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1000 results found for “dehydrogenase”
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Name :
QTRT1 HumanDescription:
Queuine TRNA-Ribosyltransferase 1 Human Recombinant
Queuine TRNA-Ribosyltransferase 1, TRNA-Guanine Transglycosylase, TGT, Guanine Insertion Enzyme, EC 2.4.2.29, TGUT, Queuine TRNA-Ribosyltransferase, TGT, Catalytic Subunit, TGT, 43-KD Subunit, FP3235, Queuine tRNA-ribosyltransferase.
Product # :
ENZ-877Price :
Quantity :
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Shipped with Ice Packs
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Description
QTRT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 428 amino acids (1-403 a.a) and having a molecular mass of 46.7kDa. QTRT1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
QTRT1 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Queuine TRNA-Ribosyltransferase 1 also known as QTRT1 is a member of the queuine tRNA-ribosyltransferase family. QTRT1 interacts with QTRTD1 to form an active queuine tRNA-ribosyltransferase. Furthermore, QTRT1 exchanges queuine for the guanine at the wobble position of tRNAs with GUN anticodons (tRNA-Asp, -Asn, -His and -Tyr), in this manner forming the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
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Synonyms
Queuine TRNA-Ribosyltransferase 1, TRNA-Guanine Transglycosylase, TGT, Guanine Insertion Enzyme, EC 2.4.2.29, TGUT, Queuine TRNA-Ribosyltransferase, TGT, Catalytic Subunit, TGT, 43-KD Subunit, FP3235, Queuine tRNA-ribosyltransferase.
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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 MGSEFMAGAA TQASLESAPR IMRLVAECSR SRARAGELWL PHGTVATPVF MPVGTQATMK GITTEQLDAL GCRICLGNTY HLGLRPGPEL IQKANGLHGF MNWPHNLLTD SGGFQMVSLV SLSEVTEEGV RFRSPYDGNE TLLSPEKSVQ IQNALGSDII MQLDDVVSST VTGPRVEEAM YRSIRWLDRC IAAHQRPDKQ NLFAIIQGGL DADLRATCLE EMTKRDVPGF AIGGLSGGES KSQFWRMVAL STSRLPKDKP RYLMGVGYAT DLVVCVALGC DMFDCVFPTR TARFGSALVP TGNLQLRKKV FEKDFGPIDP ECTCPTCQKH SRAFLHALLH SDNTAALHHL TVHNIAYQLQ LMSAVRTSIV EKRFPDFVRD FMGAMYGDPT LCPTWATDAL ASVGITLG.
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 :
GSTM1 Human, Sf9Description:
Glutathione S-Transferase M1 Human Recombinant, Sf9
GST1, GTH4, GTM1, GSTM1-1, MGC26563, GSTM1a-1a, GSTM1b-1b, GSTM1, Glutathione S-transferase Mu 1, GST class-mu 1, Glutathione S-transferase GT8.7, pmGT10, GST 1-1.
Product # :
ENZ-1092Price :
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Description
GSTM1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain (1-218a.a.) fused to a 9 aa His Tag at C-terminus containing 227 amino acids and having a molecular mass of 26.8kDa. GSTM1 shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
GSTM1 protein solution (0.5mg/ml) contains 40% glycerol, 0.2M NaCl, 2mM DTT and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cytosolic and membrane-bound types of GST are encoded by 2 different supergene families. There are 8 classes of the soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are arranged in a gene cluster on chromosome 1p13.3 and aare highly polymorphic. These genetic differences can change an individual's resistance to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Null mutations of this class mu gene have been linked with the rise in a number of cancers.
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Synonyms
GST1, GTH4, GTM1, GSTM1-1, MGC26563, GSTM1a-1a, GSTM1b-1b, GSTM1, Glutathione S-transferase Mu 1, GST class-mu 1, Glutathione S-transferase GT8.7, pmGT10, GST 1-1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPMPMILGY WDIRGLAHAI RLLLEYTDSS YEEKKYTMGD APDYDRSQWL NEKFKLGLDF PNLPYLIDGA HKITQSNAIL CYIARKHNLC GETEEEKIRV DILENQTMDN HMQLGMICYN PEFEKLKPKY LEELPEKLKL YSEFLGKRPW FAGNKITFVD FLVYDVLDLH RIFEPKCLDA FPNLKDFISR FEGLEKISAY MKSSRFLPRP VFSKMAVWGN KHHHHHH.
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 :
pGH 22kDa HumanDescription:
Growth Hormone Placental 22kDa Human Recombinant
GHL, GHV, GH-V, hGH-V, PGH.
Product # :
CYT-235Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Placental HGH 22kDa Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 192 amino acids and having a molecular mass of 22367 Dalton. Predicted pI=7.80. Placental Growth Hormone has dimished lactogenic (prolactin receptor mediated) activity characteristic to pituitary GHs. GH Placental Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3 previously adjusted pH 8-9.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.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
GHL, GHV, GH-V, hGH-V, PGH.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GH placental although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization HGH placental can be stored at 4°C for up to 4 weeks. For long term storage and more diluted solutions 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 Placental HGH in 0.4% NaHCO3or water adjusted to pH 9, not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Phe-Pro-Thr-Ile.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.18 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 GH-22K-placental 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.
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Name :
ACHE HumanDescription:
Acetylcholinesterase Human Recombinant
AChE, ACEE, ACES_HUMAN, Acetylcholinesterase, ACHE, ARACHE, N-ACHE, VT, Acetylcholinesterase isoform E4-E6
Product # :
ENZ-1174Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ACHE Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (32-614 a.a) containing a total of 592 amino acids, having a molecular mass of 65.6 kDa. ACHE is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The ACHE solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 6,000 nmol/min/ug. Defined by the amount of enzyme that cleaves 1 nmole of acetylthiocholine per minute at pH 7.5 at 25˚C.
More Info
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Introduction
Acetylcholinesterase (ACHE) belongs to the type-B carboxylesterase/lipase family. ACHE catalyzes the breakdown of acetylcholine and other choline esters that play a role as neurotransmitters. During neurotransmission, ACH is released from the presynaptic neuron into the synaptic cleft and binds ACH receptors on the post-synaptic membrane, transmitting the signal from the nerve. ACHE is located on the post-synaptic membrane, terminates the signal transmission by hydrolyzing ACH.
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Synonyms
AChE, ACEE, ACES_HUMAN, Acetylcholinesterase, ACHE, ARACHE, N-ACHE, VT, Acetylcholinesterase isoform E4-E6
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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
DGSEGREDAE LLVTVRGGRL RGIRLKTPGG PVSAFLGIPF AEPPMGPRRF LPPEPKQPWS GVVDATTFQS VCYQYVDTLY PGFEGTEMWN PNRELSEDCL YLNVWTPYPR PTSPTPVLVW IYGGGFYSGA SSLDVYDGRF LVQAERTVLV SMNYRVGAFG FLALPGSREA PGNVGLLDQR LALQWVQENV AAFGGDPTSV TLFGESAGAA SVGMHLLSPP SRGLFHRAVL QSGAPNGPWA TVGMGEARRR ATQLAHLVGC PPGGTGGNDT ELVACLRTRP AQVLVNHEWH VLPQESVFRF SFVPVVDGDF LSDTPEALIN AGDFHGLQVL VGVVKDEGSY FLVYGAPGFS KDNESLISRA EFLAGVRVGV PQVSDLAAEA VVLHYTDWLH PEDPARLREA LSDVVGDHNV VCPVAQLAGR LAAQGARVYA YVFEHRASTL SWPLWMGVPH GYEIEFIFGI PLDPSRNYTA EEKIFAQRLM RYWANFARTG DPNEPRDPKA PQWPPYTAGA QQYVSLDLRP LEVRRGLRAQ ACAFWNRFLP KLLSATDTLD EAERQWKAEF HRWSSYMVHW KNQFDHYSKQ DRCSDLHHHH HH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ACE2 RatDescription:
Angiotensin Converting Enzyme 2 Rat Recombinant
ACE2, 2010305L05Rik, Angiotensin I Converting Enzyme, Angiotensin I Converting, Enzyme (Peptidyl-Dipeptidase A), Angiotensin-Converting Enzyme Homolog, Angiotensin-Converting Enzyme, ACE-Related Carboxypeptidase, Metalloprotease MPROT15, Peptidyl-Dipeptidase A, ACEH, EC 3.4.17.23, EC 3.4.17.
Product # :
ENZ-1124Price :
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Shipped with Ice Packs
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Description
ACE2 Rat produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 731 amino acids (18-740 aa) and having a molecular mass of 84.7kDa. ACE2 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The ACE2 solution contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 150 pmol/min/ug, and is defined as the amount of enzyme that hydrolysis 1.0 pmole of McaYVADAPK(Dnp)-OH per minute at pH 7.5, at 25C.
More Info
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Introduction
Angiotensin converting enzyme 2 or ACE-2 is an enzyme that is located in the cell membranes in different organs such as kidney, intestines, lungs, heart & arteries. ACE2 acts as an entry receptor of SARS coronaviruses & SARS-CoV-2.The coronavirus spike (S) glycoprotein is a class I viral fusion antigen bound to the external envelope of the virion that has a role in a crucial part in viral infection by identifying host cell receptors and starting fusion of the viral and cellular membranes. Couple of main domains in coronavirus S1 have been identified, the N-terminal domain and C-terminal domain. One or the other and/or both S1 domains acts as a receptor-binding domain. SARS-CoV + MERS-CoV equally use C-domain to attach their receptors.ACE2 is a type I transmembrane antigen with an extracellular N-terminal domain having the catalytic site and an intracellular C-terminal tail. ACE2 has a signal peptide, a transmembrane domain & a single metalloproteinase active site holds an HEXXH zinc-binding domain. ACE-2 takes part as a mono-carboxypeptidase which degrades Ang I to produce the nonapeptide Ang 1–9 and Ang II to create the heptapeptide Ang 1–7.
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Synonyms
ACE2, 2010305L05Rik, Angiotensin I Converting Enzyme, Angiotensin I Converting, Enzyme (Peptidyl-Dipeptidase A), Angiotensin-Converting Enzyme Homolog, Angiotensin-Converting Enzyme, ACE-Related Carboxypeptidase, Metalloprotease MPROT15, Peptidyl-Dipeptidase A, ACEH, EC 3.4.17.23, EC 3.4.17.
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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
QSLIEEKAES FLNKFNQEAE DLSYQSSLAS WNYNTNITEE NAQKMNEAAA KWSAFYEEQS KIAQNFSLQE IQNATIKRQL KALQQSGSSA LSPDKNKQLN TILNTMSTIY STGKVCNSMN PQECFLLEPG LDEIMATSTD YNRRLWAWEG WRAEVGKQLR PLYEEYVVLK NEMARANNYE DYGDYWRGDY EAEGVEGYNY NRNQLIEDVE NTFKEIKPLY EQLHAYVRTK LMEVYPSYIS PTGCLPAHLL GDMWGRFWTN LYPLTTPFLQ KPNIDVTDAM VNQSWDAERI FKEAEKFFVS VGLPQMTPGF WTNSMLTEPG DDRKVVCHPT AWDLGHGDFR IKMCTKVTMD NFLTAHHEMG HIQYDMAYAK QPFLLRNGAN EGFHEAVGEI MSLSAATPKH LKSIGLLPSN FQEDNETEIN FLLKQALTIV GTLPFTYMLE KWRWMVFQDK IPREQWTKKW WEMKREIVGV VEPLPHDETY CDPASLFHVS NDYSFIRYYT RTIYQFQFQE ALCQAAKHDG PLHKCDISNS TEAGQKLLNM LSLGNSGPWT LALENVVGSR NMDVKPLLNY FQPLFVWLKE QNRNSTVGWS TDWSPYADQS IKVRISLKSA LGKNAYEWTD NEMYLFRSSV AYAMREYFSR EKNQTVPFGE ADVWVSDLKP RVSFNFFVTS PKNVSDIIPR SEVEEAIRMS RGRINDIFGL NDNSLEFLGI YPTLKPPYEP PVTLEHHHHH 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 :
OAS1 HumanDescription:
2’-5’ Oligoadenylate Synthetase 1 Human Recombinant
2'-5'-oligoadenylate synthetase 1, (2-5')oligo(A) synthetase 1, 2-5A synthetase 1, p46/p42 OAS, E18/E16, OAS1, OIAS, IFI-4, OIASI.
Product # :
ENZ-445Price :
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Shipped with Ice Packs
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Description
OAS1 Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 384 amino acids (1-364 a.a.) and having a molecular mass of 43.9kDa.The OAS1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OAS1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
OAS1 enzyme is a member of the 2’,5’-oligoadenylate synthetase family. OAS1 is induced by interferons and uses adenosine triphosphate in 2’-specific nucleotidyl transfer reactions to synthesize 2’,5’-oligoadenylates(2-5As). These molecules in turn activate latent RNase L resulting in viral RNA degradation and the inhibition of viral replication.
OAS1 may have a role in mediating resistance to virus infection, control of cell growth, differentiation, and apoptosis. OAS1 binds double-stranded RNA and polymerizes ATP into PPP (A2'P5'A)N oligomers, which activate the latent RNase L that, once activated, cleaves single-stranded RNAs.
OAS1 gene mutations are been linked to host susceptibility to viral infection.
OSA1 gene polymorphisms are linked to the outcome of hepatitis C virus infection. Furthermore, OAS1 gene polymorphisms are linked to the susceptibility to severe acute respiratory syndrome. -
Synonyms
2'-5'-oligoadenylate synthetase 1, (2-5')oligo(A) synthetase 1, 2-5A synthetase 1, p46/p42 OAS, E18/E16, OAS1, OIAS, IFI-4, OIASI.
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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 MMDLRNTPAK SLDKFIEDYL LPDTCFRMQI NHAIDIICGF LKERCFRGSS YPVCVSKVVK GGSSGKGTTL RGRSDADLVV FLSPLTTFQD QLNRRGEFIQ EIRRQLEACQ RERAFSVKFE VQAPRWGNPR ALSFVLSSLQ LGEGVEFDVL PAFDALGQLT GSYKPNPQIY VKLIEECTDL QKEGEFSTCF TELQRDFLKQ RPTKLKSLIR LVKHWYQNCK KKLGKLPPQY ALELLTVYAW ERGSMKTHFN TAQGFRTVLE LVINYQQLCI YWTKYYDFKN PIIEKYLRRQ LTKPRPVILD PADPTGNLGG GDPKGWRQLA QEAEAWLNYP CFKNWDGSPV SSWILLVRPP ASSLPFIPAP LHEA.
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 :
KMT5A HumanDescription:
Lysine Methyltransferase 5A Human Recombinant
KMT5A, PR-Set7, SET07, SET8, SETD8, H4-K20-HMTase KMT5A.
Product # :
ENZ-1080Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KMT5A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 165 amino acids (195-352 a.a.) and having a molecular mass of 18.9kDa (Migrates at 18-28 kDa on SDS-PAGE under reducing conditions).KMT5A is expressed with a 7 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
KMT5A protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 5mM DTT, 0.2M NaCl, 1mM EDTA and 50% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Lysine Methyltransferase 5A (KMT5A) is an enzyme which catalyzes both histones and non-histone proteins. KMT5A contributes to the maintenance of proper higher-order structure of DNA during mitosis. KMT5A takes part in cell-cycle-dependent transcriptional silencing and mitotic regulation in metazoans. KMT5A plays a role as a barrier to prevent cellular senescence through chromatinmediated regulation of senescence-associated metabolic remodeling. KMT5A mediates monomethylation of p53/TP53 at 'Lys-382', which leads to repress p53/TP53-target genes. The loss of KMT5A simultaneously stimulate nucleolar function and retinoblastoma protein-mediated mitochondrial metabolism.
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Synonyms
KMT5A, PR-Set7, SET07, SET8, SETD8, H4-K20-HMTase KMT5A.
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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
MKAELQSEER KRIDELIESG KEEGMKIDLI DGKGRGVIAT KQFSRGDFVV EYHGDLIEIT DAKKREALYA QDPSTGCYMY YFQYLSKTYC VDATRETNRL GRLINHSKCG NCQTKLHDID GVPHLILIAS RDIAAGEELL YDYGDRSKAS IEAHPWLKHH HHHHH.
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 :
PRDX2 RatDescription:
Peroxiredoxin-2 Rat Recombinant
Peroxiredoxin-2, Prdx2, Prdx, Thiol-specific antioxidant protein, TSA, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1.
Product # :
ENZ-910Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PRDX2 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (1-198 a.a) and having a molecular mass of 24.3kDa. PRDX2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PRDX2 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
PRDX2 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX2 takes part as an antioxidant protective role in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX2 has proliferative effect in cancer development or progression.
If PRDX2 protection is insufficient against peroxidases, the DNA damage results in neurological disease such as Alzheimer's or DNA damage leading to cancer. -
Synonyms
Peroxiredoxin-2, Prdx2, Prdx, Thiol-specific antioxidant protein, TSA, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMASGNA HIGKPAPDFT GTAVVDGAFK EIKLSDYRGK YVVLFFYPLD FTFVCPTEII AFSDHAEDFR KLGCEVLGVS VDSQFTHLAW INTPRKEGGL GPLNIPLLAD VTKSLSQNYG VLKNDEGIAY RGLFIIDAKG VLRQITVNDL PVGRSVDEAL RLVQAFQYTD EHGEVCPAGW KPGSDTIKPN VDDSKEYFSK HN.
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 :
MMP10 HumanDescription:
Matrix Metallopeptidase 10 Human Recombinant
SL-2, STMY2, Stromelysin-2, Matrix metalloproteinase-10, MMP-10, Transin-2, MMP10.
Product # :
ENZ-764Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MMP10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (99-476a.a) and having a molecular mass of 45.4kDa. MMP10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MMP10 solution (0.5mg/ml) contains 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
MMP10 (Matrix Metallopeptidase 10) which is a part of the matrix metalloproteinase (MMP) is activating procollagenase. MMP10 is part of a cluster of MMP genes which localize to chromosome 11q22.3. MMP10 takes part in the breakdown of extracellular matrix in normal physiological processes, like embryonic development, reproduction, and tissue remodeling, as also in disease processes, such as arthritis and metastasis. The majority MMP's are secreted as inactive proproteins that are activated when cleaved by extracellular proteinases. MMP10 encodes an enzyme which degrades proteoglycans and fibronectin.
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Synonyms
SL-2, STMY2, Stromelysin-2, Matrix metalloproteinase-10, MMP-10, Transin-2, MMP10.
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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 MGSFSSFPGM PKWRKTHLTY RIVNYTPDLP RDAVDSAIEK ALKVWEEVTP LTFSRLYEGE ADIMISFAVK EHGDFYSFDG PGHSLAHAYP PGPGLYGDIH FDDDEKWTED ASGTNLFLVA AHELGHSLGL FHSANTEALM YPLYNSFTEL AQFRLSQDDV NGIQSLYGPP PASTEEPLVP TKSVPSGSEM PAKCDPALSF DAISTLRGEY LFFKDRYFWR RSHWNPEPEF HLISAFWPSL PSYLDAAYEV NSRDTVFIFK GNEFWAIRGN EVQAGYPRGI HTLGFPPTIR KIDAAVSDKE KKKTYFFAAD KYWRFDENSQ SMEQGFPRLI ADDFPGVEPK VDAVLQAFGF FYFFSGSSQF EFDPNARMVT HILKSNSWLH C.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NDK E.ColiDescription:
Nucleoside Diphosphate Kinase E.Coli Recombinant
Nucleoside diphosphate kinase, NDK, NDP kinase, Nucleoside-2-P kinase, b2518, JW2502.
Product # :
PKA-034Price :
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Description
NDK E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (1-143 a.a.) and having a molecular mass of 18kDa.NDK is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
NDK protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Nucleoside diphosphate kinase (Ndk) is an enzyme which catalyzes the exchange of phosphate groups between different nucleoside diphosphates. Ndk’s activity sustains equilibrium between the concentrations of various nucleoside triphosphates for example, when GTP is produced in the citric acid (Krebs) cycle is converted to ATP. Ndk has a key role in the synthesis of nucleoside triphosphates other than ATP.
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Synonyms
Nucleoside diphosphate kinase, NDK, NDP kinase, Nucleoside-2-P kinase, b2518, JW2502.
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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 MGSHMAIERT FSIIKPNAVA KNVIGNIFAR FEAAGFKIVG TKMLHLTVEQ ARGFYAEHDG KPFFDGLVEF MTSGPIVVSV LEGENAVQRH RDLLGATNPA NALAGTLRAD YADSLTENGT HGSDSVESAA REIAYFFGEG EVCPRTR.
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 :
SULT1B1 HumanDescription:
Sulfotransferase Family, Cytosolic, 1B, Member 1 Human Recombinant
Sulfotransferase family cytosolic 1B member 1, Thyroid hormone sulfotransferase, Sulfotransferase 1B1, Sulfotransferase 1B2, ST1B1, EC 2.8.2.-, SULT1B2.
Product # :
ENZ-610Price :
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Description
SULT1B1 Human Recombinant produced in E. coli is a single polypeptide chain containing 320 amino acids (1-296) and having a molecular mass of 37.4kDa.SULT1B1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SULT1B1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
SULT1B1 enzyme in humans is encoded by the SULT1B1 gene. SULT1B1 holds a binding site for 3-prime-phosphoadenosine 5-prime-phosphosulfate, a sulfate donor, in addition to a cysteine residue conserved in the ST1 gene family of sulfotransferases. Sulfotransferases like SULT1B1 catalyze the biotransformation of a great amount of endogenous amalgams such as bile acids, neurotransmitters, steroids, and thyroid hormones, in addition to drugs and xenobiotics.
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Synonyms
Sulfotransferase family cytosolic 1B member 1, Thyroid hormone sulfotransferase, Sulfotransferase 1B1, Sulfotransferase 1B2, ST1B1, EC 2.8.2.-, SULT1B2.
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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 MGSHMLSPKD ILRKDLKLVH GYPMTCAFAS NWEKIEQFHS RPDDIVIATY PKSGTTWVSE IIDMILNDGD IEKCKRGFIT EKVPMLEMTL PGLRTSGIEQ LEKNPSPRIV KTHLPTDLLP KSFWENNCKM IYLARNAKDV SVSYYHFDLM NNLQPFPGTW EEYLEKFLTG KVAYGSWFTH VKNWWKKKEE HPILFLYYED MKENPKEEIK KIIRFLEKNL NDEILDRIIH HTSFEVMKDN PLVNYTHLPT TVMDHSKSPF MRKGTAGDWK NYFTVAQNEK FDAIYETEMS KTALQFRTEI
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 :
SULT2B1 HumanDescription:
Sulfotransferase Family, Cytosolic, 2B, Member 1 Human Recombinant
SULT2B1, HSST2, EC 2.8.2.2, Sulfotransferase 2B1, Hydroxysteroid sulfotransferase 2, ST2B1, Sulfotransferase family cytosolic 2B member 1.
Product # :
ENZ-512Price :
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Description
SULT2B1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 365 amino acids (1-365 a.a.) and having a molecular mass of 41.3 kDa. SULT2B1 protein is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
SULT2B1 Human solution containing 20mM Tris-HCl pH-7.5, & 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
SULT2B1 catalyzes the sulfate conjugation of numerous hormones, neurotransmitters, drugs and xenobiotic compounds. Sulfonation enhances the water solubility of molecules, and therefore their renal excretion, however it can also result in bioactivation to form active metabolites. SULT2B1b is localized in the cytosol and nuclei of human cells. SULT2B1b is selective for the sulfation of 3beta-hydroxysteroids such as dehydroepiandrosterone and pregnenolone, and participates in cholesterol sulfation in human skin.
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Synonyms
SULT2B1, HSST2, EC 2.8.2.2, Sulfotransferase 2B1, Hydroxysteroid sulfotransferase 2, ST2B1, Sulfotransferase family cytosolic 2B member 1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MDGPAEPQIP GLWDTYEDDI SEISQKLPGE YFRYKGVPFP VGLYSLESIS LAENTQDVRD DDIFIITYPK SGTTWMIEII CLILKEGDPS WIRSVPIWER APWCETIVGA FSLPDQYSPR LMSSHLPIQI FTKAFFSSKA KVIYMGRNPR DVVVSLYHYS KIAGQLKDPG TPDQFLRDFL KGEVQFGSWF DHIKGWLRMK GKDNFLFITY EELQQDLQGS VERICGFLGR PLGKEALGSV VAHSTFSAMK ANTMSNYTLL PPSLLDHRRG AFLRKGVCGD WKNHFTVAQS EAFDRAYRKQ MRGMPTFPWD EDPEEDGSPD PEPSPEPEPK PSLEPNTSLE REPRPNSSPS PSPGQASETP HPRPS.
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 :
KAT2A HumanDescription:
K (lysine) Acetyltransferase 2A Human Recombinant
Histone acetyltransferase KAT2A, General control of amino acid synthesis protein 5-like 2, Histone acetyltransferase GCN5, HsGCN5, Lysine acetyltransferase 2A, STAF97, KAT2A, GCN5, GCN5L2, HGCN5, PCAF-b.
Product # :
ENZ-166Price :
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Description
KAT2A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids (411-837 a.a) and having a molecular mass of 51.1kDa.KAT2A is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KAT2A protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 40% glycerol, 200mM NaCl and 1mM EDTA.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
General control of amino acid synthesis protein 5 like 2 (KAT2A) is a member of the GCN5 family. KAT2A functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Acetylation of histones gives a specific tag for epigenetic transcription activation. KAT2A interacts with Ku70, TAF9, transcription initiation protein SPT3 homolog, TADA2L, Ku80 and DDB1.
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Synonyms
Histone acetyltransferase KAT2A, General control of amino acid synthesis protein 5-like 2, Histone acetyltransferase GCN5, HsGCN5, Lysine acetyltransferase 2A, STAF97, KAT2A, GCN5, GCN5L2, HGCN5, PCAF-b.
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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 MGGGSNSSLS LDSAGAEPMP GEKRTLPENL TLEDAKRLRV MGDIPMELVN EVMLTITDPA AMLGPETSLL SANAARDETA RLEERRGIIE FHVIGNSLTP KANRRVLLWL VGLQNVFSHQ LPRMPKEYIA RLVFDPKHKT LALIKDGRVI GGICFRMFPT QGFTEIVFCA VTSNEQVKGY GTHLMNHLKE YHIKHNILYF LTYADEYAIG YFKKQGFSKD IKVPKSRYLG YIKDYEGATL MECELNPRIP YTELSHIIKK QKEIIKKLIE RKQAQIRKVY PGLSCFKEGV RQIPVESVPG IRETGWKPLG KEKGKELKDP DQLYTTLKNL LAQIKSHPSA WPFMEPVKKS EAPDYYEVIR FPIDLKTMTE RLRSRYYVTR KLFVADLQRV IANCREYNPP DSEYCRCASA LEKFFYFKLK EGGLIDK.
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 :
GSTA1 MouseDescription:
Glutathione S-Transferase Alpha 1 Mouse Recombinant
Glutathione S-transferase A1, GST class-alpha member 1, Glutathione S-transferase Ya , Glutathione S-transferase Ya1.
Product # :
ENZ-873Price :
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Description
GSTA1 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 28kDa.GSTA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GSTA1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The specific activity is defined as the amount of enzyme that conjugate 1.0 pmole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C and is > 4,000 pmol/min/ug.
More Info
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Introduction
Membrane-bound & Cytosolic forms of GST are encoded by 2 separate supergene families. These enzymes function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. There are 8 different classes of soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The GSTA1 is found in a cluster mapped to chromosome 6, and is highly expressed in the liver. GSTA1 protects the cells from reactive oxygen species.
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Synonyms
Glutathione S-transferase A1, GST class-alpha member 1, Glutathione S-transferase Ya , Glutathione S-transferase Ya1.
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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 MGSMAGKPVL HYFNARGRME CIRWLLAAAG VEFEEKFIQS PEDLEKLKKD GNLMFDQVPM VEIDGMKLAQ TRAILNYIAT KYDLYGKDMK ERALIDMYSE GILDLTEMIG QLVLCPPDQR EAKTALAKDR TKNRYLPAFE KVLKSHGQDY LVGNRLTRVD IHLLEVLLYV EEFDASLLTP FPLLKAFKSR ISSLPNVKKF LQPGSQRKPP MDAKQIQEAR KAFKIQ.
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 :
DUSP21 HumanDescription:
Dual Specificity Phosphatase 21 Human Recombinant
Dual specificity phosphatase 21, Low molecular weight dual specificity phosphatase 21, LMW-DSP21, BJ-HCC-26 tumor antigen, EC 3.1.3.16, EC 3.1.3.48.
Product # :
ENZ-239Price :
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Description
DUSP21 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 214 amino acids (1-190) and having a molecular mass of 24.1kDa.DUSP21 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The DUSP21 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
DUSP21 is a member of the protein-tyrosine phosphatase family. DUSPs inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residuesb. DUSP21 is able to dephosphorylate single and diphosphorylated synthetic MAPK peptides, favoring the phosphotyrosine and diphosphorylated forms over phosphothreonine. DUSP21 is only expressed in testis where there are dephosphorylated phosphotyrosine residues in MAPK peptides.
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Synonyms
Dual specificity phosphatase 21, Low molecular weight dual specificity phosphatase 21, LMW-DSP21, BJ-HCC-26 tumor antigen, EC 3.1.3.16, EC 3.1.3.48.
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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 MGSHMTASAS SFSSSQGVQQ PSIYSFSQIT RSLFLSNGVA ANDKLLLSSN RITAIVNASV EVVNVFFEGI QYIKVPVTDA RDSRLYDFFD PIADLIHTID MRQGRTLLHC MAGVSRSASL CLAYLMKYHS MSLLDAHTWT KSRRPIIRPN NGFWEQLINY EFKLFNNNTV RMINSPVGNI PDIYEKDLRM MISM
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 :
NAA30 HumanDescription:
N Alpha-Acetyltransferase 30, NatC Catalytic Subunit Human Recombinant
N(Alpha)-Acetyltransferase 30, NatC Catalytic Subunit, C14orf35, NAT12, N-Acetyltransferase 12 (GCN5-Related, Putative), N-Acetyltransferase 12, NatC Catalytic Subunit, MAK3, N-Acetyltransferase MAK3 Homolog, Chromosome 14 Open Reading Frame 35, Mak3p, NAT12P, N-Alpha-Acetyltransferase 30, N-Alpha-Acetyltransferase 30, NatC Catalytic Subunit, Putative N-Acetyltransferase, EC 2.3.1.88.
Product # :
ENZ-720Price :
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Description
NAA30 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 385 amino acids (1-362 a.a) and having a molecular mass of 41.7kDa.NAA30 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NAA30 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
N-alpha-acetyltransferase 30 (NAA30) is catalytic subunit of the N-terminal acetyltransferase C (NatC) complex. NAA30 catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly. In addition, NAA30 is essential for the lysosomal localization and function of ARL8B. The disease Eastern equine encephalitis has been associated with NAA30.
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Synonyms
N(Alpha)-Acetyltransferase 30, NatC Catalytic Subunit, C14orf35, NAT12, N-Acetyltransferase 12 (GCN5-Related, Putative), N-Acetyltransferase 12, NatC Catalytic Subunit, MAK3, N-Acetyltransferase MAK3 Homolog, Chromosome 14 Open Reading Frame 35, Mak3p, NAT12P, N-Alpha-Acetyltransferase 30, N-Alpha-Acetyltransferase 30, NatC Catalytic Subunit, Putative N-Acetyltransferase, EC 2.3.1.88.
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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 MGSMAEVPPG PSSLLPPPAP PAPAAVEPRC PFPAGAALAC CSEDEEDDEE HEGGGSRSPA GGESATVAAK GHPCLRCPQP PQEQQQLNGL ISPELRHLRA AASLKSKVLS VAEVAATTAT PDGGPRATAT KGAGVHSGER PPHSLSSNAR TAVPSPVEAA AASDPAAARN GLAEGTEQEE EEEDEQVRLL SSSLTADCSL RSPSGREVEP GEDRTIRYVR YESELQMPDI MRLITKDLSE PYSIYTYRYF IHNWPQLCFL AMVGEECVGA IVCKLDMHKK MFRRGYIAML AVDSKYRRNG IGTNLVKKAI YAMVEGDCDE VVLETEITNK SALKLYENLG FVRDKRLFRY YLNGVDALRL KLWLR
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 :
NNMT MouseDescription:
Nicotinamide N-Methyltransferase Mouse Recombinant
Nicotinamide N-methyltransferase , Nnmt, icotinamide N-methyltransferase isoform1.
Product # :
ENZ-1037Price :
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Description
NNMT Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids (1-264a.a) and having a molecular mass of 32.1kDa.NNMT is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NNMT protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
NNMT is part of the family of transferases, especially those transferring one-carbon group methyltransferases. NNMT is mostly expressed in the liver, and a lower expression is seen in the kidney, lung, skeletal muscle, placenta and heart. NNMT catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is significant for biotransformation of many drugs and xenobiotic compounds. NNMT is accountable for the enzymatic activity which uses S-adenosyl methionine as the methyl donor. NNMT expression is related with tumor stage and DFS time in hepatocellular carcinoma cases. NNMT is a good candidate as a tumor marker of various kinds of cancers. NNMT serum levels have significance in the premature detection and in the management of patients with colorectal cancer.
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Synonyms
Nicotinamide N-methyltransferase , Nnmt, icotinamide N-methyltransferase isoform1.
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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 MGSHMESGFT SKDTYLSHFN PRDYLEKYYS FGSRHCAENE ILRHLLKNLF KIFCLGAVKG ELLIDIGSGP TIYQLLSACE SFTEIIVSDY TDQNLWELQK WLKKEPGAFD WSPVVTYVCD LEGNRMKGPE KEEKLRRAIK QVLKCDVTQS QPLGGVSLPP ADCLLSTLCL DAACPDLPAY RTALRNLGSL LKPGGFLVMV DALKSSYYMI GEQKFSSLPL GWETVRDAVE EAGYTIEQFE VISQNYSSTT SNNEGLFSLV GRKPGRSE.
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 :
CASP2 HumanDescription:
Caspase 2 Apoptosis-Related Cysteine Peptidase Human Recombinant
Caspase-2, CASP-2, CASP2, Caspase 2 Apoptosis-Related Cysteine Peptidase, Neural precursor cell expressed developmentally down-regulated protein 2, NEDD-2, Protease ICH-1, ICH1, NEDD2, Caspase-2 subunit p18, Caspase-2 subunit p13, Caspase-2 subunit p12, Caspase 2 isoform 1, PPP1R57.
Product # :
ENZ-801Price :
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Description
CASP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (348-452) and having a molecular mass of 14.1kDa.CASP2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CASP2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Caspase 2 Apoptosis-Related Cysteine Peptidase (CASP2) is a part of the cysteine-aspartic acid protease (caspase) family. CASP2 takes part in the activation cascade of caspases responsible for apoptosis execution. CASP2 is also responsible for inactivating proteins essential for cell survival. The proteolytic cleavage of CASP2 is induced by a variety of apoptotic stimuli.
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Synonyms
Caspase-2, CASP-2, CASP2, Caspase 2 Apoptosis-Related Cysteine Peptidase, Neural precursor cell expressed developmentally down-regulated protein 2, NEDD-2, Protease ICH-1, ICH1, NEDD2, Caspase-2 subunit p18, Caspase-2 subunit p13, Caspase-2 subunit p12, Caspase 2 isoform 1, PPP1R57.
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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 MAGKEKLPKM RLPTRSDMIC GYACLKGTAA MRNTKRGSWY IEALAQVFSE RACDMHVADM LVKVNALIKD REGYAPGTEF HRCKEMSEYC STLCRHLYLF PGHPPT.
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 :
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 :
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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.
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Name :
GH Rainbow TroutDescription:
Growth Hormone Rainbow Trout (Oncorhynchus mykiss) Recombinant
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
Product # :
CYT-1010Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Somatotropin Rainbow Trout (Oncorhynchus mykiss) Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids with an additional Ala at the N-terminus and having a molecular mass of 21, 535 Dalton. The Rainbow Trout (Oncorhynchus mykiss) Growth-Hormone Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.5% NaHCO3. Adjusted to pH-8.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Somatotropin Rainbow Trout (Oncorhynchus mykiss) Recombinant is biologically active in PDF-P1 3B9 cells stable transfected with rabbit GH receptors, though its activity is about 10 fold lower than that of human GH.
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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
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Growth-Hormone Rainbow Trout (Oncorhynchus mykiss) although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions 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 Growth-Hormone Rainbow Trout (Oncorhynchus mykiss) in 0.4% NaHCO3 or water adjusted to pH 8-9, not less than 100µg/ml and not more than 3mg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.
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Amino Acid Sequence
AIENQRLFNIAVSRVQHLHLLAQKMFNDFDGTLLPDERRQLNKIFLLDFCNSDSIVSPVD
KHETQKSSVLKLLHISFRLIESWEYPSQTLIISNSLMVRNANQISEKLSDLKVGINLLIT
GSQDGVLSLDDNDSQQLPPYGNYYQNLGGDGNVRRNYELLACFKKDMHKVETYLTVAKCR
KSLEANCTL.
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 :
MMP23B HumanDescription:
Matrix Metallopeptidase 23B Human Recombinant
Matrix Metallopeptidase 23B, MMP23B, MMP22, Matrix Metalloproteinase 23B, Matrix Metalloproteinase 22, Matrix Metalloproteinase In The Female Reproductive Tract, Matrix Metalloproteinase-21, Matrix Metalloproteinase-22, MIFR-1, MMP-21, MMP-22, MMP-23, MIFR, MMP23A, Matrix Metalloproteinase-23, EC 3.4.24.-, Femalysin, MMP21.
Product # :
ENZ-793Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MMP23B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 199 amino acids (79-254) and having a molecular mass of 22.6kDa.MMP23B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MMP23B solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Matrix Metallopeptidase 23B (MMP23B) belongs to the matrix metalloproteinase (MMP) family, and it is section of a duplicated region of chromosome 1p36.3. MMP23B is a protease. MMP23B regulates the surface expression of some potassium channels by holding them in the endoplasmic reticulum. Members of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis.
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Synonyms
Matrix Metallopeptidase 23B, MMP23B, MMP22, Matrix Metalloproteinase 23B, Matrix Metalloproteinase 22, Matrix Metalloproteinase In The Female Reproductive Tract, Matrix Metalloproteinase-21, Matrix Metalloproteinase-22, MIFR-1, MMP-21, MMP-22, MMP-23, MIFR, MMP23A, Matrix Metalloproteinase-23, EC 3.4.24.-, Femalysin, MMP21.
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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 MGSYTLTPAR LRWDHFNLTY RILSFPRNLL SPRETRRALA AAFRMWSDVS PFSFREVAPE QPSDLRIGFY PINHTDCLVS ALHHCFDGPT GELAHAFFPP HGGIHFDDSE YWVLGPTRYS WKKGVWLTDL VHVAAHEIGH ALGLMHSQHG RALMHLNATL RGWKALSQDE LWGLHRLYG.
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 :
P4HB HumanDescription:
Prolyl 4-Hydroxylase Beta Human Recombinant
P4Hbeta, PDI, PDIA1, PHD, PO4DB, PO4HB, ERBA2L.
Product # :
ENZ-252Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
P4HB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 512 amino acids (18-508 a.a.) and having a molecular mass of 57.5 kDa. The P4HB is fused to a 21 amino acid His Tag and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The P4HB 1mg/ml protein solution contains 20mM Tris-HCl pH-8, and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
P4HB is a multifunctional and highly abundant enzyme that is part of the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, P4HB has a role in hydroxylation of prolyl residues in preprocollagen. P4HB is a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds.
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Synonyms
P4Hbeta, PDI, PDIA1, PHD, PO4DB, PO4HB, ERBA2L.
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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 MDAPEEEDHV LVLRKSNFAE ALAAHKYLLV EFYAPWCGHC KALAPEYAKA AGKLKAEGSE IRLAKVDATE ESDLAQQYGV RGYPTIKFFR NGDTASPKEY TAGREADDIV NWLKKRTGPA ATTLPDGAAA ESLVESSEVA VIGFFKDVES DSAKQFLQAA
EAIDDIPFGI TSNSDVFSKY QLDKDGVVLF KKFDEGRNNF EGEVTKENLL DFIKHNQLPL VIEFTEQTAP KIFGGEIKTH ILLFLPKSVS DYDGKLSNFK TAAESFKGKI LFIFIDSDHT DNQRILEFFG LKKEECPAVR LITLEEEMTK YKPESEELTA ERITEFCHRF LEGKIKPHLM
SQELPEDWDK QPVKVLVGKN FEDVAFDEKK NVFVEFYAPW CGHCKQLAPI WDKLGETYKD HENIVIAKMD STANEVEAVK VHSFPTLKFF PASADRTVID YNGERTLDGF KKFLESGGQD GAGDDDDLED LEEAEEPDME EDDDQKAVKD EL.
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 :
LAP3 HumanDescription:
Leucine Aminopeptidase 3 Human Recombinant
Leucine Aminopeptidase 3, Peptidase S, PEPS, Proline Aminopeptidase, Leucyl Aminopeptidase, Prolyl Aminopeptidase, EC 3.4.11.1, LAP-3, LAPEP, Epididymis Secretory Protein Li 106, Cytosol Aminopeptidase, EC 3.4.11.5, HEL-S-106, EC 3.4.11, LAP, Cytosol aminopeptidase, Leucine aminopeptidase 3, Leucyl aminopeptidase, Proline aminopeptidase, Prolyl aminopeptidase.
Product # :
ENZ-889Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LAP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 539 amino acids (1-519 a.a) and having a molecular mass of 58.3kDa. LAP3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LAP3 protein solution (0.5mg/ml) containing 20mM Tris-HCl(pH8.5), 50% glycerol, 5mM DTT and 1mM EDTA.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Leucine Aminopeptidase 3 also known as LAP3 is a member of the peptidase M17 family. LAP3 is implicated in the processing as well as regular turnover of intracellular proteins. LAP3 catalyzes the removal of unsubstituted N-terminal amino acids from different peptides. LAP3 is responsible of releasing an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but could be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are as well readily hydrolyzed; however rates on arylamides are exceedingly low.
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Synonyms
Leucine Aminopeptidase 3, Peptidase S, PEPS, Proline Aminopeptidase, Leucyl Aminopeptidase, Prolyl Aminopeptidase, EC 3.4.11.1, LAP-3, LAPEP, Epididymis Secretory Protein Li 106, Cytosol Aminopeptidase, EC 3.4.11.5, HEL-S-106, EC 3.4.11, LAP, Cytosol aminopeptidase, Leucine aminopeptidase 3, Leucyl aminopeptidase, Proline aminopeptidase, Prolyl aminopeptidase.
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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 MFLLPLPAAG RVVVRRLAVR RFGSRSLSTA DMTKGLVLGI YSKEKEDDVP QFTSAGENFD KLLAGKLRET LNISGPPLKA GKTRTFYGLH QDFPSVVLVG LGKKAAGIDE QENWHEGKEN IRAAVAAGCR QIQDLELSSV EVDPCGDAQA AAEGAVLGLY EYDDLKQKKK MAVSAKLYGS GDQEAWQKGV LFASGQNLAR QLMETPANEM TPTRFAEIIE KNLKSASSKT EVHIRPKSWI EEQAMGSFLS VAKGSDEPPV FLEIHYKGSP NANEPPLVFV GKGITFDSGG ISIKASANMD LMRADMGGAA TICSAIVSAA KLNLPINIIG LAPLCENMPS GKANKPGDVV RAKNGKTIQV DNTDAEGRLI LADALCYAHT FNPKVILNAA TLTGAMDVAL GSGATGVFTN SSWLWNKLFE ASIETGDRVW RMPLFEHYTR QVVDCQLADV NNIGKYRSAG ACTAAAFLKE FVTHPKWAHL DIAGVMTNKD EVPYLRKGMT GRPTRTLIEF LLRFSQDNA.
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 :
GLRX2 HumanDescription:
Glutaredoxin 2 Human Recombinant
Thioltransferase, Glutathione-dependent oxidoreductase 2, TTR, TTR1, GLRX2, GRX2, GRX-2, GLRX-2, Glutaredoxin 2, CGI133.
Product # :
ENZ-466Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Glutaredoxin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 154 amino acids (20-164 a.a.) and having a molecular mass of 17 kDa. The GRX2 is fused to 9 amino acid His tag at C-Terminus.
Source
Escherichia Coli.
Formulation
Glutaredoxin-2 solution (0.5mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0), 0.1mM PMSF and 10% glycerol.
Purity
Purity of GRX2 is greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
GLRX2 is a multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. Glutaredoxins are a family of glutathione-dependent hydrogen donors that participate in a variety of cellular redox reactions.
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Synonyms
Thioltransferase, Glutathione-dependent oxidoreductase 2, TTR, TTR1, GLRX2, GRX2, GRX-2, GLRX-2, Glutaredoxin 2, CGI133.
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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
MSAGWLDRAA GAAGAAAAAA SGMESNTSSS LENLATAPVN QIQETISDNC VVIFSKTSCS YCTMAKKLFH DMNVNYKVVE LDLLEYGNQF QDALYKMTGE RTVPRIFVNG TFIGGATDTH RLHKEGKLLP LVHQCYLKKS KRKEFQLEHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.