGPLTPP VKHFQLKRKP KSATLRAELL QKSTETAQQL KRSAGVPFHA KGRGLLRKMD TTTPLKGIPK QAPFRSPTAP SVFSPTGNRT PIPPSRTLLR KERGVKLLDI SELDMVGAGR EAKRRRKTLD AEVVEKPAKE ETVVENATPD YAAGLVSTQK LGSLNNEPAL PSTSYLPSTP SVVPASSYIP SSETPPAPSS REASRPPEEP SAPSPTLPAQ FKQRAPMYNS GLSPATPTPA APTSPLTPTT PPAVAPTTQT PPVAMVAPQT QAPAQQQPKK NLSLTREQMF AAQEMFKTAN KVTRPEKALI LGFMAGSREN PCQEQGDVIQ IKLSEHTEDL PKADGQGSTT MLVDTVFEMN YATGQWTRFK KYKPMTNVS.
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 :
EBI3 Human, HisDescription:
Epstein Barr Virus Induced 3 Human Recombinant, His Tag
Interleukin-27 subunit beta, IL-27 subunit beta, IL-27B, Epstein-Barr virus-induced gene 3 protein, EBV-induced gene 3 protein, EBI3, IL27B.
Product # :
CYT-668Price :
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Description
EBI3 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 209 amino acids fragment (21-229) having a molecular weight of 34kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The EBI3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EBI3 protein is supplied in 1xPBS, 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
EBI3 has an induced expression in B lymphocytes in reaction to Epstein-Barr virus infection. EBI3 encodes a secreted glycoprotein belonging to the hematopoietin receptor family, and heterodimerizes with a 28 kDa protein to form iIL-27. EBI3 drives rapid clonal expansion of naive cd4(+) t-cells. EBI3 strongly synergizes with IL-12 to activate IFN-gamma production of naive cd4(+) t-cells. EBI3 mediates its biologic effects through the cytokine receptor wsx-1/tccr.
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Synonyms
Interleukin-27 subunit beta, IL-27 subunit beta, IL-27B, Epstein-Barr virus-induced gene 3 protein, EBV-induced gene 3 protein, EBI3, IL27B.
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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. Please avoid freeze thaw cycles.
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Background
What is the molecular weight/Mw of EBI3 Protein?
EBI3 Protein has a total Mw of 34kDa.
What is the source or expression system of EBI3 Protein?
Escherichia Coli.
What is the Purity of EBI3 Protein?
EBI3 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EBI3 Protein?
The biological functionality of EBI3 Protein will be determined in the future.
What is the amino acid sequence of EBI3 Protein?
EBI3 Protein is composed from 209 amino acids.
What applications can EBI3 Protein be used in?
EBI3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EBI3 Protein?
The endotoxin level is minimal, EBI3 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 :
UBE2G HumanDescription:
Ubiquitin-Conjugating Enzyme E2G Human Recombinant
E217K, UBC7, UBE2G, Ubiquitin-conjugating enzyme E2 G1, E2 ubiquitin-conjugating enzyme G1, E217K, UBC7, Ubiquitin carrier protein G1, Ubiquitin-protein ligase G1.
Product # :
ENZ-838Price :
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Description
UBE2G Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 193 amino acids (1-170 a.a) and having a molecular mass of 21.9kDa.UBE2G is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UBE2G protein solution (0.5mg/ml) containing Phosphate buffered saline, (pH7.4) 30% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Protein modification with ubiquitin is an essential cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least 3 classes of enzymes: ubiquitin-activating enzymes (E1s) ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). Ubiquitin-Conjugating Enzyme E2G (UBE2G1) belongs to the E2 ubiquitin-conjugating enzyme family and catalyzes the covalent attachment of ubiquitin to other proteins. UE2G1 protein is involved in degradation of muscle-specific proteins.
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Synonyms
E217K, UBC7, UBE2G, Ubiquitin-conjugating enzyme E2 G1, E2 ubiquitin-conjugating enzyme G1, E217K, UBC7, Ubiquitin carrier protein G1, Ubiquitin-protein ligase G1.
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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 MGSMTELQSA LLLRRQLAEL NKNPVEGFSA GLIDDNDLYR WEVLIIGPPD TLYEGGVFKA HLTFPKDYPL RPPKMKFITE IWHPNVDKNG DVCISILHEP GEDKYGYEKP EERWLPIHTV ETIMISVISM LADPNGDSPA NVDAAKEWRE DRNGEFKRKV ARCVRKSQET AFE.
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 :
AKR1B1 HumanDescription:
Aldose Reductase Human Recombinant
Aldehyde Reductase, EC 1.1.1.21, ALR2, ALDR1, MGC1804, Aldo-keto reductase family1 member B1, Aldose Reductase, AKR1B1, AR, ADR.
Product # :
ENZ-390Price :
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Description
AKR1B1 Human Recombinant amino produced in E.Coli is a single, non-glycosylated polypeptide chain containing 316 amino acids having a molecular mass of 35.8 kDa.The AKR1B1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The 1mg/ml protein solution contains 20mM Tris-HCl buffer pH 8, 10% glycerol, and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 800pmol/min/ug, and is defined as the amount of enzyme that catalyze the reduction of 1.0 pmole DL-glyceraldehyde in the presence of NADPH per minute at pH7.0 at 37°C.Citations
More Info
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Introduction
AKR1B1 is part of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. AKR1B1 catalyzes the reduction several aldehydes, including the aldehyde form of glucose, and thus involved in the development of diabetic complications by catalyzing the reduction of glucose to sorbitol. AKR1B1 catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Transgenic mice over expressing human aldose reductase show that AKR1B1 is a key player in ischemic injury and impairment of functional and metabolic recovery after ischemia. Aldose Reductase is an obligatory mediator of TNF-alpha signaling leading to an increase in the expression of adhesion molecules and increased binding of monocytes to the endothelium. AKR1B1 is a critical regulator of TNF-alpha-induced apoptotic signaling in endothelial cells.
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Synonyms
Aldehyde Reductase, EC 1.1.1.21, ALR2, ALDR1, MGC1804, Aldo-keto reductase family1 member B1, Aldose Reductase, AKR1B1, AR, ADR.
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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
MASRLLLNNG AKMPILGLGT WKSPPGQVTE AVKVAIDVGY RHIDCAHVYQ NENEVGVAIQ EKLREQVVKR EELFIVSKLW CTYHEKGLVK GACQKTLSDL KLDYLDLYLI HWPTGFKPGK EFFPLDESGN VVPSDTNILD TWAAMEELVD EGLVKAIGIS NFNHLQVEMI LNKPGLKYKP AVNQIECHPY LTQEKLIQYC QSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK HNKTTAQVLI RFPMQRNLVV IPKSVTPERI AENFKVFDFE LSSQDMTTLL SYNRNWRVCA LLSCTSHKDY PFHEEF.
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 :
AKR1D1 Human, HisDescription:
Aldo-Keto Reductase Family 1 Member D1 Human Recombinant, His Tag
3-oxo-5-beta-steroid 4-dehydrogenase, Aldo-keto reductase family 1 member D1, Delta(4)-3-ketosteroid 5-beta-reductase, Delta(4)-3-oxosteroid 5-beta-reductase, KR1D1, SRD5B1, CBAS2, 3o5bred.
Product # :
ENZ-098Price :
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Description
AKR1D1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 346 amino acids (1-326 a.a.) and having a molecular mass of 39.5kDa. The AKR1D1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AKR1D1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 100mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Aldo-keto reductase family 1 member D1 (AKR1D1) belongs to the AKR superfamily. The AKR family proteins are soluble NADPH oxidoreductases, which have vital roles in the metabolism of drugs, carcinogens and reactive aldehydes. AKR1D1 is also responsible for the catalysis of the 5-beta-reduction of bile acid intermediates and steroid hormones that carry a delta (4)-3-1 structure. AKR1D1 is highly expressed in the liver, colon and testis. Deficiency of the AKR1D1 enzyme may contribute to hepatic dysfunction.
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Synonyms
3-oxo-5-beta-steroid 4-dehydrogenase, Aldo-keto reductase family 1 member D1, Delta(4)-3-ketosteroid 5-beta-reductase, Delta(4)-3-oxosteroid 5-beta-reductase, KR1D1, SRD5B1, CBAS2, 3o5bred.
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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 MDLSAASHRI PLSDGNSIPI IGLGTYSEPK STPKGACATS VKVAIDTGYR HIDGAYIYQN EHEVGEAIRE KIAEGKVRRE DIFYCGKLWA TNHVPEMVRP TLERTLRVLQ LDYVDLYIIE VPMAFKPGDE IYPRDENGKW LYHKSNLCAT WEAMEACKDA GLVKSLGVSN FNRRQLELIL NKPGLKHKPV SNQVECHPYF TQPKLLKFCQ QHDIVITAYS PLGTSRNPIW VNVSSPPLLK DALLNSLGKR YNKTAAQIVL RFNIQRGVVV IPKSFNLERI KENFQIFDFS LTEEEMKDIE ALNKNVRFVE LLMWRDHPEY PFHDEY.
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 :
ALKBH3 HumanDescription:
ALKB Alkylation Repair Homolog 3 Human Recombinant
Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3, Alkylated DNA repair protein alkB homolog 3, DEPC-1, Prostate cancer antigen 1, ALKBH3, ABH3, DEPC1, PCA1, FLJ43614, MGC118790, MGC118792, MGC118793.
Product # :
ENZ-101Price :
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Description
ALKBH3 Human Recombinant fused to 39 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 325 amino acids (1-286 a.a.) and having a molecular mass of 37.9kDa. The ALKBH3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ALKBH3 solution 1mg/ml contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ALKBH3 belongs to the ALKB family of proteins and acts as a dioxygenase with a preference for RNA and single stranded DNA substrates. ALKBH3 protein repairs 1-methyladenine and 3-methylcytosine lesions in alkylated DNA and RNA and its activity is stimulated by ascorbate. ALKBH3 is expressed in a broad array of tissues and localizes to the cytoplasm and the nucleus.
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Synonyms
Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3, Alkylated DNA repair protein alkB homolog 3, DEPC-1, Prostate cancer antigen 1, ALKBH3, ABH3, DEPC1, PCA1, FLJ43614, MGC118790, MGC118792, MGC118793.
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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 KDRWGSELDM EEKRRRARVQ GAWAAPVKSQ AIAQPATTAK SHLHQKPGQT WKNKEHHLSD REFVFKEPQQ VVRRAPEPRV IDREGVYEIS LSPTGVSRVC LYPGFVDVKE ADWILEQLCQ DVPWKQRTGI REDITYQQPR LTAWYGELPY TYSRITMEPN PHWHPVLRTL KNRIEENTGH TFNSLLCNLY RNEKDSVDWH SDDEPSLGRC PIIASLSFGA TRTFEMRKKP PPEENGDYTY VERVKIPLDH GTLLIMEGAT QADWQHRVPK EYHSREPRVN LTFRTVYPDP RGAPW.
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 :
ARSG HumanDescription:
Arylsulfatase G Human Recombinant
Arylsulfatase G, ASG, ARSG, KIAA1001, UNQ839/PRO1777.
Product # :
ENZ-677Price :
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Description
ARSG Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 532 amino acids (17-525) and having a molecular mass of 57kDa.ARSG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ARSG solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Arylsulfatase G (ARSG) is a member of the sulfatase enzyme family. Sulfatases are enzymes which hydrolyze sulfate esters from sulfated steroids, carbohydrates, proteoglycans, and glycolipids. Sulfatases are involved in hormone biosynthesis, modulation of cell signaling, and degradation of macromolecules. The ARSG protein exhibits arylsulfatase activity at acidic pH, as is characteristic of lysosomal sulfatases. The Arylsulfatase G enzyme localizes in the lysosomes. ARSG is inhibited by phosphate, which forms a covalent bond with the active site 3-oxoalanine. Arylsulfatase G is widely expressed, having very low expression in the brain, lung, heart and skeletal muscle.
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Synonyms
Arylsulfatase G, ASG, ARSG, KIAA1001, UNQ839/PRO1777.
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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 MGSGFLYPLV DFCISGKTRG QKPNFVIILA DDMGWGDLGA NWAETKDTAN LDKMASEGMR FVDFHAAAST CSPSRASLLT GRLGLRNGVT RNFAVTSVGG LPLNETTLAE VLQQAGYVTG IIGKWHLGHH GSYHPNFRGF DYYFGIPYSH DMGCTDTPGY NHPPCPACPQ GDGPSRNLQR DCYTDVALPL YENLNIVEQP VNLSSLAQKY AEKATQFIQR ASTSGRPFLL YVALAHMHVP LPVTQLPAAP RGRSLYGAGL WEMDSLVGQI KDKVDHTVKE NTFLWFTGDN GPWAQKCELA GSVGPFTGFW QTRQGGSPAK QTTWEGGHRV PALAYWPGRV PVNVTSTALL SVLDIFPTVV ALAQASLPQG RRFDGVDVSE VLFGRSQPGH RVLFHPNSGA AGEFGALQTV RLERYKAFYI TGGARACDGS TGPELQHKFP LIFNLEDDTA EAVPLERGGA EYQAVLPEVR KVLADVLQDI ANDNISSADY TQDPSVTPCC NPYQIACRCQ AA.
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 :
BACE1 HumanDescription:
Beta-Secretase 1 Human Recombinant
Beta-Secretase, Membrane-Associated Aspartic Protease, Beta-Site APP Cleaving Enzyme, Beta-Site APP-Cleaving Enzyme, Aspartyl Protease, EC 3.4.23.46, Memapsin-2, Asp, BACE, ASP2, Beta-Site Amyloid Beta A4 Precursor Protein-Cleaving Enzyme, Beta-Site Amyloid Precursor Protein Cleaving Enzyme, Transmembrane Aspartic Proteinase Asp2, Beta-Secretase 1 Precursor Variant, Beta-Site APP-Cleaving Enzyme, APP Beta-Secretase, EC 3.4.23, KIAA1149, HSPC104.
Product # :
ENZ-1119Price :
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Description
BACE1 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 442 amino acids (22-457 a.a.) and having a molecular mass of 49.2kDa. BACE1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
BACE1 protein solution containing Phosphate-Buffered Saline (pH 7.4) containing 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 5 pmol/min/ug in which one unit will convert 1.0 pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25C.
Citations
More Info
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Introduction
Beta-secretase 1 or BACE1 or beta-site amyloid precursor protein cleaving enzyme 1, is a protein that is encoded by the BACE1 gene in humans. Expression of BACE1 is seen primarily in neurons as it is crucial for the creation of myelin sheats in the peripheric nervous system. Beta-secretase 1 is a proteas that is located in the cell membrane (transmembrane). The enzyme consists of 2 active sites (aspartate residues) in the extracellular domain that can act as a dimer.
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Synonyms
Beta-Secretase, Membrane-Associated Aspartic Protease, Beta-Site APP Cleaving Enzyme, Beta-Site APP-Cleaving Enzyme, Aspartyl Protease, EC 3.4.23.46, Memapsin-2, Asp, BACE, ASP2, Beta-Site Amyloid Beta A4 Precursor Protein-Cleaving Enzyme, Beta-Site Amyloid Precursor Protein Cleaving Enzyme, Transmembrane Aspartic Proteinase Asp2, Beta-Secretase 1 Precursor Variant, Beta-Site APP-Cleaving Enzyme, APP Beta-Secretase, EC 3.4.23, KIAA1149, HSPC104.
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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
TQHGIRLPLR SGLGGAPLGL RLPRETDEEP EEPGRRGSFV EMVDNLRGKS GQGYYVEMTV GSPPQTLNIL VDTGSSNFAV GAAPHPFLHR YYQRQLSSTY RDLRKGVYVP YTQGKWEGEL GTDLVSIPHG PNVTVRANIA AITESDKFFI NGSNWEGILG LAYAEIARPD DSLEPFFDSL VKQTHVPNLF SLQLCGAGFP LNQSEVLASV GGSMIIGGID HSLYTGSLWY TPIRREWYYE VIIVRVEING QDLKMDCKEY NYDKSIVDSG TTNLRLPKKV FEAAVKSIKA ASSTEKFPDG FWLGEQLVCW QAGTTPWNIF PVISLYLMGE VTNQSFRITI LPQQYLRPVE DVATSQDDCY KFAISQSSTG TVMGAVIMEG FYVVFDRARK RIGFAVSACH VHDEFRTAAV EGPFVTLDME DCGYNIPQTD ESTLMTHHHH HH.
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.