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1000 results found for “cyclin-dependent kinase”
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Name :
YWHAH Human, HisDescription:
Tyr-3/Trp-5 Monooxygenase Activation Protein ETA Human Recombinant, His Tag
14-3-3 ETA, YWHAH, YWHA1, Protein AS1, Tyr-3/Trp-5 Monooxygenase Activation Protein ETA.
Product # :
PKA-347Price :
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Shipped with Ice Packs
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Description
YWHAH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 266 amino acids and having a molecular mass of 30.3 kDa. YWHAH is fused to an N-Terminal His Tag and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
YWHAH solution containing 20mM Tris pH-8.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
YWHAH belongs to the 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins. 14-3-3 ETA is found in plants and mammals, and there is 99% identity to the mouse, rat and bovine orthologs. YWHAH gene contains a 7 base pair repeat sequence in its 5' UTR, and changes in the number of this repeat has been associated with early-onset schizophrenia.
14-3-3 eta is specific to the site of joint inflammation.
14-3-3 proteins are colocalized with Lewy bodies in Parkinson disease, though there is no specific staining for the 14-3-3 eta subunit.
There are 3 different isoforms types of 14-3-3: Beta, Gamma and ETA that are DAL-1/Protein 4.1B-binding proteins. -
Synonyms
14-3-3 ETA, YWHAH, YWHA1, Protein AS1, Tyr-3/Trp-5 Monooxygenase Activation Protein ETA.
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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 MGDREQLLQR ARLAEQAERY DDMASAMKAV TELNEPLSNE DRNLLSVAYK NVVGARRSSW RVISSIEQKT MADGNEKKLE KVKAYREKIE KELETVCNDV LSLLDKFLIK NCNDFQYESK VFYLKMKGDY YRYLAEVASG EKKNSVVEAS EAAYKEAFEI SKEQMQPTHP IRLGLALNFS VFYYEIQNAP EQACLLAKQA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDE EAGEGN.
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 :
CBR1 AntibodyDescription:
Carbonyl Reductase-1, Monoclonal Mouse Anti Human Antibody
Carbonyl Reductase 1, SDR21C1, Prostaglandin-E(2) 9-reductase, NADPH-dependent carbonyl reductase 1, CBR, hCBR1, 15-hydroxyprostaglandin dehydrogenase, CRN.
Product # :
ANT-032Price :
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Formulation
1mg/ml containing Phosphate-Buffered Saline (pH 7.4) with 0.1% Sodium Azide.
More Info
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Introduction
CBR1 is a NADPH-dependent, monomeric, and cytosolic enzyme which is related to a family of short-chain dehydrogenases/reductases. CBR1 protein (277 a.a.) is broadly spread in human tissues such as liver, epidermis, stomach, small intestine, kidney, neuronal cells, and smooth muscle fiber. CBR1 metabolizes numerous toxic environmental quinones and pharmacological relevant substrates such as the anticancer drug, doxorubicin. The best substrates of CBR1 are quinones, including ubiquinone-1 and tocophrolquinone (vitamin E).
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Synonyms
Carbonyl Reductase 1, SDR21C1, Prostaglandin-E(2) 9-reductase, NADPH-dependent carbonyl reductase 1, CBR, hCBR1, 15-hydroxyprostaglandin dehydrogenase, CRN.
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Immunogen
Anti-human CBR1 mAb is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human CBR1 protein.
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Ig Subclass
Mouse IgG2a heavy chain and Kappa light chain
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Clone
4E12.
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Applications
The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1:1,000.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
Recombinant human CBR1 (1-277 aa ) purified from E. coli
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 :
PPP3CA HumanDescription:
Protein Phosphatase 3, Catalytic subunit, Alpha Isozyme Human Recombinant
Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform, CAM-PRP catalytic subunit, Calmodulin-dependent calcineurin A subunit alpha isoform, PPP3CA, CALNA, CAN, CALN, CCN1, CNA1, PPP2B, CALNA1.
Product # :
ENZ-051Price :
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Description
PPP3CA Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 534 amino acids (1-511 a.a.) and having a molecular mass of 60kDa. The PPP3CA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PPP3CA solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT, 1mM EDTA and 20% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
PPP3CA (aka Calcineurin A) is a major soluble calmodulin binding protein in the brain and a Ca2+/calmodulin dependent serine/threonine protein phosphatase, with a relatively limited substrate specificity. PPP3CA activates the T cells of the immune system and can be blocked by drugs. PPP3CA activates NFATc (a transcription factor) by dephosphorylating it. The activated NFATc is subsequently translocated into the nucleus, where it upregulates the expression of interleukin 2.
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Synonyms
Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform, CAM-PRP catalytic subunit, Calmodulin-dependent calcineurin A subunit alpha isoform, PPP3CA, CALNA, CAN, CALN, CCN1, CNA1, PPP2B, CALNA1.
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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 TGSMSEPKAI DPKLSTTDRV VKAVPFPPSH RLTAKEVFDN DGKPRVDILK AHLMKEGRLE ESVALRIITE GASILRQEKN LLDIDAPVTV CGDIHGQFFD LMKLFEVGGS PANTRYLFLG DYVDRGYFSI ECVLYLWALK ILYPKTLFLL RGNHECRHLT EYFTFKQECK IKYSERVYDA CMDAFDCLPL AALMNQQFLC VHGGLSPEIN TLDDIRKLDR FKEPPAYGPM CDILWSDPLE DFGNEKTQEH FTHNTVRGCS YFYSYPAVCE FLQHNNLLSI LRAHEAQDAG YRMYRKSQTT GFPSLITIFS APNYLDVYNN KAAVLKYENN VMNIRQFNCS PHPYWLPNFM DVFTWSLPFV GEKVTEMLVN VLNICSDDEL GSEEDGFDGA TAAARKEVIR NKIRAIGKMA RVFSVLREES ESVLTLKGLT PTGMLPSGVL SGGKQTLQSA IKGFSPQHKI TSFEEAKGLD RINERMPPRR DAMPSDANLN SINKALTSET NGTDSNGSNS SNIQ.
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 :
ECHDC1 HumanDescription:
Enoyl CoA Hydratase Domain Containing 1 Human Recombinant
Ethylmalonyl-CoA decarboxylase, Enoyl-CoA hydratase domain-containing protein 1, Methylmalonyl-CoA decarboxylase, MMCD, ECHDC1, dJ351K20.2.
Product # :
ENZ-573Price :
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Description
SNAP25 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids (1-206 a.a.) and having a molecular mass of 25.4 kDa. SNAP25 is fused to a 20 amino acid His Tag at N-terminus and purified by conventional chromatography techniques.
Source
E.coli.
Formulation
The ECHDC1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 0.1M NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Enoyl CoA hydratase domain containing 1 (ECHDC1) is a member of the enoyl-CoA hydratase/isomerase family. ECHDC1 is an enzyme which hydrates the double bond between the second and third carbons on acyl-CoA. The ECHDC1 enzyme is crucial to metabolizing fatty acids to supply both acetyl CoA and energy.
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Synonyms
Ethylmalonyl-CoA decarboxylase, Enoyl-CoA hydratase domain-containing protein 1, Methylmalonyl-CoA decarboxylase, MMCD, ECHDC1, dJ351K20.2.
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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 MALKQEMAKS LLKTASLSGR TKLLHQTGLS LYSTSHGFYE EEVKKTLQQF PGGSIDLQKE DNGIGILTLN NPSRMNAFSG VMMLQLLEKV IELENWTEGK GLIVRGAKNT FSSGSDLNAV KSLGTPEDGM AVCMFMQNTL TRFMRLPLIS VALVQGWALG
GGAEFTTACD FRLMTPESKI RFVHKEMGII PSWGGTTRLV EIIGSRQALK VLSGALKLDS KNALNIGMVE EVLQSSDETK SLEEAQEWLK QFIQGPPEVI RALKKSVCSG RELYLEEALQ NERDLLGTVW GGPANLEAIA KKGKFNK.
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 :
Bcl 2 Human (1-206 a.a.)Description:
B-Cell Leukemia/Lymphoma 2, (1-206 a.a.) Human Recombinant
Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.
Product # :
PRO-630Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Bcl-2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 1-206. The wild type Bcl-2 is missing 12 amino acids from C-terminus. C-terminus is fused to His-Tag. C-terminus his-tag, mimics the deleted C-terminus membrane domain thus maintaining its biological activity. Bcl-2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein contains 10mM Tris-HCl pH-8, 1mM EDTA and 250mM NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
BCL2 gene encodes an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants, produced by alternate splicing, differ in their C-terminal ends.
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Synonyms
Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bcl-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bcl-2 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
Suspend Bcl-2 in 100ul of 0.5M Acetic acid, over night at 4°C. Dilute 10 fold into selected buffer system. BCL-2 has tendency to form intramolecular disulfide bond, 5mM DTT is recommended in assay buffer. When running SDS-PAGE gel, 10mM DTT is recommended.
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 :
UCHL1 Mouse, ActiveDescription:
Ubiquitin Carboxyl-Terminal Esterase L1 Mouse Recombinant, Active
Ubiquitin carboxyl-terminal hydrolase isozyme L1, UCH-L1, Neuron cytoplasmic protein 9.5, PGP 9.5, PGP9.5, Ubiquitin thioesterase L1.
Product # :
PRO-2424Price :
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Shipped with Ice Packs
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Description
UCHL1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-223 a.a) and having a molecular mass of 27.2kDa. UCHL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UCHL1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 70 pmol/min/ug, and is defined as the amount of enzyme that hydrolysis 1.0 pmole of ubiquitin-AMC per minute at pH 7.5, at 37°C.
More Info
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Introduction
Ubiquitin Carboxyl-Terminal Esterase L1 (UCHL1) is a part of a family whose products hydrolyze small C-terminal adducts of ubiquitin to create the ubiquitin monomer. UCHL1 is a part of the ubiquitin system, which regulates many biological activities. UCHL1 is a thiol protease that distinguishes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. UCHL1 binds to free monoubiquitin and avoids its degradation in lysosomes.
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Synonyms
Ubiquitin carboxyl-terminal hydrolase isozyme L1, UCH-L1, Neuron cytoplasmic protein 9.5, PGP 9.5, PGP9.5, Ubiquitin thioesterase L1.
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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 MGSMQLKPME INPEMLNKVL AKLGVAGQWR FADVLGLEEE TLGSVPSPAC ALLLLFPLTA QHENFRKKQI EELKGQEVSP KVYFMKQTIG NSCGTIGLIH AVANNQDKLE FEDGSVLKQF LSETEKLSPE DRAKCFEKNE AIQAAHDSVA QEGQCRVDDK VNFHFILFNN VDGHLYELDG RMPFPVNHGA SSEDSLLQDA AKVCREFTER EQGEVRFSAV ALCKAA.
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 :
ALDH2 HumanDescription:
Aldehyde Dehydrogenase-2 Human Recombinant
ALDM, ALDHI, ALDH-E2, MGC1806, ALDH2, Aldehyde dehydrogenase mitochondrial, ALDH class 2.
Product # :
ENZ-401Price :
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Shipped with Ice Packs
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Description
ALDH2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 501 amino acids (18-517 a.a.) & having a molecular mass of 54.5 kDa. The ALDH2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ALDH2 protein (1mg/ml) contains 20mM Tris-HCl buffer, pH-7.5, 1mM DTT, 1mM EDTA and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity was found to be > 250pmol/min/ug, and was obtained by measuring the increase of NADH in absorbance at 340 nm resulting from the reduction of NAD at pH 8.0 at 25°C.
More Info
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Introduction
ALDH2 is part of the aldehyde dehydrogenase family of proteins which catalyze the chemical transformation from acetaldehyde to acetic acid. ALDH2 is the second enzyme of the major oxidative pathway of alcohol metabolism. ALDH2 has 2 major liver isoforms: cytosolic and mitochondrial, which differ by their electrophoretic mobilities, kinetic properties, and subcellular localizations. Nearly all Caucasians have 2 major isozymes, whereas roughly 50% of Orientals have only the cytosolic isozyme, omitting the mitochondrial isozyme. The extremely higher rate of acute alcohol intoxication with Orientals compared to Caucasians is due to the fact of the absence of mitochondrial isozyme. ALDH2 has a low Km for acetaldehydes, and is localized in mitochondrial matrix.
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Synonyms
ALDM, ALDHI, ALDH-E2, MGC1806, ALDH2, Aldehyde dehydrogenase mitochondrial, ALDH class 2.
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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 prevent freeze-thaw cycles.
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Amino Acid Sequence
MSAAATQAVP APNQQPEVFC NQIFINNEWH DAVSRKTFPT VNPSTGEVIC QVAEGDKEDV DKAVKAARAA FQLGSPWRRM DASHRGRLLNRLADLIERDR TYLAALETLD NGKPYVISYL VDLDMVLKCL RYYAGWADKY HGKTIPIDGD FFSYTRHEPV GVCGQIIPWN FPLLMQAWKL GPALATGNVV VMKVAEQTPL TALYVANLIK EAGFPPGVVN IVPGFGPTAG AAIASHEDVD KVAFTGSTEI GRVIQVAAGS SNLKRVTLEL GGKSPNIIMS DADMDWAVEQ AHFALFFNQG QCCCAGSRTF VQEDIYDEFV ERSVARAKSR VVGNPFDSKT EQGPQVDETQ FKKILGYINT GKQEGAKLLC GGGIAADRGY FIQPTVFGDV QDGMTIAKEE IFGPVMQILK FKTIEEVVGR ANNSTYGLAA AVFTKDLDKA NYLSQALQAGTVWVNCYDVF GAQSPFGGYK MSGSGRELGE YGLQAYTEVK TVTVKVPQKN S.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DHRS9 HumanDescription:
Dehydrogenase/Reductase Member 9 Human Recombinant
Dehydrogenase/reductase SDR family member 9, 3-alpha hydroxysteroid dehydrogenase, 3-alpha-HSD, NADP-dependent retinol dehydrogenase/reductase, RDH-E2, RDHL, Short-chain dehydrogenase/reductase retSDR8, DHRS9, RDH15, RDHTBE, SDR9C4, RETSDR8, 3ALPHA-HSD.
Product # :
ENZ-216Price :
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Shipped with Ice Packs
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Description
DHRS9 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (18-319) and having a molecular mass of 35.9kDa.DHRS9 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DHRS9 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Dehydrogenase/reductase SDR family member 9 (DHRS9) functions as a homotetramer, which converts both 3-alpha-tetrahydroprogesterone (allopregnanolone) and 3-alpha-androstanediol to dihydroxyprogesterone and is believed to have a part in retinoic acid biosynthesis.
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Synonyms
Dehydrogenase/reductase SDR family member 9, 3-alpha hydroxysteroid dehydrogenase, 3-alpha-HSD, NADP-dependent retinol dehydrogenase/reductase, RDH-E2, RDHL, Short-chain dehydrogenase/reductase retSDR8, DHRS9, RDH15, RDHTBE, SDR9C4, RETSDR8, 3ALPHA-HSD.
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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 MGSHMRKGKL KIEDITDKYI FITGCDSGFG NLAARTFDKK GFHVIAACLT ESGSTALKAE TSERLRTVLL DVTDPENVKR TAQWVKNQVG EKGLWGLINN AGVPGVLAPT DWLTLEDYRE PIEVNLFGLI SVTLNMLPLV KKAQGRVINV SSVGGRLAIV GGGYTPSKYA VEGFNDSLRR DMKAFGVHVS CIEPGLFKTN LADPVKVIEK KLAIWEQLSP DIKQQYGEGY IEKSLDKLKG NKSYVNMDLS PVVECMDHAL TSLFPKTHYA AGKDAKIFWI PLSHMPAALQ DFLLLKQKAE LANPKAV.
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 :
BHMT2 HumanDescription:
Betaine-Homocysteine Methyltransferase 2 Human Recombinant
BHMT2, Betaine--Homocysteine S-Methyltransferase 2, SMM-Hcy Methyltransferase, Betaine-Homocysteine Methyltransferase 2, S-Methylmethionine--Homocysteine S-Methyltransferase BHMT2, EC 2.1.1.10, EC 2.1.1.5.
Product # :
ENZ-798Price :
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Shipped with Ice Packs
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Description
BHMT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 386 amino acids (1-363 a.a.) and having a molecular mass of 42.7kDa. BHMT2 is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
BHMT2 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Betaine-Homocysteine Methyltransferase 2 (BHMT2) is involved in the regulation of homocysteine metabolism. Homocysteine is a sulfur-containing amino acid which has a key role in methylation reactions. Transfer of the methyl group from betaine to homocysteine generates methionine, which donates the methyl group to methylate DNA, proteins, lipids, and other intracellular metabolites. BHMT2 is one of two methyl transferases which can catalyze the transfer of the methyl group from betaine to homocysteine. BHMT2 converts homocysteine to methionine using S-methylmethionine (SMM) as a methyl donor. Homocysteine metabolism anomalies are implicated in disorders varying from vascular disease to neural tube birth defects such as spina bifida.
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Synonyms
BHMT2, Betaine--Homocysteine S-Methyltransferase 2, SMM-Hcy Methyltransferase, Betaine-Homocysteine Methyltransferase 2, S-Methylmethionine--Homocysteine S-Methyltransferase BHMT2, EC 2.1.1.10, EC 2.1.1.5.
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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 MGSMAPAGRP GAKKGILERL ESGEVVIGDG SFLITLEKRG YVKAGLWTPE AVIEHPDAVR QLHMEFLRAG SNVMQTFTFS ASEDNMESKW EDVNAAACDL AREVAGKGDA LVAGGICQTS IYKYQKDEAR IKKLFRQQLE VFAWKNVDFL IAEYFEHVEE AVWAVEVLKE SDRPVAVTMC IGPEGDMHDI TPGECAVRLV KAGASIVGVN CRFGPDTSLK TMELMKEGLE WAGLKAHLMV QPLGFHAPDC GKEGFVDLPE YPFGLESRVA TRWDIQKYAR EAYNLGVRYI GGCCGFEPYH IRAIAEELAP ERGFLPPASE KHGSWGSGLD MHTKPWIRAR ARREYWENLL PASGRPFCPS LSKPDF.
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 :
ADAT2 HumanDescription:
Adenosine Deaminase, tRNA-specific 2 Human Recombinant
DEADC1, TAD2.
Product # :
ENZ-561Price :
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Shipped with Ice Packs
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Description
Recombinant Human ADAT2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (1-191 a.a) and having a molecular mass of 23.2 kDa. ADAT2 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ADAT2 (0.5mg/ml) protein contains 20mM Tris-HCl buffer pH-8, 2mM DTT, 50mM NaCl and 10% glycerol.
Purity
Greater than 90% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Adenosine Deaminase (ADA), also recognized as ADAT2 is an enzyme that takes part in purine metabolism. ADAT2 is necessary for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. ADAT2 is involved in the deamination of adenosine-34 to inosine in numerous tRNAs. ADAT2 is part of the cytidine and deoxycytidylate deaminase protein family, ADAT2 employs zinc as a cofactor. ADAT2 is a 191 amino acid enzyme that exists as two isoforms formed by alternative splicing events.
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Synonyms
DEADC1, TAD2.
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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 MEAKAAPKPA ASGACSVSAE ETEKWMEEAM HMAKEALENT EVPVGCLMVY NNEVVGKGRN EVNQTKNATR HAEMVAIDQV LDWCRQSGKS PSEVFEHTVL YVTVEPCIMC AAALRLMKIP LVVYGCQNER FGGCGSVLNI ASADLPNTGR PFQCIPGYRA EEAVEMLKTF YKQENPNAPK SKVRKKECQK S.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
KCTD11 HumanDescription:
Potassium Channel Tetramerisation Domain Containing 11 Human Recombinant
C17orf36, KCASH1, MGC129844, REN, REN/KCTD11, KCTD11, BTB/POZ domain-containing protein KCTD11.
Product # :
PRO-1376Price :
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Description
KCTD11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (1-232a.a) and having a molecular mass of 28kDa. KCTD11 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
KCTD11 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Potassium Channel Tetramerisation Domain Containing 11 (KCTD11) is a 232 amino acid regulator of neuronal differentiation which induces growth arrest, apoptosis and the expression of p27 (cyclin-dependent kinase inhibitor). KCTD11 is expressed most highly in cerebellum. KCTD11 functions as an antagonist of the Hedgehog pathway and activator of the caspase cascade and among its related super-pathways are Melatonin Signaling and Activation of cAMP-Dependent PKA.
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Synonyms
C17orf36, KCASH1, MGC129844, REN, REN/KCTD11, KCTD11, BTB/POZ domain-containing protein KCTD11.
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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 MLGAMFRAGT PMPPNLNSQG GGHYFIDRDG KAFRHILNFL RLGRLDLPRG YGETALLRAE ADFYQIRPLL DALRELEASQ GTPAPTAALL HADVDVSPRL VHFSARRGPH HYELSSVQVD TFRANLFCTD SECLGALRAR FGVASGDRAE GSPHFHLEWA PRPVELPEVE YGRLGLQPLW TGGPGERREV VGTPSFLEEV LRVALEHGFR LDSVFPDPED LLNSRSLRFV RH.
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 :
EFNA1 Human, HEKDescription:
Ephrin A1 Human Recombinant, HEK
Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.
Product # :
PRO-2477Price :
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Description
EFNA1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 19-182) containing 170 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 20.2kDa (calculated).
Source
HEK293 cells.
Formulation
EFNA1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline, pH 7.5 containing 5 % (w/v) trehalose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.
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Synonyms
Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.
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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 one week 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. EFNA1 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
DRHTVFWNSS NPKFRNEDYT IHVQLNDYVD IICPHYEDHS VADAAMEQYI LYLVEHEEYQ LCQPQSKDQV RWQCNRPSAK HGPEKLSEKF QRFTPFTLGK EFKEGHSYYY ISKPIHQHED RCLRLKVTVS GKITHSPQAH DNPQEKRLAA DDPEVRVLHS IGHS HHHHHH.
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 :
TIMP2 Human, HisDescription:
Tissue Inhibitor of Metalloprotease 2 Human Recombinant, His Tag
TIMP metallopeptidase inhibitor 2, metalloproteinase inhibitor 2, Tissue inhibitor of metalloproteinases 2, TIMP-2, CSC-21K.
Product # :
ENZ-646Price :
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Description
TIMP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 232 amino acids (27-220) and having a molecular mass of 26.1 kDa.TIMP2 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TIMP2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
TIMP2 belongs to the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases, a group of peptidases that take part in degradation of the extracellular matrix. Besides having an inhibitory role against metalloproteinases, the encoded protein has a exclusive part among TIMP family members in its capability to directly suppress the proliferation of endothelial cells. Consequently, the encoded protein is crucial to the conservation of tissue homeostasis by suppressing the production of quiescent tissues as an answer to angiogenic factors, and by inhibiting protease activity in tissues undergoing renovation of the extracellular matrix.
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Synonyms
TIMP metallopeptidase inhibitor 2, metalloproteinase inhibitor 2, Tissue inhibitor of metalloproteinases 2, TIMP-2, CSC-21K.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHM CS CSPVHPQQAF CNADVVIRAK AVSEKEVDSG NDIYGNPIKR IQYEIKQIKM FKGPEKDIEF IYTAPSSAVC GVSLDVGGKK EYLIAGKAEG DGKMHITLCD FIVPWDTLST TQKKSLNHRY QMGCECKITR CPMIPCYISS PDECLWMDWV TEKNINGHQA KFFACIKRSD GSCAWYRGAA PPKQEFLDIE DP
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 :
TP53I3 HumanDescription:
Tumor Protein p53 Inducible Protein 3 Human Recombinant
TP53I3, PIG3, Quinone Oxidoreductase, tumor protein p53 inducible protein 3.
Product # :
ENZ-519Price :
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Description
TP53I3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 352 amino acids (1-332 a.a.) and having a molecular mass of 37.6 kDa. TP53I3 protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
1mg/ml solution containing 20mM Tris HCl pH-8, 0.1M NaCl & 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
TP53I3 participates in the generation of reactive oxygen species (ROS). TP53I3 has low NADPH-dependent naphtoquinone reductase activity, with a preference for 1,2-naphtoquinone over 1,4-naphtoquinone. TP53I3 has low NADPH-dependent diamine reductase activity (in vitro). TP53I3 is localized to the cytoplasm and induced in primary, non-transformed and transformed cell cultures after exposure to genotoxic agents. TP53I3 microsatellite polymorphism is associated with differential susceptibility to cancer.
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Synonyms
TP53I3, PIG3, Quinone Oxidoreductase, tumor protein p53 inducible protein 3.
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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 MLAVHFDKPG GPENLYVKEV AKPSPGEGEV LLKVAASALN RADLMQRQGQ YDPPPGASNI LGLEASGHVAELGPGCQGHW KIGDTAMALL PGGGQAQYVT VPEGLLMPIP EGLTLTQAAA IPEAWLTAFQ LLHLVGNVQA GDYVLIHAGL SGVGTAAIQLTRMAGAIPLV TAGSQKKLQM AEKLGAAAGF NYKKEDFSEA TLKFTKGAGV NLILDCIGGS YWEKNVNCLA LDGRWVLYGL MGGGDINGPLFSKLLFKRGS LITSLLRSRD NKYKQMLVNA FTEQILPHFS TEGPQRLLPV LDRIYPVTEI QEAHKYMEAN KNIGKIVLEL PQ.
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 :
SSU72 HumanDescription:
SSU72 RNA Polymerase II CTD Phosphatase Human Recombinant
SSU72 RNA polymerase II CTD phosphatase homolog (S. cerevisiae), HSPC182, CTD phosphatase SSU72, Ssu72 RNA polymerase II CTD phosphatase homolog (yeast), PNAS-120, RNA polymerase II subunit A C-terminal domain phosphatase SSU72, EC 3.1.3.16.
Product # :
ENZ-243Price :
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Description
SSU72 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 217 amino acids (1-194) and having a molecular mass of 25.0kDa.SSU72 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SSU72 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.
More Info
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Introduction
SSU72 is an extremely conserved homologue of yeast Ssu72, a CTD phosphatase and a component of the polyadenylation/termination machinery. SSU72 interacts with TFIIB, Rb and DNAM-1 and operates to catalyze the dephosphorylation of target proteins, and taking part in RNA processing and termination via dephosphorylation of Pol II. SSU72 is found in multiple alternatively spliced isoforms.
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Synonyms
SSU72 RNA polymerase II CTD phosphatase homolog (S. cerevisiae), HSPC182, CTD phosphatase SSU72, Ssu72 RNA polymerase II CTD phosphatase homolog (yeast), PNAS-120, RNA polymerase II subunit A C-terminal domain phosphatase SSU72, EC 3.1.3.16.
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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 MGSMPSSPLR VAVVCSSNQN RSMEAHNILS KRGFSVRSFG TGTHVKLPGP APDKPNVYDF KTTYDQMYND LLRKDKELYT QNGILHMLDR NKRIKPRPER FQNCKDLFDL ILTCEERVYD QVVEDLNSRE QETCQPVHVV NVDIQDNHEE ATLGAFLICE LCQCIQHTED MENEIDELLQ EFEEKSGRTF LHTVCFY
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 :
CANT1 HumanDescription:
Calcium Activated Nucleotidase 1 Human Recombinant
Soluble calcium-activated nucleotidase 1, SCAN-1, Apyrase homolog, Putative MAPK-activating protein PM09, Putative NF-kappa-B-activating protein 107, CANT1, SHAPY, DBQD, SCAN1.
Product # :
PRO-1010Price :
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Description
CANT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (63-401 a.a.) and having a molecular mass of 40.5kDa. CANT1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CANT1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Calcium-activated nucleotidase 1 (CANT1) is a member of the apyrase family. The CANT1 protein is calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is as follows: UDP > GDP > UTP > GTP. Moreover, CANT1 has a very low activity towards ADP and an even lower activity towards ATP. As well as it doesn’t hydrolyze AMP and GMP. CANT1’s specific function is yet unknown, nevertheless its substrates are involved in several key signaling functions, including Ca2+ release, through activation of pyrimidinergic signaling. Mutations in the CANT1 gene are linked with Desbuquois dysplasia with hand anomalies.
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Synonyms
Soluble calcium-activated nucleotidase 1, SCAN-1, Apyrase homolog, Putative MAPK-activating protein PM09, Putative NF-kappa-B-activating protein 107, CANT1, SHAPY, DBQD, SCAN1.
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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 MGSHMRPAPG RPPTHNAHNW RLGQAPANWY NDTYPLSPPQ RTPAGIRYRI AVIADLDTES RAQEENTWFS YLKKGYLTLS DSGDKVAVEW DKDHGVLESH LAEKGRGMEL SDLIVFNGKL YSVDDRTGVV YQIEGSKAVP WVILSDGDGT VEKGFKAEWL AVKDERLYVG GLGKEWTTTT GDVVNENPEW VKVVGYKGSV DHENWVSNYN ALRAAAGIQP PGYLIHESAC WSDTLQRWFF LPRRASQERY SEKDDERKGA NLLLSASPDF GDIAVSHVGA VVPTHGFSSF KFIPNTDDQI IVALKSEEDS GRVASYIMAF TLDGRFLLPE TKIGSVKYEG IEFI.
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 :
CCDC69 HumanDescription:
Coiled-Coil Domain Containing 69 Human Recombinant
Coiled-coil domain-containing protein 69, CCDC69.
Product # :
PRO-1880Price :
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Description
CCDC69 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 319 amino acids (1-296 a.a) and having a molecular mass of 37.2kDa. CCDC69 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CCDC69 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Coiled-Coil Domain Containing 69, also known as CCDC69 is a protein-coding gene. A significant paralog of CCDC69 is MTUS1.
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Synonyms
Coiled-coil domain-containing protein 69, CCDC69.
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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 MGSMGCRHSR LSSCKPPKKK RQEPEPEQPP RPEPHELGPL NGDTAITVQL CASEEAERHQ KDITRILQQH EEEKKKWAQQ VEKERELELR DRLDEQQRVL EGKNEEALQV LRASYEQEKE ALTHSFREAS STQQETIDRL TSQLEAFQAK MKRVEESILS RNYKKHIQDY GSPSQFWEQE LESLHFVIEM KNERIHELDR RLILMETVKE KNLILEEKIT TLQQENEDLH VRSRNQVVLS RQLSEDLLLT REALEKEVQL RRQLQQEKEE LLYRVLGANA SPAFPLAPVT PTEVSFLAT.
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 :
BMPR1A Human, CHODescription:
Bone Morphogenetic Protein Receptor-1A Human Recombinant, CHO
BMPR-1A, BMP-R1A, BMPR1A, BMR1A, CD292, CD-292, Serine/threonine-protein kinase receptor R5, SKR5, ALK-3, ACVRLK3, EC 2.7.11.30, CD292 antigen.
Product # :
CYT-1094Price :
Quantity :
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Shipped at Room temp
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Description
Bone Morphogenetic Protein Receptor-1A Human Recombinant produced in CHO cells is a glycosylated homodimer chain containing 2x362 amino acids and having a total molecular mass of 80.8kDa. BMPR1A is purified by proprietary chromatographic techniques.
Source
CHO cells.
Formulation
The protein was lyophilized from a sterile (0.2µm) filtered solution containing PBS.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as calculated by the Inhibition of human BMP-4-induced alkaline phosphatase production caused by ATDC5 cells is 120ng/ml corresponding to a specific activity of 8.3x10^3 units/mg.
More Info
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Introduction
The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the receptors, ACVR1 and ACVR2. The ligands of these receptors are members of the TGF-beta superfamily. TGF-betas transduce their signals through the formation of heteromeric complexes with 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding.
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Synonyms
BMPR-1A, BMP-R1A, BMPR1A, BMR1A, CD292, CD-292, Serine/threonine-protein kinase receptor R5, SKR5, ALK-3, ACVRLK3, EC 2.7.11.30, CD292 antigen.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BMPR1A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMPR1A should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized BMPR1A 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
QNLDSMLHGT GMKSDSDQKK SENGVTLAPE DTLPFLKCYC SGHCPDDAIN NTCITNGHCF AIIEEDDQGE TTLASGCMKY EGSDFQCKDS PKAQLRRTIE CCRTNLCNQY LQPTLPPVVI GPFFDGSIRI EGRMDDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK.
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Background
Research Paper on Bone Morphogenetic Protein Receptor-1A Human Recombinant, CHO, Monomer, HEK
Abstract:
Welcome to the captivating world of Bone Morphogenetic Protein Receptor-1A Human Recombinant, CHO, Monomer (BMPR-1A HR) in Human Embryonic Kidney Cells (HEK). This research paper explores the vital role of BMPR-1A HR in cellular responses. As a key receptor in the transforming growth factor-beta (TGF-β) superfamily, BMPR-1A HR plays a significant part in guiding cellular differentiation and tissue development. Join us as we unravel the molecular mechanisms behind BMPR-1A HR signaling in HEK cells and delve into its interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).
Introduction:
Welcome to the intriguing world of BMPR-1A HR! In this section, we introduce the remarkable BMPR-1A HR and its crucial role in shaping cellular responses. Together, let's explore how this receptor influences cellular behavior and contributes to tissue growth, fostering our understanding of its importance in biological processes.
BMPR-1A HR Signaling in HEK Cells:
Be amazed by the intricate dance of BMPR-1A HR signaling within HEK cells! Uncover the complex process of ligand-receptor binding, initiating both the canonical SMAD-dependent and non-canonical SMAD-independent pathways. This harmonious interplay regulates a wide range of cellular processes, including gene transcription, cell proliferation, and differentiation, forming the foundation of cellular communication.
Influential Role in Cellular Responses:
Marvel at the influential role of BMPR-1A HR as a critical mediator of cellular responses within HEK cells. Witness its ability to modulate cellular differentiation, driving the expression of key differentiation markers such as DIF. Our exploration will highlight the multifaceted nature of BMPR-1A HR, impacting diverse cellular pathways, including those involving TNF-α and TNFSF2, shaping a dynamic and interconnected cellular network.
Interplay with Key Cytokines:
Discover the intriguing interactions between BMPR-1A HR and key cytokines like TNF-α and TNFSF2. Explore how BMPR-1A HR influences their expression and activity, hinting at potential cross-talk between BMPR-1A HR and inflammatory pathways. This delicate balance fosters a harmonious cellular environment, where multiple players contribute to overall cellular responses.
Therapeutic Implications and Tissue Development:
Witness the potential therapeutic implications of BMPR-1A HR in tissue development. Together, we explore the exciting possibilities of utilizing BMPR-1A HR in regenerative medicine, offering hope for enhanced tissue development and repair. As we venture forth, we also address challenges, such as optimal dosage, innovative delivery methods, and safety considerations, ensuring a responsible and effective approach.
Conclusion:
As we conclude our exploration of BMPR-1A HR in HEK cells, we stand in awe of its role in mediating cellular responses and tissue development. Equipped with this knowledge, we look forward to a promising future, where BMPR-1A HR from CHO cells opens doors to innovative applications in regenerative medicine, contributing to improved human health and well-being.
What is the molecular weight/Mw of BMPR1A Protein?
BMPR1A Protein has a total Mw of 80.8kDa.
What is the source or expression system of BMPR1A Protein?
CHO cells.
What is the Purity of BMPR1A Protein?
BMPR1A Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMPR1A Protein?
The ED50, as calculated by the Inhibition of human BMP-4-induced alkaline phosphatase production caused by ATDC5 cells is 120ng/ml corresponding to a specific activity of 8.3x10^3 units/mg.
What is the amino acid sequence of BMPR1A Protein?
QNLDSMLHGT GMKSDSDQKK SENGVTLAPE DTLPFLKCYC SGHCPDDAIN NTCITNGHCF AIIEEDDQGE TTLASGCMKY EGSDFQCKDS PKAQLRRTIE CCRTNLCNQY LQPTLPPVVI GPFFDGSIRI EGRMDDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK.
What applications can BMPR1A Protein be used in?
BMPR1A Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMPR1A Protein?
The endotoxin level is minimal, BMPR1A Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PhosphotransacetylaseDescription:
Phosphotransacetylase Bacillus S. Recombinant
Phosphate Acetyltransferase, EC 2.3.1.8, Phosphotransacetylase, phosphoacylase.
Product # :
ENZ-1205Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Phosphotransacetylase Bacillus Stearothermophilus Recombinant produced in E.Coli is a single, non glycosylated polypeptide chain containing 325 amino acids and having a total molecular mass of 34.7kDa.
Phosphotransacetylase Recombinant is purified by proprietary chromatographic techniques.Source
E.Coli
Formulation
The protein was lyophilized with 0.15M NaCl and 20mM Tris pH-8.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Phosphotransacetylase activity is assessed by using the DTNB spectrophotometric method which was found to be greater than 3,000 Units/mg.More Info
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Introduction
Phosphotransacetylase (PTA) is a metabolic enzyme (EC 2.3.1.8) that catalyzes the reversible conversion: acetyl-CoA + Pi ⇄ acetyl-phosphate + CoA. The reversible reaction of acetyl-CoA to acetate node and back, is useful in R&D and biotech assays such as Metabolic engineering, Synthetic biology, Production of biopolymers, Enzymatic synthesis of acetyl-phosphate, bacterial signaling
and Fermentation. Phosphotransacetylase controls acetate formation and manipulates acetyl-CoA flux thus is widely used in protein expression, metabolic engineering, and synthetic pathways. -
Synonyms
Xylosyltransferase 2, Peptide O-xylosyltransferase 1, Xylosyltransferase II, XT-II, XylT-II, XYLT2, XT2.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Phosphate Acetyltransferase although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Phosphate Acetyltransferase should be stored at 4C between 2-7 days and for future use below -18C. 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 Phosphate Acetyltransferase in
sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be
further diluted to other aqueous solutions. -
Amino Acid Sequence
TTDLFTALKA KVTGTARKIV FPEGTDDRIL TAASRLATEQ VLQPIVLGDE QAIRVKAAAL GLPLEGVEIV NPRRYGGFDE LVSAFVERRK GKVTEETARE LLFDENYFGT MLVYMGAADG LVSGAAHSTA DTVRPALQII KTKPGVGKTS GVFIMVRGDE KYVFADCAIN IAPNSQDLAE IAVESARTAK MFGLKPRVAL LSFSTKGSAS SPETEKVVEA VRLAKEMAPD LILDGEFQFD AAFVPEVAKK KAPDSVIQGD ANVFIFPSLE AGNIGYKIAQ RLGGFEAVGP ILQGLNKPVN DLSRGCSAED AYKLALITAA QSLGE
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Unit Definition
1 unit will convert 1umole of Coenzyme A to acetyl coenzyme A /min/pH-7.5/30˚C using acetyl phosphate as substrate
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 :
PTGES3 HumanDescription:
Prostaglandin E Synthase 3 Human Recombinant
TEBP, CPGES, SID3177, 5730442A20Rik, p23, HSP90 co-chaperone, Prostaglandin E synthase 3, Cytosolic prostaglandin E2 synthase, Telomerase-binding protein p23, Progesterone receptor complex p23, PTGES3.
Product # :
ENZ-458Price :
Quantity :
Shipping Method :
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Description
Recombinant Human PTGES3 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 160 amino acids (1-160 a.a.) and having a molecular mass of 18.6 kDa.PTGES3 is purified by convential chromatogrpahy techniques.
Source
Escherichia Coli.
Formulation
The PTGES3 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT & 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PTGES3 takes part as a cochaperone and is involved in signal transduction.
PTGES3 is a molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexess. PTGES3 is necessary for appropriate functioning of the glucocorticoid and other steroid receptors.
PTGES3 localizes to genomic response elements in a hormone-dependent method and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes. -
Synonyms
TEBP, CPGES, SID3177, 5730442A20Rik, p23, HSP90 co-chaperone, Prostaglandin E synthase 3, Cytosolic prostaglandin E2 synthase, Telomerase-binding protein p23, Progesterone receptor complex p23, PTGES3.
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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
MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS VDFNNWKDWE DDSDEDMSNF DRFSEMMNNM GGDEDVDLPE VDGADDDSQD SDDEKMPDLE.
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 :
A2LD1 HumanDescription:
AIG2-Like Domain 1 Human Recombinant
Gamma-glutamylaminecyclotransferase, GGACT, AIG2-like domain-containing protein 1, A2LD1.
Product # :
PRO-172Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
A2LD1 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 173 amino acids (1-153 a.a.) and having a molecular mass of 19.4kDa. The A2LD1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The A2LD1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Gamma-glutamylaminecyclotransferase (A2LD1) is an enzyme which converts gamma-glutamylamines to free amines and 5-oxoproline. A2LD1 demonstrates high activity toward gamma-glutamyl-epsilon-lysine, derived from the breakdown of fibrin and other proteins cross-linked by transglutaminases. A2LD1 assists in the proteolytic degradation of crosslinked fibrin by breaking down isodipeptide L-gamma-glutamyl-L-epsilon-lysine, which is a byproduct of fibrin degradation. The reaction catalyzed by the A2LD1 produces 5-oxo-L-proline and a free alkylamine.
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Synonyms
Gamma-glutamylaminecyclotransferase, GGACT, AIG2-like domain-containing protein 1, A2LD1.
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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 MALVFVYGTL KRGQPNHRVL RDGAHGSAAF RARGRTLEPY PLVIAGEHNI PWLLHLPGSG RLVEGEVYAV DERMLRFLDD FESCPALYQR TVLRVQLLED RAPGAEEPPA PTAVQCFVYS RATFPPEWAQ LPHHDSYDSE GPHGLRYNPR ENR.
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 :
HMOX2 HumanDescription:
Heme Oxygenase-2 Human Recombinant
EC 1.14.99.3, HO2, Heme oxygenase 2, HO-2, HMOX2.
Product # :
ENZ-478Price :
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Shipping Method :
Shipped with Ice Packs
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Description
HMOX2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 264 amino acids (1-264 a.a.) and having a molecular mass of 30.5 kDa. HMOX2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HMOX2 solution containing 20mM Tris pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
HMOX2 cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently transferred to bilirubin by biliverdin reductase. Under physiological conditions, the activity of HMOX2 is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. HMOX2 participates in the production of carbon monoxide in the brain where it operates as a neurotransmitter. HMOX2 is an essential enzyme in heme catabolism and is involved in cellular response to oxidative stress.
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Synonyms
EC 1.14.99.3, HO2, Heme oxygenase 2, HO-2, HMOX2.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
HMOX2 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
SAEVETSEG VDESEKKNSG ALEKENQMRM ADLSELLKEG TKEAHDRAEN TQFVKDFLKG NIKKELFKLA TTALYFTYSA LEEEMERNKD HPAFAPLYFP MELHRKEALT KDMEYFFGEN WEEQVQCPKA AQKYVERIHY IGQNEPELLV AHAYTRYMGD LSGGQVLKKV AQRALKLPST GEGTQFYLFE NVDNAQQFKQ LYRARMNALD LNMKTKERIV EEANKAFEYN MQIFNELDQA GSTLARETLE DGFPVHDGKG DMRK.
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 :
ACADL HumanDescription:
Acyl-CoA Dehydrogenase, Long Chain, Human Recombinant
Acyl-CoA dehydrogenase long chain, Acyl-Coenzyme A dehydrogenase long chain, LCAD, ong-chain specific acyl-CoA dehydrogenase mitochondrial, ACAD4, EC 1.3.99.13.
Product # :
ENZ-190Price :
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Shipped with Ice Packs
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Description
ACADL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 421 amino acids (31-430) and having a molecular mass of 46.7 kDa.ACADL is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ACADL solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
ACADL is a homotetramer belonging to the acyl-CoA dehydrogenase family. ACADL takes part in the catabolism of fatty acids and amino acids and is a key source of energy for the heart and skeletal muscle. Mutation in the ACADL gene results in non-ketotic hypoglycemia and hypotonia (muscle weakness).
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Synonyms
Acyl-CoA dehydrogenase long chain, Acyl-Coenzyme A dehydrogenase long chain, LCAD, ong-chain specific acyl-CoA dehydrogenase mitochondrial, ACAD4, EC 1.3.99.13.
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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 MGGEERLETP SAKKLTDIGI RRIFSPEHDI FRKSVRKFFQ EEVIPHHSEW EKAGEVSREV WEKAGKQGLL GVNIAEHLGG IGGDLYSAAI VWEEQAYSNC SGPGFSIHSG IVMSYITNHG SEEQIKHFIP QMTAGKCIGA IAMTEPGAGS DLQGIKTNAK KDGSDWILNG SKVFISNGSL SDVVIVVAVT NHEAPSPAHG ISLFLVENGM KGFIKGRKLH KMGLKAQDTA ELFFEDIRLP ASALLGEENK GFYYIMKELP QERLLIADVA ISASEFMFEE TRNYVKQRKA FGKTVAHLQT VQHKLAELKT HICVTRAFVD NCLQLHEAKR LDSATACMAK YWASELQNSV AYDCVQLHGG WGYMWEYPIA KAYVDARVQP IYGGTNEIMK ELIAREIVFD K
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 :
CTSF HumanDescription:
Cathepsin-F Human Recombinant
800x600 CATSF, CLN13, Cathepsin F, EC=3.4.22.41. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}
Product # :
ENZ-738Price :
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Description
800x600 CTSF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (271-484) and having a molecular mass of 26kDa.CTSF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CTSF solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cathepsin F ( CTSF) is a member of the peptidase C1 family. Cathepsins are papain familycysteine proteinases which are a main component of the lysosomal proteolytic system. The CTSF gene isubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. CTSF plays a role in normal protein catabolism. CTSF involved in some degradative processes occurring in tumor progression since it is highly expressed in some cancer cell lines.
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Synonyms
CATSF, CLN13, Cathepsin F, EC=3.4.22.41.
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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 MGSAPPEWDW RSKGAVTKVK DQGMCGSCWA FSVTGNVEGQ WFLNQGTLLS LSEQELLDCD KMDKACMGGL PSNAYSAIKN LGGLETEDDY SYQGHMQSCN FSAEKAKVYI NDSVELSQNE QKLAAWLAKR GPISVAINAF GMQFYRHGIS RPLRPLCSPW LIDHAVLLVG YGNRSDVPFW AIKNSWGTDW GEKGYYYLHR GSGACGVNTM ASSAVVD.
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.