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1000 results found for “htlv”
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Name :
HIF1AN HumanDescription:
Hypoxia-Inducible Factor-1 Alpha Inhibitor Human Recombinant
FIH1, FIH-1, HIF1AN, Factor Inhibiting HIF1A, Hypoxia-inducible factor 1-alpha inhibitor, Hypoxia-inducible factor asparagine hydroxylase, Factor inhibiting HIF-1, FLJ20615, FLJ22027, DKFZp762F1811.
Product # :
PRO-662Price :
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Description
HIF1AN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (1-349) and having a molecular mass of 40.2kDa. The HIF1AN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein solution (1mg/ml) contains 20mM Tris-HCl pH-8.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Overexpression of the HIF1AN is linked with tumor aggressiveness in pancreatic endocrine tumors. HIF1AN hydroxylates Notch ICD at two residues that are crucial for the function of Notch ICD as a transactivator within cells and during neurogenesis and myogenesis. HIF1AN is commonly expressed in invasive breast carcinoma. The hypoxic response and survival recommends that tumour regulation of HIF1AN is an additional important mechanism for HIF pathway activation. HIF1AN is an asparaginyl hydroxylase enzyme that controls the transcriptional activity of hypoxia-inducible factor. FIH1 is a part of the Fe2+ and 2-oxoglutarate-dependent dioxygenase superfamily, FIH1 is protein that hydoxylates a specific asparagine residue (Asn-803) within the HIF1A C-terminal transactivation domain. In normoxia, the HIF1AN-mediated hydroxylation of the HIF1? transactivation domain which results in blockage of the HIF1A-p300/CBP interaction and represses transcriptional activity of HIF1A targeted genes.
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Synonyms
FIH1, FIH-1, HIF1AN, Factor Inhibiting HIF1A, Hypoxia-inducible factor 1-alpha inhibitor, Hypoxia-inducible factor asparagine hydroxylase, Factor inhibiting HIF-1, FLJ20615, FLJ22027, DKFZp762F1811.
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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
MAATAAEAVA SGSGEPREEA GALGPAWDES QLRSYSFPTR PIPRLSQSDP RAEELIENEE PVVLTDTNLV YPALKWDLEY LQENIGNGDF SVYSASTHKF LYYDEKKMAN FQNFKPRSNR EEMKFHEFVE KLQDIQQRGG EERLYLQQTL NDTVGRKIVM DFLGFNWNWI NKQQGKRGWG QLTSNLLLIG MEGNVTPAHY DEQQNFFAQI KGYKRCILFP PDQFECLYPY PVHHPCDRQS QVDFDNPDYE RFPNFQNVVG YETVVGPGDV LYIPMYWWHH IESLLNGGIT ITVNFWYKGA PTPKRIEYPL KAHQKVAIMR NIEKMLGEAL GNPQEVGPLL NTMIKGRYN.
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 :
MYL7 HumanDescription:
Myosin Light Chain 7 Human Recombinant
Myosin light chain 7 regulatory, myosin light polypeptide 7 regulatory, Myosin light chain 2a myosin regulatory light chain 2 atrial isoform, MYL2A, MYLC2A.
Product # :
PRO-1109Price :
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Description
MYL7 Human Recombinant produced in E. coli is a single polypeptide chain containing 199 amino acids (1-175) and having a molecular mass of 22.0kDa.MYL7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MYL7 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
MYL7 protein is an atrial isoform of myosin regulatory light chain 2 (MYL2). Myosin is a hexamer containing 4 light chains and 2 heavy chains. MYL7 is mainly expressed in adult atrial muscle.
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Synonyms
Myosin light chain 7 regulatory, myosin light polypeptide 7 regulatory, Myosin light chain 2a myosin regulatory light chain 2 atrial isoform, MYL2A, MYLC2A.
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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 MGSHMASRKA GTRGKVAATK QAQRGSSNVF SMFEQAQIQE FKEAFSCIDQ NRDGIICKAD LRETYSQLGK VSVPEEELDA MLQEGKGPIN FTVFLTLFGE KLNGTDPEEA ILSAFRMFDP SGKGVVNKDE FKQLLLTQAD KFSPAEVEQM FALTPMDLAG NIDYKSLCYI ITHGDEKEE
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 :
HNRNPA1 HumanDescription:
Heterogeneous Nuclear Ribonucleoprotein A1 Human Recombinant
Heterogeneous nuclear ribonucleoprotein A1, hnRNP A1, Helix-destabilizing protein, Single-strand RNA-binding protein, hnRNP core protein A1, HNRNPA1, HNRPA1, HNRPA1L3, hnRNP-A1.
Product # :
PRO-1038Price :
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Description
HNRNPA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-320 a.a.) and having a molecular mass of 36.6kDa.HNRNPA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HNRNPA1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Heterogeneous nuclear ribonucleoprotein A1 (HNRNPA1) is a member of the A/B subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). HNRNPA1 is involved in the packing of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may control splice site selection. The HNRNPA1 protein may also have a role in HCV RNA replication. In addition, HNRNPA1 is believed to have a key role in the formation of specific myometrial protein species in parturition.
The hnRNP proteins have distinctive nucleic acid binding properties. HNRNPA1 has 2 repeats of quasi-RRM domains that bind to RNAs. HNRNPA1 is one of the most copious core proteins of hnRNP complexes and it is restricted to the nucleoplasm. The HNRNPA1 protein, along with other hnRNP proteins, is exported from the nucleus, most likely bound to mRNA, and is immediately re-imported. The M9 domain of HNRNPA1 functions as both a nuclear localization and nuclear export signal. -
Synonyms
Heterogeneous nuclear ribonucleoprotein A1, hnRNP A1, Helix-destabilizing protein, Single-strand RNA-binding protein, hnRNP core protein A1, HNRNPA1, HNRPA1, HNRPA1L3, hnRNP-A1.
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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 MGSMSKSESP KEPEQLRKLF IGGLSFETTD ESLRSHFEQW GTLTDCVVMR DPNTKRSRGF GFVTYATVEE VDAAMNARPH KVDGRVVEPK RAVSREDSQR PGAHLTVKKI FVGGIKEDTE EHHLRDYFEQ YGKIEVIEIM TDRGSGKKRG FAFVTFDDHD SVDKIVIQKY HTVNGHNCEV RKALSKQEMA SASSSQRGRS GSGNFGGGRG GGFGGNDNFG RGGNFSGRGG FGGSRGGGGY GGSGDGYNGF GNDGSNFGGG GSYNDFGNYN NQSSNFGPMK GGNFGGRSSG PYGGGGQYFA KPRNQGGYGG SSSSSSYGSG RRF.
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 :
HPRT1 HumanDescription:
Hypoxanthine-Guanine Phosphoribosyltransferase Human Recombinant
Hypoxanthine-Guanine Phosphoribosyltransferase , EC 2.4.2.8, HGPRT, HGPRTase, HPRT, HPRT1.
Product # :
ENZ-524Price :
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Shipped with Ice Packs
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Description
HPRT1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 238 amino acids (1-218 a.a.) and having a molecular mass of 26.7 kDa. The HPRT1 is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HPRT1 Human solution containing 20mM Tris HCl pH-8, & 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HPRT1 has a main part in the generation of purine nucleotides through the purine salvage pathway. HPRT1 primarily functions to salvage purines from degraded DNA to renewed purine synthesis. Therefore, it performs as a catalyst in the reaction between guanine and phosphoribosyl pyrophosphate to form GMP.
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Synonyms
Hypoxanthine-Guanine Phosphoribosyltransferase , EC 2.4.2.8, HGPRT, HGPRTase, HPRT, HPRT1.
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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 MATRSPGVVI SDDEPGYDLD LFCIPNHYAE DLERVFIPHG LIMDRTERLA RDVMKEMGGH HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI RLKSYCNDQS TGDIKVIGGD DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV RQYNPKMVKV ASLLVKRTPR SVGYKPDFVG FEIPDKFVVG YALDYNEYFR DLNHVCVISE TGKAKYKA.
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 :
DLD HumanDescription:
Dihydrolipoamide Dehydrogenase Human Recombinant
EC 1.8.1.4, DLD, DLDH, GCSL, PHE3, Dihydrolipoyl dehydrogenase mitochondrial, Dihydrolipoamide dehydrogenase, Glycine cleavage system L protein, LAD, E3.
Product # :
ENZ-502Price :
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Description
DLD Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 511 amino acids (36-509 a.a.) and having a molecular mass of 54.4 kDa. The DLD is fused to a 37 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DLD solution contains 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
DLD is an L protein of the mitochondrial glycine cleavage system which is also a component of the pyruvate dehydrogenase complex, the alpha-ketoglutarate dehydrogenase complex, and the branched-chain alpha-keto acide dehydrogenase complex. DLD mutations were found in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency.
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Synonyms
EC 1.8.1.4, DLD, DLDH, GCSL, PHE3, Dihydrolipoyl dehydrogenase mitochondrial, Dihydrolipoamide dehydrogenase, Glycine cleavage system L protein, LAD, E3.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMADQ PIDADVTVIG SGPGGYVAAI KAAQLGFKTV CIEKNETLGG TCLNVGCIPS KALLNNSHYY HMAHGKDFAS RGIEMSEVRL NLDKMMEQKS TAVKALTGGI AHLFKQNKVV HVNGYGKITG KNQVTATKAD GGTQVIDTKN ILIATGSEVT PFPGITIDED TIVSSTGALS LKKVPEKMVV IGAGVIGVEL GSVWQRLGAD VTAVEFLGHV GGVGIDMEIS KNFQRILQKQ GFKFKLNTKV TGATKKSDGK IDVSIEAASG GKAEVITCDV LLVCIGRRPF TKNLGLEELG IELDPRGRIP VNTRFQTKIP NIYAIGDVVA GPMLAHKAED EGIICVEGMA GGAVHIDYNC VPSVIYTHPE VAWVGKSEEQ LKEEGIEYKV GKFPFAANSR AKTNADTDGM VKILGQKSTD RVLGAHILGP GAGEMVNEAA LALEYGASCE DIARVCHAHP TLSEAFREAN LAASFGKSIN F.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SH3BGRL2 HumanDescription:
SH3 Domain Binding Glutamic Acid-Rich Protein Like 2 Human Recombinant
SH3 Domain Binding Glutamic Acid-Rich Protein Like 2, Fovea-Associated SH3 Domain-Binding Protein, FASH3.
Product # :
PRO-1215Price :
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Description
SH3BGRL2 Human Recombinant produced in E. coli is a single polypeptide chain containing 130 amino acids (1-107) and having a molecular mass of 14.7 kDa.SH3BGRL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SH3BGRL2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SH3 domain-binding glutamic acid-rich-like protein 2 (SH3BGRL2) belongs to the human SH3BGR family. SH3BGRL2 is a protein of 107 amino acids, which, like SH3BGRL and SH3BGRL3 proteins, is highly homologous to the N-terminal region of the SH3BGR protein and seems to be related to Glutaredoxins and to PKC-interacting cousin of thioredoxin homology domain. SH3BGRL2 is highly expressed in the brain, placenta, liver and kidney and it is also expressed in the retina. The SH3BGRL2 gene is located to chromosome 6q13-15 and its messenger RNA has a large 3' untranslated region containing several AUUUA repeats.
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Synonyms
SH3 Domain Binding Glutamic Acid-Rich Protein Like 2, Fovea-Associated SH3 Domain-Binding Protein, FASH3.
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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 MGSMVIRVFI ASSSGFVAIK KKQQDVVRFL EANKIEFEEV DITMSEEQRQ WMYKNVPPEK KPTQGNPLPP QIFNGDRYCG DYDSFFESKE SNTVFSFLGL KPRLASKAEP
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 :
HSPA5 (19-654) HumanDescription:
Heat Shock 70kDa protein 5 (19-654 a.a.) Human Recombinant
78 kDa glucose-regulated protein, GRP-78, Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78, Heat shock 70 kDa protein 5, Immunoglobulin heavy chain-binding protein, BiP, HSPA5, GRP78, MIF2, FLJ26106.
Product # :
HSP-058Price :
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Description
HSPA5 (19-654) Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 659 amino acids (19-654) and having a molecular mass of 72.9kDa.HSPA5 (19-654) is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HSPA5 (19-654) solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Binding immunoglobulin protein (BiP or HSPA5) is a member of the family of ~70kDa heat shock proteins (HSP 70). HSPA5 is a stress response protein which is induced by agents or conditions that adversely affect endoplasmic reticulum (ER) function. HSPA5 is crucial for the proper glycosylation, folding as well as for the maintenance of cell homeostasis and the prevention of apoptosis.
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Synonyms
78 kDa glucose-regulated protein, GRP-78, Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78, Heat shock 70 kDa protein 5, Immunoglobulin heavy chain-binding protein, BiP, HSPA5, GRP78, MIF2, FLJ26106.
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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 MGSEEEDKKE DVGTVVGIDL GTTYSCVGVF KNGRVEIIAN DQGNRITPSY VAFTPEGERL IGDAAKNQLT SNPENTVFDA KRLIGRTWND PSVQQDIKFL PFKVVEKKTK PYIQVDIGGG QTKTFAPEEI SAMVLTKMKE TAEAYLGKKV THAVVTVPAY FNDAQRQATK DAGTIAGLNV MRIINEPTAA AIAYGLDKRE GEKNILVFDL GGGTFDVSLL TIDNGVFEVV ATNGDTHLGG EDFDQRVMEH FIKLYKKKTG KDVRKDNRAV QKLRREVEKA KRALSSQHQA RIEIESFYEG EDFSETLTRA KFEELNMDLF RSTMKPVQKV LEDSDLKKSD IDEIVLVGGS TRIPKIQQLV KEFFNGKEPS RGINPDEAVA YGAAVQAGVL SGDQDTGDLV LLDVCPLTLG IETVGGVMTK LIPRNTVVPT KKSQIFSTAS DNQPTVTIKV YEGERPLTKD NHLLGTFDLT GIPPAPRGVP QIEVTFEIDV NGILRVTAED KGTGNKNKIT ITNDQNRLTP EEIERMVNDA EKFAEEDKKL KERIDTRNEL ESYAYSLKNQ IGDKEKLGGK LSSEDKETME KAVEEKIEWL ESHQDADIED FKAKKKELEE IVQPIISKLY GSAGPPPTGE EDTAEKDEL.
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 :
DnaK Human, HisDescription:
DnaK Human Recombinant, His Tag
Heat shock 70 kDa protein, heat shock 70kDa protein 1A, HSP70.1, HSP70-1/HSP70-2, HSPA1A, HSPA1, HSPA1B, HSP72, HSP70I, HSP70-1, FLJ54303, FLJ54370, FLJ54392, FLJ54408, FLJ75127, HSP70-1A.
Product # :
HSP-170Price :
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Description
HSP 70kDa produced in E.Coli is a single, non-glycosylated polypeptide chain (1-641 a.a.) containing 661 amino acids fused to a 20 a.a. His-tag at N-terminus and having a total Mw of 72.2 kDa.
Source
Escherichia Coli.
Formulation
The Heat Shock Protein 70kDa contains 20mM Tris-HCl pH7.5 and 2mM DTT at a concentration of 1mg/ml.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HSP70 is a human heat shock protein. HSP-70 is an important part of the cell's machinery for protein folding, and help to protect cells from stress. In most species, there are many proteins that belong to the HSP70 family. Some of these are only expressed under stress conditions, while some are present in cells under normal growth conditions and are not heat-inducible. They can be found in different cellular compartments (nuclear, cytosolic, mitochondrial, endoplasmic reticulum, etc...).
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Synonyms
Heat shock 70 kDa protein, heat shock 70kDa protein 1A, HSP70.1, HSP70-1/HSP70-2, HSPA1A, HSPA1, HSPA1B, HSP72, HSP70I, HSP70-1, FLJ54303, FLJ54370, FLJ54392, FLJ54408, FLJ75127, HSP70-1A.
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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 MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPSYVAFTDTERL IGDAAKNQVA LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDKPKVQVSYKGD TKAFYPEEIS SMVLTKMKEI AEAYLGYPVT NAVITVPAYF NDSQRQATKDAGVIAGLNVL RIINEPTAAA IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVKATAGDTHLGG EDFDNRLVNH FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLSLGLETAGGVM TALIKRNSTI PTKQTQIFTT YSDNQPGVLI QVYEGERAMT KDNNLLGRFELSGIPPAPRG VPQIEVTFDI DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQEAEKYKAEDE VQRERVSAKN ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEVD.
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 :
BHMT HumanDescription:
Betaine Homocysteine S-Methyltransferase Human Recombinant
BHMT, Betaine Homocysteine S-Methyltransferase 1, BHMT1.
Product # :
ENZ-292Price :
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Description
Betaine Homocysteine S-Methyltransferase Human Recombinant fused to His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 443 amino acids (21-236) and having a molecular mass of 49.2 kDa. The BHMT is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BHMT solution contains 20mM Tris-HCl pH-7.5 and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Betaine-homocysteine methyltransferase (BHMT) is a cytosolic enzyme that catalyzes the conversion of betaine and homocysteine to dimethylglycine and methionine, respectively. BHMT displays differential expression in a model of liver cirrhosis.
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Synonyms
BHMT, Betaine Homocysteine S-Methyltransferase 1, BHMT1.
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Physical Appearance
Sterile Filtered clear colorless solution 1 mg/ml.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMPP VGGKKAKKGI LERLNAGEIV IGDGGFVFAL EKRGYVKAGP WTPEAAVEHP EAVRQLHREF LRAGSNVMQT FTFYASEDKL ENRGNYVLEK ISGQEVNEAA CDIARQVADE GDALVAGGVS QTPSYLSCKS ETEVKKVFLQ QLEVFMKKNV DFLIAEYFEH VEEAVWAVET LIASGKPVAA TMCIGPEGDL HGVPPGECAV RLVKAGASII GVNCHFDPTI SLKTVKLMKE GLEAARLKAH LMSQPLAYHT PDCNKQGFIDLPEFPFGLEP RVATRWDIQK YAREAYNLGV RYIGGCCGFE PYHIRAIAEE LAPERGFLPPASEKHGSWGS GLDMHTKPWV RARARKEYWE NLRIASGRPY NPSMSKPDGW GVTKGTAELM QQKEATTEQQ LKELFEKQKF KSQ.
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 :
TEK Human FcDescription:
TEK Tyrosine Kinase Endothelial Fc Chimera Human Recombinant
Angiopoietin-1 receptor precursor, Tyrosine-protein kinase receptor TIE-2, hTIE2, Tyrosine-protein kinase receptor TEK, p140 TEK, Tunica interna endothelial cell kinase, CD202b, VMCM, VMCM1, TIE2.
Product # :
PKA-248Price :
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Shipping Method :
Shipped at Room temp
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Description
Soluble TEK Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is a monomeric, glycosylated, polypeptide containing 730 amino acids and having a total molecular mass of 250 kDa. Human TIE-2/Fc monomer has a calculated molecular mass of approximately 125 kDa. As a result of glycosylation, the recombinant protein migrates as an approximately 140 kDa protein in SDS-PAGE under reducing conditions.The TEK Fc Chimera is purified by proprietary chromatographic techniques.
Source
Insect Cells.
Formulation
TEK Fc Chimera was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.
Purity
Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
TIE-1 (tyrosine kinase with Ig and EGF homology domains 1) and TIE-2/Tek comprise a receptor tyrosine kinase (RTK) subfamily with unique structural characteristics: two immunoglobulin-like domains flanking three epidermal growth factor (EGF)-like domains and followed by three fibronectin type III-like repeats in the extracellular region and a split tyrosine kinase domain in the cytoplasmic region. These receptors are expressed primarily on endothelial and hematopoietic progenitor cells and play critical roles in angiogenesis, vasculogenesis and hematopoiesis. Human TIE-1 cDNA encodes a 1122 amino acid (aa) residue precursor protein with an 18 residue putative signal peptide, a 726 residue extracellular domain and a 353 residue cytoplasmic domain. Two ligands, angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2), which bind TIE-2 with high-affinity have been identified. Ang2 has been reported to act as an antagonist for Ang1. Mice engineered to overexpress Ang2 or to lack Ang1 or Tie-1 display similar angiogenic defects.
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Synonyms
Angiopoietin-1 receptor precursor, Tyrosine-protein kinase receptor TIE-2, hTIE2, Tyrosine-protein kinase receptor TEK, p140 TEK, Tunica interna endothelial cell kinase, CD202b, VMCM, VMCM1, TIE2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized sTIE-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TEK 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 TIE-2 Fc Chimera in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TNF b HumanDescription:
Tumor Necrosis Factor-Beta Human Recombinant
Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, LT, TNFB, TNFSF1.
Product # :
CYT-224Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Tumor Necrosis Factor-b Human Recombinant (Lymphotoxin) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 18645 Dalton. The TNF-b is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized protein with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAG.Biological Activity
The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.05ng/ml, corresponding to a Specific Activity of 20,000,000IU/mg.Citations
More Info
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Introduction
Lymphotoxin alpha, a member of the tumor necrosis factor family, is a cytokine produced by lymphocytes. LTA is highly inducible, secreted, and exists as homotrimeric molecule. LTA forms heterotrimers with lymphotoxin-beta which anchors lymphotoxin-alpha to the cell surface. LTA mediates a large variety of inflammatory, immunostimulatory, and antiviral responses. LTA is also involved in the formation of secondary lymphoid organs during development and plays a role in apoptosis.
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Synonyms
Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, LT, TNFB, TNFSF1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Tumor Necrosis Factor-b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-b 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 Tumor Necrosis Factor-beta 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
MLPGVGLTPS AAQTARQHPK MHLAHSTLKP AAHLIGDPSK QNSLLWRANT DRAFLQDGFS LSNNSLLVPT SGIYFVYSQV VFSGKAYSPK ATSSPLYLAH EVQLFSSQYP FHVPLLSSQK MVYPGLQEPW LHSMYHGAAF QLTQGDQLST HTDGIPHLVL SPSTVFFGAF AL.
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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 1.082 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 calibrated solution of TNF-b 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 :
TNNT2 Human, HisDescription:
Cardiac Muscle Troponin T Human Recombinant, His Tag
CMH2, RCM3, TnTC, cTnT, CMPD2, MGC3889, TNNT2, Troponin T- cardiac muscle, Cardiac muscle troponin T, troponin T type 2 (cardiac).
Product # :
PRO-703Price :
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Shipped with Ice Packs
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Description
TNNT2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 305 amino acids (1-285 a.a.) and having a molecular mass of 36.4 kDa. The TNNT2 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TNNT2 solution contains 20mM Tris pH-8.0, 50% glycerol, 0.1mM PMSF, 0.5M NaCl, 1mM DTT and 100mM imidazole.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
TNNT2 is the tropomyosin-binding subunit of the troponin complex, which is situated on the thin filament of striated muscles and regulates muscle contraction in response to alterations in intracellular calcium ion concentration. Mutations in TNNT2 gene are related with familial hypertrophic cardiomyopathy as well as with dilated cardiomyopathy. TNNT2 mutation takes part in hypertrophic cardiomyopathy.
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Synonyms
CMH2, RCM3, TnTC, cTnT, CMPD2, MGC3889, TNNT2, Troponin T- cardiac muscle, Cardiac muscle troponin T, troponin T type 2 (cardiac).
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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).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSDIEEVVEE YEEEEQEEAA VEEQEEAAEE DAEAEAETEE TRAEEDEEEE EAKEAEDGPM EESKPKPRSF MPNLVPPKIP DGERVDFDDI HRKRMEKDLN ELQALIEAHF ENRKKEEEEL VSLKDRIERR RAERAEQQRI RNEREKERQN RLAEERARRE EEENRRKAED EARKKKALSN MMHFGGYIQK TERKSGKRQT EREKKKKILA ERRKVLAIDH LNEDQLREKA KELWQSIYNL EAEKFDLQEK FKQQKYEINV LRNRINDNQK VSKTRGKAKV TGRWK.
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 :
CCL4L1 Human, HisDescription:
LAG-1 (CCL4L1) Human Recombinant, His Tag
C-C motif chemokine 4-like, Lymphocyte activation gene 1 protein, LAG-1, Macrophage inflammatory protein 1-beta, MIP-1-beta, Monocyte adherence-induced protein 5-alpha, Small-inducible cytokine A4-like, CCL4L1, CCL4L, LAG1, SCYA4L1, CCL4L2, SCYA4L2, AT744.2.
Product # :
CHM-272Price :
Quantity :
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Shipped with Ice Packs
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Description
LAG-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 94 amino acids (24-92 a.a.) and having a molecular mass of 10.5kDa (Molecular weight on SDS-PAGE will appear higher).LAG-1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LAG-1 protein solution (0.5mg/ml) containing 10mM sodium citrate (pH 3.5) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CCL4L1 (C-C motif chemokine 4-like) is a member of to intercrine beta (chemokine CC) family. The CCL4L1 protein is similar to CCL4 which inhibits HIV replication in peripheral blood monocytes which express CCR5.
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Synonyms
C-C motif chemokine 4-like, Lymphocyte activation gene 1 protein, LAG-1, Macrophage inflammatory protein 1-beta, MIP-1-beta, Monocyte adherence-induced protein 5-alpha, Small-inducible cytokine A4-like, CCL4L1, CCL4L, LAG1, SCYA4L1, CCL4L2, SCYA4L2, AT744.2.
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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 MGSHMAPMGS DPPTACCFSY TARKLPRNFV VDYYETSSLC SQPAVVFQTK RGKQVCADPS ESWVQEYVYD LELN.
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Background
What is the molecular weight/Mw of CCL4L1 HUMAN, HIS Protein?
CCL4L1 HUMAN, HIS Protein has a total Mw of 10.5kDa.
What is the source or expression system of CCL4L1 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CCL4L1 HUMAN, HIS Protein?
CCL4L1 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL4L1 HUMAN, HIS Protein?
The biological functionality of CCL4L1 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CCL4L1 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMAPMGS DPPTACCFSY TARKLPRNFV VDYYETSSLC SQPAVVFQTK RGKQVCADPS ESWVQEYVYD LELN.
What applications can CCL4L1 HUMAN, HIS Protein be used in?
CCL4L1 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL4L1 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL4L1 HUMAN, HIS Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL4L1 HUMAN, HIS 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 CCL4L1 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
GGH HumanDescription:
Gamma-Glutamyl Hydrolase Human Recombinant
Gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase), Gamma-Glu-X carboxypeptidase, gamma-glutamyl hydrolase, Conjugase, GH, EC 3.4.19.9.
Product # :
ENZ-242Price :
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Shipping Method :
Shipped with Ice Packs
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Description
GGH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (25-318) and having a molecular mass of 35.9kDa.GGH is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GGH solution (0.5mg/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
-
Introduction
GGH is a homodimeric protein which catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates. GGH is a vital enzyme in folyl and antifolyl poly-gamma-glutamate metabolism and it has a significant part in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of antifolates and pteroylpolyglutamates.
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Synonyms
Gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase), Gamma-Glu-X carboxypeptidase, gamma-glutamyl hydrolase, Conjugase, GH, EC 3.4.19.9.
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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 MRPHGDTAKK PIIGILMQKC RNKVMKNYGR YYIAASYVKY LESAGARVVP VRLDLTEKDY EILFKSINGI LFPGGSVDLR RSDYAKVAKI FYNLSIQSFD DGDYFPVWGT CLGFEELSLL ISGECLLTAT DTVDVAMPLN FTGGQLHSRM FQNFPTELLL SLAVEPLTAN FHKWSLSVKN FTMNEKLKKF FNVLTTNTDG KIEFISTMEG YKYPVYGVQW HPEKAPYEWK NLDGISHAPN AVKTAFYLAE FFVNEARKNN HHFKSESEEE KALIYQFSPI YTGNISSFQQ CYIFD
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 :
TTC32 HumanDescription:
Tetratricopeptide Repeat Domain 32 Human Recombinant
Tetratricopeptide Repeat Domain 32, Tetratricopeptide Repeat Protein 32, TPR Repeat Protein 32.
Product # :
PRO-1246Price :
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Description
TTC32 Human Recombinant produced in E. coli is a single polypeptide chain containing 174 amino acids (1-151) and having a molecular mass of 19.7 kDa. TTC32 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TTC32 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 2mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
TTC32 contains 3 TPR repeats. The tetratricopeptide repeat (TPR) is a structural motif. TPR is observed in organized 3–16 motifs, which form scaffolds to mediate protein–protein interactions and frequently the assembly of multiprotein complexes. TPR-containing proteins include the anaphase-promoting complex subunits cdc16, cdc23 and cdc27, the NADPH oxidase subunit p67-phox, hsp90-binding immunophilins, transcription factors, the major receptor for peroxisomal matrix protein import PEX5, the PKR protein kinase inhibitor and mitochondrial import proteins.
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Synonyms
Tetratricopeptide Repeat Domain 32, Tetratricopeptide Repeat Protein 32, TPR Repeat Protein 32.
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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 MGSMEGQRQE SHATLTLAQA HFNNGEYAEA EALYSAYIRR CACAASSDES PGSKCSPEDL ATAYNNRGQI KYFRVDFYEA MDDYTSAIEV QPNFEVPYYN RGLILYRLGY FDDALEDFKK VLDLNPGFQD ATLSLKQTIL DKEEKQRRNV AKNY.
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 :
PTX3 HumanDescription:
Pentraxin-3 Human Recombinant
TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.
Product # :
PRO-694Price :
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Shipped with Ice Packs
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Description
Recombinant Human PTX3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (18-381 a.a) and having a molecular mass of 44.4 kDa. PTX3 is fused to a 37 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PTX3 protein contains 20mM Tris-HCl buffer pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by Analysis by SDS-PAGE.
Citations
More Info
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Introduction
PTX3 is part of the pentraxin family sharing the C-terminal domain with short pentraxins and containing a unique N-terminal domain. PTX3 is produced and released at inflammatory sites by various cell types including monocytes/macrophages, endothelial cells, vascular smooth muscle cells, fibroblasts, and adipocytes. PTX3 is involved in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility. PTX3 is used as a marker for disease activity of psoriasis. High serum PTX3 levels are associated with the disease severity of systemic sclerosis. Elevated serum PTX3 is associated with pulmonary fungal infections.
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Synonyms
TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMENS DDYDLMYVNL DNEIDNGLHP TEDPTPCDCG QEHSEWDKLF IMLENSQMRE RMLLQATDDV LRGELQRLRE ELGRLAESLA RPCAPGAPAE ARLTSALDEL LQATRDAGRR LARMEGAEAQ RPEEAGRALA AVLEELRQTR ADLHAVQGWA ARSWLPAGCE TAILFPMRSK KIFGSVHPVR PMRLESFSAC IWVKATDVLN KTILFSYGTK RNPYEIQLYL SYQSIVFVVG GEENKLVAEA MVSLGRWTHL CGTWNSEEGL TSLWVNGELA ATTVEMATGH IVPEGGILQI GQEKNGCCVG GGFDETLAFS GRLTGFNIWD SVLSNEEIRE TGGAESCHIR GNIVGWGVTE IQPHGGAQYV 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.
- View Data Sheet
Name :
GSTZ1 HumanDescription:
Glutathione Transferase Zeta 1 Human Recombinant
MAAI, GSTZ-1, MAI, Maleylacetone Isomerase, EC 2.5.1.18, Maleylacetoacetate isomerase, Glutathione S-transferase zeta 1, EC 5.2.1.2, GSTZ1-1, MGC2029, GSTZ1.
Product # :
ENZ-494Price :
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Description
GSTZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-216 a.a.) and having a molecular mass of 26.2 kDa. The GSTZ1 is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The GSTZ1 protein solution contains 1x PBS pH-7.4 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GSTZ1 is part of the glutathione S-transferase super-family which encodes multifunctional enzymes vital in the detoxification of electrophilic molecules, including carcinogens, mutagens, and several therapeutic drugs, by conjugation with glutathione. GSTZ1 participates in the catabolism of phenylalanine and tyrosine. Thus defects in GSTZ1 cause harsh metabolic disorders including alkaptonuria, phenylketonuria and tyrosinaemia. GSTZ1 is a bifunctional protein which has minimal glutathione-conjugating activity with 7-chloro-4-nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. GSTZ1 has low glutathione peroxidase activity with T-butyl and cumene hydroperoxides. GSTZ1 catalyzes the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid.
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Synonyms
MAAI, GSTZ-1, MAI, Maleylacetone Isomerase, EC 2.5.1.18, Maleylacetoacetate isomerase, Glutathione S-transferase zeta 1, EC 5.2.1.2, GSTZ1-1, MGC2029, GSTZ1.
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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 MQAGKPILYS YFRSSCSWRV RIALALKGID YETVPINLIK DGGQQFSKDF QALNPMKQVP TLKIDGITIH QSLAIIEYLE ETRPTPRLLP QDPKKRASVR MISDLIAGGI QPLQNLSVLK QVGEEMQLTW AQNAITCGFN ALEQILQSTA GIYCVGDEVT MADLCLVPQV ANAERFKVDL TPYPTISSIN KRLLVLEAFQ VSHPCRQPDT PTELRA.
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 :
RALA MouseDescription:
V-ral Simian Leukemia Viral Oncogene Homolog A Mouse Recombinant
Ras-related protein Ral-A, Rala, Ral, Ral-a, RALA.
Product # :
PRO-2497Price :
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Description
RALA Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-203 a.a) and having a molecular mass of 25.7kDa. RALA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RALA protein solution (0.5mg/ml) 20mM Tris-Hcl buffer (pH8.5) containing 30% glycerol, 0.1M NaCl and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Ras-related protein Ral-A (RALA) is a member of the small GTPase superfamily, Ras family of proteins. RALA mediates a distinct downstream signaling pathway from Ras which facilitates cellular transformation. Furthermore, RALA is thought to be involved in various signaling cascades, including regulation of the cytoskeleton, vesicle trafficking, and endocytosis.
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Synonyms
Ras-related protein Ral-A, Rala, Ral, Ral-a, RALA.
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Physical Appearance
Sterile Filtered clear 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 MGSHMAANKP KGQNSLALHK VIMVGSGGVG KSALTLQFMY DEFVEDYEPT KADSYRKKVV LDGEEVQIDI LDTAGQEDYA AIRDNYFRSG EGFLCVFSIT EMESFAATAD FREQILRVKE DENVPFLLVG NKSDLEDKRQ VSVEEAKNRA DQWNVNYVET SAKTRANVDK VFFDLMREIR ARKMEDSKEK NGKKKRKSLA KRIRERC
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 :
YWHAB HumanDescription:
Tyr-3/Trp- 5 Monooxygenase Activation Protein Beta Human Recombinant
14-3-3 protein beta/alpha, Protein kinase C inhibitor protein 1, Protein 1054, YWHAB, HS1, GW128, KCIP-1, Tyr-3/Trp- 5 Monooxygenase Activation Protein Beta, 14-3-3 Beta.
Product # :
PKA-348Price :
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Description
YWHAB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 246 amino acids (1-246) and having a molecular mass of 28kDa. YWHAB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The YWHAB protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM EDTA & 50mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
YWHAB belongs to the 14-3-3 family of proteins which are in charge for signal transduction by binding to phosphoserine-containing proteins. YWHAB is found in both plants and mammals. YWHAB protein interacts with RAF1 and CDC25 phosphatases,thus linking mitogenic signaling and the cell cycle machinery. YWHAB is an adapter protein involved in the regulation of a large spectrum of both general and specialized signaling pathway. YWHAB binds to a large number of proteins by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.
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Synonyms
14-3-3 protein beta/alpha, Protein kinase C inhibitor protein 1, Protein 1054, YWHAB, HS1, GW128, KCIP-1, Tyr-3/Trp- 5 Monooxygenase Activation Protein Beta, 14-3-3 Beta.
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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
MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL ELLDKYLIPN ATQPESKVFY LKMKGDYFRY LSEVASGDNK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD
AGEGEN.
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 :
AHCY Human, Sf9Description:
Adenosylhomocysteinase Human Recombinant, Sf9
EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.
Product # :
ENZ-1034Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AHCY Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 441 amino acids (1-432 a.a.) and having a molecular mass of 48.8kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). AHCY is fused to a 6 amino acids His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
AHCY protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
AHCY is an enzyme that catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). AHCY controls the intracellular S-adenosylhomocysteine (SAH) concentration that is crucial for transmethylation reactions. AHCY deficiency causes hypermethioninemia.
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Synonyms
EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.
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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
ADLMSDKLPY KVADIGLAAW GRKALDIAEN EMPGLMRMRE RYSASKPLKG ARIAGCLHMT VETAVLIETL VTLGAEVQWS SCNIFSTQDH AAAAIAKAGI PVYAWKGETD EEYLWCIEQT LYFKDGPLNM ILDDGGDLTN LIHTKYPQLL PGIRGISEET TTGVHNLYKM MANGILKVPA INVNDSVTKS KFDNLYGCRE SLIDGIKRAT DVMIAGKVAV VAGYGDVGKG CAQALRGFGA RVIITEIDPI NALQAAMEGY EVTTMDEACQ EGNIFVTTTG CIDIILGRHF EQMKDDAIVC NIGHFDVEID VKWLNENAVE KVNIKPQVDR YRLKNGRRII LLAEGRLVNL GCAMGHPSFV MSNSFTNQVM AQIELWTHPD KYPVGVHFLP KKLDEAVAEA HLGKLNVKLT KLTEKQAQYL GMSCDGPFKP DHYRYHHHHH 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 :
TTC33 HumanDescription:
Tetratricopeptide Repeat Domain 33 Human Recombinant
Tetratricopeptide Repeat Domain 33, Osmosis-Responsive Factor, Tetratricopeptide Repeat Protein 33, TPR Repeat Protein 33, OSRF.
Product # :
PRO-1217Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TTC33 Human Recombinant produced in E. coli is a single polypeptide chain containing 285 amino acids (1-262) and having a molecular mass of 31.8 kDa.TTC33 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TTC33 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Tetratricopeptide repeat protein 33 (TTC33) is comprised of 3 TPR repeats.
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Synonyms
Tetratricopeptide Repeat Domain 33, Osmosis-Responsive Factor, Tetratricopeptide Repeat Protein 33, TPR Repeat Protein 33, OSRF.
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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 MGS MASFGWK RKIGEKVSKV TSQQFEAEAA DEKDVVDNDE GNWLHAIKRR KEILLEGCAE KSKQLKDEGA SLAENKRYRE AIQKWDEALQ LTPNDATLYE MKSQVLMSLH EMFPAVHAAE MAVQQNPHSW ESWQTLGRAQ LGLGEIILAI RSFQVALHIY
PMNPEIWKED LSWARTLQEQ QKVAQRIKKS EAPAEVTHFS PKSIPDYDFE SDEIVAVCAA IAEKEKTVSA NKTMVIVSAS GAIETVTEKE DGATPPDGSV FIKAR
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 :
GH BovineDescription:
Growth Hormone Bovine Recombinant
BGH, BST, rBGH, rBST, Bovine Somatotropin, Bovine GH, Growth hormone, GH1.
Product # :
CYT-636Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Growth Hormone Bovine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids and having a molecular mass of 21.8 kDa. The GH Bovine Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Bovine Growth Hormone protein was lyophilized from a concentrated (1mg/ml) solution with 4.5mM NaHCO3 adjusted to pH 8-9.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity as determined by the PDFP13B9 cells stably transfected with rabbit GH receptors. Bovine GH is also capable of forming a 1:2 complex with the recombinant ovine growth hormone receptor extracellular domain (ECD).Citations
More Info
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Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
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Synonyms
BGH, BST, rBGH, rBST, Bovine Somatotropin, Bovine GH, Growth hormone, GH1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bovine Growth Hormone although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GH Bovine 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 Bovine Growth Hormone in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Protein content
UV spectroscopy at 280 nm using the absorbency value of 0.63 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.
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 :
TGFA HumanDescription:
Transforming Growth Factor-Alpha Human Recombinant
Transforming Growth Factor Alpha, Protransforming Growth Factor Alpha, TGF-Alpha, TGFA.
Product # :
CYT-871Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TGFA Human Recombinant (40-89) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 50 amino acids and having a molecular mass of 5.6kDa. The TGFA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in 0.1% TFA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured in a proliferation assay using mouse BALB/c 3T3 cells, is 0.395ng/ml.
Citations
More Info
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Introduction
Transforming Growth Factor-Alpha (TGF-alpha) belongs to the EGF family of cytokines. TGFA soluble form is discharged from the membrane by proteolytic cleavage. Membrane-bound proTGF-alpha is biologically active and has a role in cell-cell adhesion or in the stimulation of adjacent cells. TGFA expression is common in transformed cells. Additionally, TGFA is expressed in normal tissues during embryogenesis and in adult cells/tissues, including the pituitary, keratinocytes, and macrophages.
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Synonyms
Transforming Growth Factor Alpha, Protransforming Growth Factor Alpha, TGF-Alpha, TGFA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TGFA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFA 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 TGFA 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
VVSHFNDCPD SHTQFCFHGT CRFLVQEDKP ACVCHSGYVG ARCEHADLLA.
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Background
Title: Transforming Growth Factor-Alpha Human Recombinant, Yeast: A Versatile Biopharmaceutical for Therapeutic Applications
Abstract:
Transforming Growth Factor-Alpha (TGF-α) is a potent growth factor involved in numerous physiological processes, including cell proliferation, differentiation, and tissue repair. The development of TGF-α human recombinant using yeast expression systems has provided a valuable biopharmaceutical tool for therapeutic applications. This research paper explores the production process, characteristics, and potential therapeutic applications of TGF-α human recombinant derived from yeast, highlighting its versatility and clinical significance.Introduction:
TGF-α is a crucial growth factor that regulates cellular functions and plays a vital role in tissue development and repair. Harnessing the therapeutic potential of TGF-α has been limited by challenges in its production and stability. However, the development of TGF-α human recombinant using yeast expression systems has overcome these limitations, making it an attractive biopharmaceutical for therapeutic interventions.Production Process and Characteristics:
TGF-α human recombinant derived from yeast is produced through recombinant DNA technology, utilizing yeast cells as expression hosts. Yeast expression systems offer several advantages, including high expression yields, cost-effectiveness, and the ability to produce correctly folded and biologically active TGF-α. The resulting TGF-α human recombinant closely resembles native TGF-α in terms of structure and function, allowing for effective therapeutic intervention.Therapeutic Applications:
TGF-α human recombinant derived from yeast has shown promise in various therapeutic applications. It has been investigated for its wound-healing properties, where it promotes tissue regeneration and accelerates the healing process. Additionally, TGF-α has been explored in tissue engineering and regenerative medicine, playing a crucial role in stimulating cell proliferation and tissue development. Furthermore, TGF-α has been studied in the context of cancer research, as it is involved in tumor growth and angiogenesis, making it a potential target for anticancer therapies.Advantages and Challenges:
The use of yeast expression systems for producing TGF-α human recombinant offers several advantages, including scalability, cost-effectiveness, and the ability to produce bioactive protein. However, challenges remain, such as optimizing production processes, purification methods, and ensuring product consistency and stability. Further research is needed to address these challenges and maximize the clinical potential of TGF-α human recombinant derived from yeast.Conclusion:
TGF-α human recombinant derived from yeast represents a versatile biopharmaceutical tool with significant therapeutic potential. Its production using yeast expression systems offers advantages in terms of scalability, cost-effectiveness, and bioactivity. The therapeutic applications of TGF-α human recombinant extend to wound healing, tissue engineering, and cancer research. Continued research and development efforts are crucial to optimizing production processes, overcoming challenges, and fully exploiting the clinical benefits of TGF-α human recombinant as a therapeutic agent.
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 :
TRAIL HumanDescription:
TRAIL / APO2 Ligand Human Recombinant
Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.
Product # :
CYT-443Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TRAIL/APO 2 Ligand Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 168 amino acids (Met+Arg115-Gly281) and having a molecular mass of ~21kDa. The sTRAIL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a filtered (0.2µm) solution containing 20mM Tris-HCl pH 8.0 and 150mM NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by the cytolysis of Murine L929 cells in the presence of Actinomycin D, ED50 for this effect is less than 2ng/ml, corresponding to a specific activity of 5,000,000IU/mg.Citations
More Info
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Introduction
TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.
In humans, the gene that encodes for TRAIL is located at chromosome 3q26. TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues. -
Synonyms
Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized APO 2 Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TRAIL 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 TRAIL 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
MRERGPQRVA AHITGTRGRS NTLSSPNSKN EKALGRKINS WESSRSGHSF LSNLHLRNGE LVIHEKGFYY IYSQTYFRFQ EEIKENTKND KQMVQYIYKY TSYPDPILLM KSARNSCWSK DAEYGLYSIY QGGIFELKEN DRIFVSVTNE HLIDMDHEAS FFGAFLVG.
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.