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1000 results found for “hepatitis b”
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Name :
NBL1 HumanDescription:
Neuroblastoma 1 Human Recombinant
D1S1733E, DAN, DAND1, NB, NO3, Neuroblastoma suppressor of tumorigenicity 1, DAN domain family member 1, Zinc finger protein DAN, NBL1.
Product # :
PRO-1365Price :
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Description
NBL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (18-181 a.a) and having a molecular mass of 20kDa. NBL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
NBL1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Neuroblastoma suppressor of tumorigenicity 1 (NBL1) is a part of the evolutionarily conserved CAN (Cerberus and DAN) family of proteins, which contain a domain resembling the CTCK (C-terminal cystine knot-like) motif found in several signaling molecules. NBL1 is a is a tumor suppressor of neuroblastoma and takes part in preventing cells from entering the final stage (G1/S) of the transformation process. NBL1 is produced in small neurons of the dorsal root ganglion. The expression of NBL1 is triggered by MATH-1.
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Synonyms
D1S1733E, DAN, DAND1, NB, NO3, Neuroblastoma suppressor of tumorigenicity 1, DAN domain family member 1, Zinc finger protein DAN, NBL1.
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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 MGSAPPPINK LALFPDKSAW CEAKNITQIV GHSGCEAKSI QNRACLGQCF SYSVPNTFPQ STESLVHCDS CMPAQSMWEI VTLECPGHEE VPRVDKLVEK ILHCSCQACG KEPSHEGLSV YVQGEDGPGS QPGTHPHPHP HPHPGGQTPE PEDPPGAPHT EEEGAED.
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 :
NFNB E.ColiDescription:
Dihydropteridine Reductase E.Coli Recombinant
DPRA, NFSB, NFSI, NTR.
Product # :
ENZ-423Price :
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Description
NFNB Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-217 a.a.) and having a molecular mass of 26 kDa. The NFNB is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1mg/ml solution containing 20mM Tris pH-8, 1mM DTT, 0.05M NaCl & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
NFNB demonstrates the capability to reduce quinines. NFNB enzyme activates prodrugs in antibody directed enzyme prodrug therapy. NFNB reduces nitrofurazone, quinones and anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species.
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Synonyms
DPRA, NFSB, NFSI, NTR.
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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 MDIISVALKR HSTKAFDASK KLTPEQAEQI KTLLQYSPSS TNSQPWHFIV ASTEEGKARV AKSAAGNYVF NERKMLDASH VVVFCAKTAM DDVWLKLVVD QEDADGRFAT PEAKAANDKG RKFFADMHRK DLHDDAEWMA KQVYLNVGNF LLGVAALGLD AVPIEGFDAA ILDAEFGLKE KGYTSLVVVP VGHHSVEDFN ATLPKSRLPQ NITLTEV.
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 :
IDH1 HumanDescription:
Isocitrate Dehydrogenase-1 Human Recombinant
Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.
Product # :
ENZ-193Price :
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Description
IDH1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 434 amino acids (1-414) and having a molecular mass of 48.8 kDa.IDH1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The IDH1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl,
1mM DTT, 0.1mM PMSF and 20% glycerol.Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
The Specific activity is > 0.7 units/ml. One unit will convert 1.0 umole of isocitrate to alpha-ketoglutarate per minute at pH7.5 at 25C.Citations
More Info
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Introduction
Isocitrate Dehydrogenase is an enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle.
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Synonyms
Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.
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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 MSKKISGGSV VEMQGDEMTR IIWELIKEKL IFPYVELDLH SYDLGIENRD ATNDQVTKDA AEAIKKHNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR NILGGTVFRE AIICKNIPRL VSGWVKPIII GRHAYGDQYR ATDFVVPGPG KVEITYTPSD GTQKVTYLVH NFEEGGGVAM GMYNQDKSIE DFAHSSFQMA LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKQYKSQFE AQKIWYEHRL IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLVCPDG KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWTRGL AHRAKLDNNK ELAFFANALE EVSIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK LGENLKIKLA QAKL
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 :
SNUPN HumanDescription:
Snurportin 1 Human Recombinant
KPNBL, RNUT1, Snurportin1, SPN1, RNA U transporter 1.
Product # :
PRO-866Price :
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Description
SNUPN Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 380 amino acids (1-360 a.a.) and having a molecular mass of 43.3 kDa. The SNUPN is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SNUPN Human solution containing 20mM Tris pH-8, 2mM DTT, 0.1M NaCl, & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SNUPN is a nuclear import adaptor protein which is part of the Snurportin family.
SNUPN is Localized to the cytoplasm and nucleus and contains an N-terminal IBB domain and a trimethylguanosine (m3G)-cap binding domain. SNUPN binds specifically the terminal 2,2,7-m3G-cap at the 5'' end of U snRNPs and is involved in transport of U snRNPs into the nucleus through an association with Importin β. -
Synonyms
KPNBL, RNUT1, Snurportin1, SPN1, RNA U transporter 1.
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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 MEELSQALAS SFSVSQDLNS TAAPHPRLSQ YKSKYSSLEQ SERRRRLLEL QKSKRLDYVN HARRLAEDDW TGMESEEENK KDDEEMDIDT VKKLPKHYAN QLMLSEWLID VPSDLGQEWI VVVCPVGKRA LIVASRGSTS AYTKSGYCVN RFSSLLPGGN RRNSTAKDYT ILDCIYNEVN QTYYVLDVMC WRGHPFYDCQ TDFRFYWMHS KLPEEEGLGE KTKLNPFKFV GLKNFPCTPE SLCDVLSMDF PFEVDGLLFY HKQTHYSPGS TPLVGWLRPY MVSDVLGVAV PAGPLTTKPD YAGHQLQQIM EHKKSQKEGM KEKLTHKASE NGHYELEHLS
TPKLKGSSHS PDHPGCLMEN.
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 :
OLA1 HumanDescription:
Obg-Like ATPase 1 Human Recombinant
Obg-like ATPase 1, DNA damage-regulated overexpressed in cancer 45, DOC45, GTP-binding protein 9, OLA1, GTPBP9, PRO2455, PTD004, GBP45, GTBP9.
Product # :
ENZ-637Price :
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Description
OLA1 Human Recombinant produced in E. coli is a single polypeptide chain containing 420 amino acids (1-396) and having a molecular mass of 47.3kDa.OLA1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OLA1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Obg-like ATPase 1 (OLA1) acts as a negative regulator of the cellular antioxidant response independent of transcriptional processes. OLA1 curbs the antioxidant response via nontranscriptional mechanisms. OLA1 hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. OLA1 is clearly down-regulated by DNA damage-inducing agents. OLA1 is expressed in all tissues; however it is more abundant in the testis, liver, lung, and brain. OLA1 is overexpressed in a number of malignancies, including cancers of the colon, rectum, ovary, lung, stomach, and uterus.
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Synonyms
Obg-like ATPase 1, DNA damage-regulated overexpressed in cancer 45, DOC45, GTP-binding protein 9, OLA1, GTPBP9, PRO2455, PTD004, GBP45, GTBP9.
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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
MGSSHHHHHH SSGLVPRGSH MGSHMPPKKG GDGIKPPPII GRFGTSLKIG IVGLPNVGKS TFFNVLTNSQ ASAENFPFCT IDPNESRVPV PDERFDFLCQ YHKPASKIPA FLNVVDIAGL VKGAHNGQGL GNAFLSHISA CDGIFHLTRA FEDDDITHVE GSVDPIRDIE IIHEELQLKD EEMIGPIIDK LEKVAVRGGD KKLKPEYDIM CKVKSWVIDQ KKPVRFYHDW NDKEIEVLNK HLFLTSKPMV YLVNLSEKDY IRKKNKWLIK IKEWVDKYDP GALVIPFSGA LELKLQELSA EERQKYLEAN MTQSALPKII KAGFAALQLE YFFTAGPDEV RAWTIRKGTK APQAAGKIHT DFEKGFIMAE VMKYEDFKEE GSENAVKAAG KYRQQGRNYI VEDGDIIFFK FNTPQQPKKK.
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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Description:
Ornithine Aminotransferase Human Recombinant
DKFZp781A11155, HOGA, OATASE, Ornithine aminotransferase mitochondrial, Ornithine--oxo-acid aminotransferase, OAT, OKT, GACR.
Product # :
ENZ-472Price :
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Description
Ornithine Aminotransferase Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 408 amino acids (33-439 a.a.) and having a molecular wieght of 45.2kDa.The Ornithine Aminotransferase is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Ornithine Aminotransferase protein solution contains 20mM Tris, pH-8, and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Ornithine Aminotransferase is a mitochondrial enzyme which is an important factor that converts arginine and ornithine into the major excitatory and inhibitory neurotransmitters glutamate and GABA. Ornithine Aminotransferase mutations result in a deficiency that cause the autosomal recessive eye disease Gyrate Atrophy.
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Synonyms
DKFZp781A11155, HOGA, OATASE, Ornithine aminotransferase mitochondrial, Ornithine--oxo-acid aminotransferase, OAT, OKT, GACR.
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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
MTVQGPPTSD DIFEREYKYG AHNYHPLPVA LERGKGIYLW DVEGRKYFDF LSSYSAVNQG HCHPKIVNAL KSQVDKLTLT SRAFYNNVLG EYEEYITKLF NYHKVLPMNT GVEAGETACK LARKWGYTVK GIQKYKAKIV AAGNFWGRT LSAISSSTDP TSYDGFGPFM PGFDIIPYND LPALERALQD PNVAAFMVEP IQGEAGVVVP DPGYLMGVRE LCTRHQVLFI ADEIQTGLAR TGRWLAVDYE NVRPDIVLLG KALSGGLYPV SAVLCDDDIM LTIKPGEHGS TYGGNPLGCR VAIAALEVLE EENLAENADK LGIILRNELM KLPSDVVTAV RGKGLLNAIV IKETKDWDAW KVCLRLRDNG LLAKPTHGDI IRFAPPLVIK EDELRESIEI INKTILSF.
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 :
BPGM HumanDescription:
2,3-Bisphosphoglycerate Mutase Human Recombinant
Bisphosphoglycerate mutase, EC 5.4.2.4, BPGM, 2,3-bisphosphoglycerate mutase erythrocyte, 2,3-bisphosphoglycerate synthase, BPG-dependent PGAM.
Product # :
ENZ-505Price :
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Description
BPGM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 267 amino acids (1-259 a.a.) and having a molecular mass of 31 kDa. The BPGM is fused to an 8 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BPGM solution (0.5mg/ml) contains 20mM Tris-HCl (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
BPGM is found at high concentrations in red blood cells where it binds to and decreases the oxygen affinity of hemoglobin. PGM deficiency increases the oxygen affinity of cells. BPGM is a multifunctional enzyme that catalyzes 2,3-DPG synthesis through its synthetase activity, and 2,3-DPG degradation using its phosphatase activity. BPGM has phosphoglycerate phosphomutase activity. Mutations in BPGM cause hemolytic anemia. BPGM catalyzes the reaction of EC 5.4.2.1 (mutase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.
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Synonyms
Bisphosphoglycerate mutase, EC 5.4.2.4, BPGM, 2,3-bisphosphoglycerate mutase erythrocyte, 2,3-bisphosphoglycerate synthase, BPG-dependent PGAM.
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Physical Appearance
Sterile Filtered clear 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
MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF EFDLVFTSVL NRSIHTAWLI LEELGQEWVP VESSWRLNERHYGALIGLNR EQMALNHGEE QVRLWRRSYN VTPPPIEESH PYYQEIYNDR RYKVCDVPLD QLPRSESLKD VLERLLPYWN ERIAPEVLRG KTILISAHGN SSRALLKHLE GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA IQAAIKKVED QGKVKQAKKL EHHHHHH.
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 :
IVD HumanDescription:
Isovaleryl Coenzyme A Dehydrogenase Human Recombinant
FLJ12715, isovaleryl-CoA dehydrogenase mitochondrial, FLJ34849, EC 1.3.99.10, IVD, ACAD2.
Product # :
ENZ-490Price :
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Description
IVD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 415 amino acids (33-426 a.a.) and having a molecular mass of 45.3 kDa. The IVD is fused to a 20 amino acid his tag at N-terminus and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The IVD protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
IVD is a mitochondrial matrix enzyme that is part of the cyl-CoA dehydrogenase family which catalyzes the third step in leucine catabolism. The genetic deficiency of IVD leads to a buildup of isovaleric acid, which is toxic to the central nervous system and results in isovaleric acidemia. IVD is a homotetrameric flavoenzyme which catalyzes the conversion of isovaleryl-CoA to 3-methylcrotonyl-CoA.
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Synonyms
FLJ12715, isovaleryl-CoA dehydrogenase mitochondrial, FLJ34849, EC 1.3.99.10, IVD, ACAD2.
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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 MHSLLPVDDA INGLSEEQRQ LRQTMAKFLQ EHLAPKAQEI DRSNEFKNLR EFWKQLGNLG VLGITAPVQY GGSGLGYLEH VLVMEEISRA SGAVGLSYGA HSNLCINQLV RNGNEAQKEK YLPKLISGEY IGALAMSEPN AGSDVVSMKL KAEKKGNHYI LNGNKFWITN GPDADVLIVY AKTDLAAVPA SRGITAFIVE KGMPGFSTSK KLDKLGMRGS NTCELIFEDC KIPAANILGH ENKGVYVLMS GLDLERLVLA GGPLGLMQAV LDHTIPYLHV REAFGQKIGH FQLMQGKMAD MYTRLMACRQ YVYNVAKACD EGHCTAKDCA GVILYSAECA TQVALDGIQC FGGNGYINDF PMGRFLRDAK LYEIGAGTSE VRRLVIGRAF NADFH.
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 :
CD74 HumanDescription:
CD74 Human Recombinant
DHLAG, HLADG, Ia-GAMMA, li, HLA-DR antigens-associated invariant chain, p33, Ia antigen-associated invariant chain, HLA class II histocompatibility antigen gamma chain, CD74, Gamma Chain Of Class II Antigens, MHC HLA-DR Gamma Chain.
Product # :
PRO-1467Price :
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Description
CD74 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (73-232 a.a) and having a molecular mass of 20.6kDa.CD74 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CD74 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CD74 (HLA class II histocompatibility antigen gamma chain isoform b), is a transmembrane protein (on antigen presenting cells) which is the invariant chain that chaperones MHC class IIdimers from the endoplasmic reticulum to the cell surface. CD74 is expressed by cells of both T lymphocyte and Blymphocyte lineages. CD74 upregulated in several cancers and is also expressed by non immune cells during inflammation. Diseases related with CD74 include thymic epithelial neoplasm and gastroduodenitis. Among its related super-pathways are Immune System and Immune response Antigen presentation by MHC class II. In addition CD74 functions as cell surface receptor for the cytokine MIF.
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Synonyms
DHLAG, HLADG, Ia-GAMMA, li, HLA-DR antigens-associated invariant chain, p33, Ia antigen-associated invariant chain, HLA class II histocompatibility antigen gamma chain, CD74, Gamma Chain Of Class II Antigens, MHC HLA-DR Gamma Chain.
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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 MGSQQQGRLD KLTVTSQNLQ LENLRMKLPK PPKPVSKMRM ATPLLMQALP MGALPQGPMQ NATKYGNMTE DHVMHLLQNA DPLKVYPPLK GSFPENLRHL KNTMETIDWK VFESWMHHWL LFEMSRHSLE QKPTDAPPKE SLELEDPSSG LGVTKQDLGP VPM
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 :
UBE2E3 HumanDescription:
Ubiquitin Conjugating Enzyme E2E3 Human Recombinant
UBCH9, UbcM2, UBE2E3, Ubiquitin-Conjugating Enzyme E2E 3, UBCH9, Ubiquitin-Conjugating Enzyme E2E 3 (Homologous To Yeast UBC4/5), Ubiquitin-Conjugating Enzyme E2E 3 (UBC4/5 Homolog, Yeast), Ubiquitin-Conjugating Enzyme E2-23 KDa, Ubiquitin Carrier Protein E3, Ubiquitin-Protein Ligase E3, EC 6.3.2.19, Ubiquitin-Conjugating Enzyme E2 E3, UBCE4.
Product # :
ENZ-906Price :
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Description
UBE2E3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 230 amino acids (1-207 a.a) and having a molecular mass of 25.3kDa.UBE2E3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UBE2E3 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
UBE2E3 or Ubiquitin-conjugating enzyme E2 E3 is part of the E2 ubiquitinconjugating enzyme family. UBE2E3 is needed for the destruction of mitotic cyclins and for cell cycle progression. The ubiquitination process covalently attaches to a short protein of 76 amino acids called ubiquitin, to a lysine residue on the target protein. When a protein has been tagged with one ubiquitin molecule, other rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein which grants passage into the proteasome's 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell.
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Synonyms
UBCH9, UbcM2, UBE2E3, Ubiquitin-Conjugating Enzyme E2E 3, UBCH9, Ubiquitin-Conjugating Enzyme E2E 3 (Homologous To Yeast UBC4/5), Ubiquitin-Conjugating Enzyme E2E 3 (UBC4/5 Homolog, Yeast), Ubiquitin-Conjugating Enzyme E2-23 KDa, Ubiquitin Carrier Protein E3, Ubiquitin-Protein Ligase E3, EC 6.3.2.19, Ubiquitin-Conjugating Enzyme E2 E3, UBCE4.
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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 MGSMSSDRQR SDDESPSTSS GSSDADQRDP AAPEPEEQEE RKPSATQQKK NTKLSSKTTA KLSTSAKRIQ KELAEITLDP PPNCSAGPKG DNIYEWRSTI LGPPGSVYEG GVFFLDITFS SDYPFKPPKV TFRTRIYHCN INSQGVICLD ILKDNWSPAL TISKVLLSIC SLLTDCNPAD PLVGSIATQY LTNRAEHDRI ARQWTKRYAT.
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 :
UBL3 HumanDescription:
Ubiquitin-Like 3 Human Recombinant
Ubiquitin-like 3, FLJ32018, HCG-1, Membrane-anchored ubiquitin-fold protein, MUB, PNSC1, HsMUB, DKFZP434K151.
Product # :
PRO-230Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
UBL3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 134 amino acids (1-114a.a) and having a molecular mass of 15.0kDa.UBL3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UBL3 protein solution (1mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
UBL3 - a member of the ubiquitin-like family is found in the membrane. UBL3 holds two N-glycosylation sites, a C-terminal prenylation site and a protein kinase C phosphorylation site. Even though Ubiquitin-like proteins are not directly involved in protein degradation, it seems they have several mechanistic similarities to the ubiquitin pathway.
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Synonyms
Ubiquitin-like 3, FLJ32018, HCG-1, Membrane-anchored ubiquitin-fold protein, MUB, PNSC1, HsMUB, DKFZP434K151.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
UBL3 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
MGSSHHHHHH SSGLVPRGSH MSSNVPADMI NLRLILVSGK TKEFLFSPND SASDIAKHVY DNWPMDWEEE QVSSPNILRL IYQGRFLHGN VTLGALKLPF GKTTVMHLVA RETLPEPNSQ GQRNREKTGE SNCC
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 :
UGT1A1 HumanDescription:
UDP Glucuronosyltransferase 1 Family Polypeptide A1 Human Recombinant
UDP Glucuronosyltransferase 1 Family, Polypeptide A1, UGT1, GNT1, UDP Glycosyltransferase 1 Family, Polypeptide A1, Bilirubin-Specific UDPGT Isozyme 1, UDP-Glucuronosyltransferase 1-A, UDP-Glucuronosyltransferase 1A1, EC 2.4.1.17, UDPGT 1-1, BILIQTL1, HUG-BR1, UGT1-01, UGT-1A, UGT1*1, UGT1.1, UGT1A, Bilirubin UDP-Glucuronosyltransferase Isozyme 1, Bilirubin UDP-Glucuronosyltransferase 1-1, UDP-Glucuronosyltransferase 1-1, UDPGT, UDP-glucuronosyltransferase 1-1.
Product # :
ENZ-864Price :
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Description
UGT1A1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 488 amino acids (26-490 a.a) and having a molecular mass of 54.7kDa. UGT1A1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UGT1A1 protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
UDP Glucuronosyltransferase 1 Family Polypeptide A1, also known as UGT1A1 has a main importance in the conjugation as well as subsequent elimination of potentially toxic xenobiotics and endogenous compounds. UGT1A1 is also capable of catalyzing glucuronidation of 17beta, 17alpha, 1-hydroxypyrene, 4-methylumbelliferone, 1-naphthol, paranitrophenol, scopoletin, and umbelliferone.
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Synonyms
UDP Glucuronosyltransferase 1 Family, Polypeptide A1, UGT1, GNT1, UDP Glycosyltransferase 1 Family, Polypeptide A1, Bilirubin-Specific UDPGT Isozyme 1, UDP-Glucuronosyltransferase 1-A, UDP-Glucuronosyltransferase 1A1, EC 2.4.1.17, UDPGT 1-1, BILIQTL1, HUG-BR1, UGT1-01, UGT-1A, UGT1*1, UGT1.1, UGT1A, Bilirubin UDP-Glucuronosyltransferase Isozyme 1, Bilirubin UDP-Glucuronosyltransferase 1-1, UDP-Glucuronosyltransferase 1-1, UDPGT, UDP-glucuronosyltransferase 1-1.
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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 MGSHAGKILL IPVDGSHWLS MLGAIQQLQQ RGHEIVVLAP DASLYIRDGA FYTLKTYPVP FQREDVKESF VSLGHNVFEN DSFLQRVIKT YKKIKKDSAM LLSGCSHLLH NKELMASLAE SSFDVMLTDP FLPCSPIVAQ YLSLPTVFFL HALPCSLEFE ATQCPNPFSY VPRPLSSHSD HMTFLQRVKN MLIAFSQNFL CDVVYSPYAT LASEFLQREV TVQDLLSSAS VWLFRSDFVK DYPRPIMPNM VFVGGINCLH QNPLSQEFEA YINASGEHGI VVFSLGSMVS EIPEKKAMAI ADALGKIPQT VLWRYTGTRP SNLANNTILV KWLPQNDLLG HPMTRAFITH AGSHGVYESI CNGVPMVMMP LFGDQMDNAK RMETKGAGVT LNVLEMTSED LENALKAVIN DKSYKENIMR LSSLHKDRPV EPLDLAVFWV EFVMRHKGAP HLRPAAHDLT WYQYHSLD.
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 :
GSTT2 HumanDescription:
Glutathione S-Transferase Theta-2 Human Recombinant
Glutathione S-transferase theta 2, GST class-theta-2, GSTT2B, Glutathione S-transferase theta-2B, EC 2.5.1.18.
Product # :
ENZ-593Price :
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Shipped with Ice Packs
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Description
GSTT2 Recombinant produced in E. coli is a single polypeptide chain containing 264 amino acids (1-244) and having a molecular mass of 29.6kDa.GSTT2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GSTT2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl,
1mM DTT and 10% glycerol.Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GSTT2 belongs to the glutathione s-transferase (GST) family of proteins. There are eight GST proteins families, named alpha, kappa, mu, omega, pi, sigma, theta and zeta. Each one of the GST families has several proteins with different functions throughout the cell. The theta type members GSTT1 and GSTT2 have a 55% aa sequence homology and hold a vital role in human carcinogenesis. The theta genes are structurally similar – each has five exons with identical exon/intron boundaries.
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Synonyms
Glutathione S-transferase theta 2, GST class-theta-2, GSTT2B, Glutathione S-transferase theta-2B, EC 2.5.1.18.
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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 MGLELFLDLV SQPSRAVYIF AKKNGIPLEL RTVDLVKGQH KSKEFLQINS LGKLPTLKDG DFILTESSAI LIYLSCKYQT PDHWYPSDLQ ARARVHEYLG WHADCIRGTF GIPLWVQVLG PLIGVQVPEE KVERNRTAMD QALQWLEDKF LGDRPFLAGQ QVTLADLMAL EELMQPVALG YELFEGRPRL AAWRGRVEAF LGAELCQEAH SIILSILEQA AKKTLPTPSP EAYQAMLLRI ARIP
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 :
REG4 HumanDescription:
Regenerating Islet-Derived 4 Human Recombinant
Regenerating islet-derived protein 4, Reg IV, REG-like protein, Gastrointestinal secretory protein, REG4, GISP, RELP.
Product # :
PRO-424Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Recombinant Human REG-4 is manufactured with N-terminal fusion of His Tag. The Recombinant Human REG-IV His-Tagged Fusion Protein is 17.4 kDa protein containing 136 amino acid residues of the Human REG 4 and 12 additional amino acid residues – His Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 20mM Tris, pH 8.0.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
REG protein was shown to be stimulated during the regeneration of pancreatic islets. Since then, many Reg-related proteins have been identified in humans and other animals. In human, the four REG family genes, i.e., REG 1 alpha, REG 1 beta, REG-related sequence (RS) and HIP/PAP, have so far been isolated. These Reg-related proteins are classified into four subfamilies according to their amino-acid sequences, but they share a similar structure and physiological function. Reg protein is a growth factor for pancreatic beta cells and also suggests that the administration of Reg protein could be used as another therapeutic approach for diabetes mellitus. Human REG cDNA which encodes a 166-amino acid protein with a 22-amino acid signal peptide. The amino acid sequence of human REG protein has 68% homology to that of rat Reg protein.
Reg I was found to be expressed mainly in pancreatic beta and acinoductular cells as well as gastric fundic enterochromaffin-like (ECL) cells. Reg I production in ECL cells is stimulated by gastrin, as well as by the proinflammatory cytokine, cytokine-induced neutrophil chemoattractant (CINC)-2Beta. In patients with chronic hypergastrinemia, Reg production is stimulated, with the increased proliferation of gastric mucosal cells. Patients with Helicobacter pylori infection also showed increased Reg production in the gastric mucosa, partly via increased plasma gastrin concentration and partly via increased proinflammatory cytokine production. The serum concentration of the reg-protein was significantly higher in patients with various pancreatic diseases than in normal controls, and was also significantly higher in patients with acute pancreatitis or chronic relapsing pancreatitis than in patients with chronic pancreatitis. Furthermore, the serum PSP/reg-protein concentration was also significantly increased in liver cirrhosis, choledocholithiasis, and various cancers of the digestive system. -
Synonyms
Regenerating islet-derived protein 4, Reg IV, REG-like protein, Gastrointestinal secretory protein, REG4, GISP, RELP.
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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
Add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS HMDIIMRPSC APGWFYHKSN CYGYFRKLRN WSDAELECQS YGNGAHLASI LSLKEASTIA EYISGYQRSQ PIWIGLHDPQ KRQQWQWIDG AMYLYRSWSG KSMGGNKHCA EMSSNNNFLT WSSNECNKRQ HFLCKYRP.
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 :
Ara h 1.0101Description:
Allergen Ara h 1.0101 Recombinant
Allergen Ara h 1, clone P41B, Allergen Ara h I, Allergen, Ara h 1.
Product # :
ALR-006Price :
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Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Allergen Ara h 1.0101 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 63,484 Dalton. Ara h 1.0101 is expressed with a 9xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Ara h 1.0101 is supplied in 20mM HEPES buffer pH-8.0, 100mM Nacl and 6M Urea.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Ara h 1 is a seed storage protein from Arachis hypogaea which causes an allergic reaction in human. Ara h 1 is found in 95% of peanut allergic patients from North America. Nevertheless, peanut-allergic patients of European populations have fewer sensitizations to Ara h 1.
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Synonyms
Allergen Ara h 1, clone P41B, Allergen Ara h I, Allergen, Ara h 1.
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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 :
BETV6.0102Description:
Allergenic Isoflavone Reductase-Like Protein Bet v 6.0102 Recombinant
Allergenic isoflavone reductase-like protein Bet v 6.0102, BETV6.0102.
Product # :
ALR-018Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant BETV6.0102 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 36,636 Dalton. BETV6.0102 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
BETV6.0102 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
BETV6.0102 allergen is one of Isoflavone reductases which were found in pear, orange, apple, mango, lychee and other plants. Isoflavone reductases are plant defense proteins which induced by plant stress, e.g. high salinity, freeze or drought.
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Synonyms
Allergenic isoflavone reductase-like protein Bet v 6.0102, BETV6.0102.
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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 :
ENHO HumanDescription:
Energy Homeostasis Associated Human Recombinant
Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.
Product # :
PRO-1569Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
ENHO Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 34-76) containing 121 amino acids including extra 78 N-terminal amino acids. The total molecular mass is 13.05kDa (calculated).
Source
Escherichia Coli.
Formulation
ENHO filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Energy Homeostasis Associated (ENHO) participates in glucose homeostasis maintenance and lipid metabolism. ENHO is expressed in the liver and the brain. The role of ENHO in obesity or diabetes is studied.
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Synonyms
Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.
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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. ENHO 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
MGGKSNGEKK YIVGFKQGFK SCAKKEDVIS EKGGKLQKCF KYVDAASATL NEKAVEELKK DPSVAYVEED KLFKALTSCHSRSADVDSLS ESSPNSSPGP CPEKAPPPQK PSHEGSYLLQ P.
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 :
Borrelia Afzelii DbpADescription:
Borrelia Afzelii Decorin Binding Protein A Recombinant
Product # :
BOR-010Price :
Quantity :
Shipping Method :
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Description
Recombinant Borrelia Afzelii Decorin Binding Protein A produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 19 kDa. Borrelia Afzelii DbpA is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Borrelia Afzelii DbpA is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.
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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 IgG- and IgM-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma; suitable for LTT (lymphocyte transformation test).
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Applications
Western blot with Lyme positive plasma.
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 :
CBR4 HumanDescription:
Carbonyl Reductase-4 Human Recombinant
Carbonyl reductase family member 4, 3-oxoacyl-[acyl-carrier-protein] reductase, Quinone reductase CBR4, CBR4, SDR45C1, FLJ14431.
Product # :
ENZ-022Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CBR4 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 257 amino acids (1-237 a.a.) and having a molecular mass of 27.5kDa. The CBR4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CBR4 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 5mM DTT and 200mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CBR4 is a member of the short-chain dehydrogenase/reductase family. CBR4 has a role in biosynthesis of fatty acids in the mitochondria and a broad substrate specificity and reduces 9,10-phenanthrenequinone, 1,4-benzoquinone and a range of other o-quinones and p-quinones (in vitro). CBR4 formation of a heteroteramer with HSD17B8 has NADH-dependent 3-ketoacyl-acyl carrier protein reductase activity for o- and p-quinones.
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Synonyms
Carbonyl reductase family member 4, 3-oxoacyl-[acyl-carrier-protein] reductase, Quinone reductase CBR4, CBR4, SDR45C1, FLJ14431.
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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 MDKVCAVFGG SRGIGRAVAQ LMARKGYRLA VIARNLEGAK AAAGDLGGDH LAFSCDVAKE HDVQNTFEEM EKHLGRVNFL VNAAGINRDG LLVRTKTEDM VSQLHTNLLG SMLTCKAAMR TMIQQQGGSI VNVGSIVGLK GNSGQSVYSA SKGGLVGFSR ALAKEVARKK IRVNVVAPGF VHTDMTKDLK EEHLKKNIPL GRFGETIEVA HAVVFLLESP YITGHVLVVD GGLQLIL.
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 :
IL4 HumanDescription:
Interleukin-4 Human Recombinant
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
Product # :
CYT-211Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids and having a molecular mass of 15kDa. The IL-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL-4 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.
Purity
Greater than 98% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.2 ng/ml, corresponding to a Specific Activity of 5x106 IU/mg.Citations
More Info
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Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-4 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 IL-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
HKCDITLQE IIKTLNSLTE QKTLCTELTV TDIFAASKNT TEKETFCRAA TVLRQFYSHH EKDTRCLGAT AQQFHRHKQL IRFLKRLDRN LWGLAGLNSC PVKEANQSTL ENFLERLKTI MREKYSKCSS.
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Background
Everything You Should Know About IL-4 Human Recombinant
Interleukin-4 (IL-4) is an important type-2 cytokine with multiple effects on numerous cells and tissues in the body. As such, it's crucial for the immune system's maintenance and function.
Recent advancements have led to the development of interleukin-4 (rhIL-4) human recombinant in laboratories. As a result, experts have started studying its potential uses and therapeutic applications.
If you're interested in learning more about IL-4 human recombinant, check out the information below!
How Does Interleukin-4 (IL-4) Work?
Interleukin-4 (IL-4) acts as a signaling molecule, specifically a protein. It communicates with various immune cells by binding to specific receptors on their surface.
This process triggers responses against common threats, such as allergens, contaminants, and infections.
IL-4 is produced by T helper 2 (Th2) cells (a type of white blood cells), mast cells, eosinophils, and basophils.
What Interleukin-4 (IL-4) Does
As mentioned, this type-2 cytokine has multiple effects on various cells and tissues, so it fulfills several functions. Below are the most important ones:
- Th2 cell differentiation: IL-4 promotes the differentiation of T cells, triggering the response of Th2 cells, which fight parasites and regulate allergic responses.
- B cell activation and antibody production: IL-4 stimulates B cells, helping them proliferate and produce antibodies, particularly immunoglobulin E (IgE), which is involved in allergic reactions.
- Inflammation reduction: IL-4 can promote inflammation to address threats, such as allergens or parasites, and suppress it when necessary, depending on the context.
- Tissue repair and remodeling: IL-4 is key for tissue repair and remodeling processes, such as wound healing and fibrosis.
What Is IL-4 Human Recombinant?
IL-4 human recombinant is a version produced in a laboratory using DNA technology. The cytokine is inserted into a host organism, commonly E. Coli bacteria, for mass production.
This method allows experts to obtain pure and contaminant-free rhIL-4 with uniform biological activity and in large quantities.
What Can IL-4 Human Recombinant Be Used For?
Since this cytokine plays a key role in different processes, it may have multiple therapeutic applications for numerous diseases. These are the most common:
- Allergic diseases, such as asthma, rhinitis, and eczema
- Autoimmune diseases, such as rheumatoid arthritis and multiple sclerosis
- Infectious diseases, including those caused by parasites and viruses
- Cancer, as research suggests IL-4 could enhance the immune system's ability to fight cancer cells
Final Thoughts
The future of IL-4 human recombinant seems promising. This laboratory-produced version of an essential type-2 cytokine may be key to developing innovative therapies. However, more research is needed on potential applications to determine if it's safe and effectiv.
What is the molecular weight/Mw of IL 4 HUMAN Protein?
IL 4 HUMAN Protein has a total Mw of 15kDa.
What is the source or expression system of IL 4 HUMAN Protein?
Escherichia Coli.
What is the Purity of IL 4 HUMAN Protein?
IL 4 HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of IL 4 HUMAN Protein?
The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.2 ng/ml, corresponding to a Specific Activity of 5x106 IU/mg.
What is the amino acid sequence of IL 4 HUMAN Protein?
HKCDITLQE IIKTLNSLTE QKTLCTELTV TDIFAASKNT TEKETFCRAA TVLRQFYSHH EKDTRCLGAT AQQFHRHKQL IRFLKRLDRN LWGLAGLNSC PVKEANQSTL ENFLERLKTI MREKYSKCSS.
What applications can IL 4 HUMAN Protein be used in?
IL 4 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL 4 HUMAN Protein?
The endotoxin level is minimal, IL 4 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant IL 4 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of IL 4 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.594 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-4 as a Reference Standard.
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 :
Dengue Polyvalent ELISADescription:
Polyvalent Dengue Antigen-I for ELISA Recombinant
Product # :
DEN-027Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Polyvalent dengue antigens are 18kDa proteins containing subtype 1,2,3 and 4 and each of them has equal amount protein. They are a new group of antigens specifically designed for ELISA assay. All the recombinant peptides are fused with a 6xHis Tag. Polyvalent dengue is purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
Phosphate buffered saline, pH-9.4 and 25mM K₂CO₃.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
Citations
More Info
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Introduction
Caused by one of four closely related virus serotypes of the genus Flavivirus, family Flaviviridae, each serotype is sufficiently different that there is no cross-protection and epidemics caused by multiple serotypes (hyperendemicity) can occur. In cell culture experiments and mice Morpholino antisense oligos have shown specific activity against Dengue virus.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Polyvalent dengue Recombinant although stable at 4°C for 1 week, should be stored below -18°C. 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 :
HIV-1 p24 PairedDescription:
Mouse Anti HIV-1 p24 Paired
Product # :
ANT-772Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HIV-1 p24 Paired antibodies coating and conjugating are used for lateral flow immunoassay and having a Mw of 24kDa. Please note that when ordering for example: 100µg antibody we ship 50µg from each of the antibodies (100µg in total).
Formulation
*HIV-1 p24 Label antibody contains PBS, pH 7.4.
* HIV-1 p24 Capture antibody contains PBS, pH 7.4.
Purity
Greater than 95%.
Citations
More Info
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Introduction
Human immunodeficiency virus (HIV) is a retrovirus that can lead to a condition in which the immune system begins to fail, leading to opportunistic infections. HIV primarily infects vital cells in the human immune system such as helper T cells (specifically CD4+ T cells), macrophage sand dendritic cells. HIV infection leads to low levels of CD4+ T cells through three main mechanisms: firstly, direct viral killing of infected cells; secondly, increased rates of apoptosis in infected cells; and thirdly, killing of infected CD4+ T cells by CD8 cytotoxic lymphocytes that recognize infected cells. When CD4+ T cell numbers decline below a critical level, cell-mediated immunity is lost, and the body becomes progressively more susceptible to opportunistic infections. HIV was classified as a member of the genus Lentivirus, part of the Retroviridae family. Lentiviruses have many common morphologies and biological properties. Many species are infected by lentiviruses, which are characteristically responsible for long-duration illnesses with a long incubation period. Lentiviruses are transmitted as single-stranded, positive-sense, enveloped RNA viruses. Upon entry of the target cell, the viral RNA genome is converted to double-stranded DNA by a virally encoded reverse transcriptase that is present in the virus particle. This viral DNA is then integrated into the cellular DNA by a virally encoded integrase so that the genome can be transcribed. Once the virus has infected the cell, two pathways are possible: either the virus becomes latent and the infected cell continues to function, or the virus becomes active and replicates, and a large number of virus particles are liberated that can then infect other cells. The p24 protein is detected in patient blood as early as 2 weeks after HIV infection, further reducing the window period necessary to accurately detect the HIV status of the patient.
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Physical Appearance
2 vials of sterile filtered clear colorless solution.
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Stability
HIV-1 p24 antibody although stable at 4°C for 1 week, should be stored 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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Applications
Lateral flow immunoassay.
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Type
Mouse Anti Human Monoclonal.
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Purification Method
Purified by protein A affinity column.
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 :
HSPB11 HumanDescription:
Heat Shock Protein Family B Member 11 Human Recombinant
Heat shock protein beta-11, Hspb11, Placental protein 25, PP25, C1orf41, HSPC034, IFT25.
Product # :
HSP-046Price :
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Shipping Method :
Shipped with Ice Packs
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Description
HSPB11 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (1-144 a.a.) and having a molecular mass of 18.5kDa (Molecular weight on SDS-PAGE will appear higher).HSPB11 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HSPB11 protein (1mg/ml) solution contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HSPB11 is a component of IFT complex B composed of IFT88, IFT57, TRAF3IP1, IFT52, IFT27, HSPB11 and IFT20. HSPB11 is detected in the placenta.
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Synonyms
Heat shock protein beta-11, Hspb11, Placental protein 25, PP25, C1orf41, HSPC034, IFT25.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
HSPB11 Human Recombinant 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
MGSSHHHHHH SSGLVPRGSH MRKIDLCLSS EGSEVILATS SDEKHPPENI IDGNPETFWT TTGMFPQEFI ICFHKHVRIE RLVIQSYFVQ TLKIEKSTSK EPVDFEQWIE KDLVHTEGQL QNEEIVAHDG SATYLRFIIV SAFDHFASVH SVSAEGTVVS NLSS.
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 :
PGAM1 MouseDescription:
Phosphoglycerate Mutase 1 Mouse Recombinant
Phosphoglycerate mutase 1, BPG-dependent PGAM 1, Phosphoglycerate mutase isozyme B, PGAM-B, Pgam1, Pgam-1, 2310050F24Rik.
Product # :
ENZ-627Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PGAM1 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 278 amino acids (1-254) and having a molecular mass of 31.4kDa.PGAM1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PGAM1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
PGAM1 is part of the phosphoglycerate mutase family. PGAM1 is an essential component of glucose and 2,3-BPGA (2,3-bisphosphoglycerate) metabolism and catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM1 is a dimeric enzyme containing, in different tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM1 mutations lead to muscle phosphoglycerate mutase deficiency, a.k.a. glycogen storage disease X.
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Synonyms
Phosphoglycerate mutase 1, BPG-dependent PGAM 1, Phosphoglycerate mutase isozyme B, PGAM-B, Pgam1, Pgam-1, 2310050F24Rik.
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Physical Appearance
Sterile Filtered clear 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 MGSHMAAYKL VLIRHGESAW NLENRFSGWY DADLSPAGHE EAKRGGQALR DAGYEFDICF TSVQKRAIRT LWTVLDAIDQ MWLPVVRTWR LNERHYGGLT GLNKAETAAK HGEAQVKIWR RSYDVPPPPM EPDHPFYSNI SKDRRYADLT EDQLPSCESL KDTIARALPF WNEEIVPQIK EGKRVLIAAH GNSLRGIVKH LEGLSEEAIM ELNLPTGIPI VYELDKNLKP IKPMQFLGDE ETVRKAMEAV AAQGKVKK.
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.