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1000 results found for “Protease”
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Name :
CKMB HumanDescription:
Creatine Kinase MB Human Recombinant
CKMB, CK-MB
Product # :
CKI-286Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Creatine Kinase MB produced in E.Coli is a single, non-glycosylated, polypeptide chain, having a molecular weight of ~44kDa.The CKMB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein solution contains 50mM Tris-HCL, 5mM B-mercaptoethanol, 1mM EDTA, 5mM disodium Succinate, Ph 8.0 and 50% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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Stability
CKMB although stable at 10°C for 7 days, should be stored below -18°C.Please prevent freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GPT2 MouseDescription:
Glutamic-Pyruvate Transaminase 2 Mouse Recombinant
ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 2.
Product # :
ENZ-1096Price :
Quantity :
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Shipped with Ice Packs
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Description
GPT2 Mouse Recombinant produced in E. coli is a single polypeptide chain containing 522 amino acids (1-522) and having a molecular mass of 60.1 kDa. Mouse GPT2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GPT2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 7.5), 20% glycerol, and 2mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
Biological Activity
Greater than 50units/mg, and is defined as the amount of enzyme that cleaves 1umole of L-Alanine to L-Glutamate per minute at pH7.5 at 37℃.
More Info
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Introduction
Glutamic-Pyruvate Transaminase 2 (GPT2) catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids.
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Synonyms
ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 2.
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Physical Appearance
Sterile Filtered colorless solution.
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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 MQRAAVLVRR GSCPRASGPW GRSHSSAAAE ASAALKVRPE RSPRDRILTL ESMNPQVKAV EYAVRGPIVL KAGEIEMELQ RGIKKPFTEV IRANIGDAHA MGQQPITFLR QVMALCTYPN LLNSPSFPED AKKRARRILQ ACGGNSLGSY SASQGVNCIR EDVAAFITRR DGVPADPDNI YLTTGASDGI STILKLLVSG GGKSRTGVMI PIPQYPLYSA VISELDAVQV NYYLDEENCW ALNVDELRRA LRQAKDHCDP KVLCIINPGN PTGQVQSRKC IEDVIHFAWE EKLFLLADEV YQDNVYSPDC RFHSFKKVLY QMGHEYSSNV ELASFHSTSK GYMGECGYRG GYMEVINLHP EIKGQLVKLL SVRLCPPVSG QAAMDIVVNP PEPGEESFEQ FSREKEFVLG NLAKKAKLTE DLFNQVPGIQ CNPLQGAMYA FPRILIPAKA VEAAQSHKMA PDMFYCMKLL EETGICVVPG SGFGQREGTY HFRMTILPPV DKLKTVLHKV KDFHLKFLEQ.
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 :
PIP ProteinDescription:
Prolactin-Induced Protein Human Recombinant
Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, GCDFP15, GPIP4, PIP.
Product # :
CYT-793Price :
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Description
PIP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (29-146 a.a.) and having a molecular mass of 15.9kDa.PIP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PIP protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Prolactin-inducible protein (PIP) is a main protein component of benign breast gross cysts. PIP is a famous indicator of breast cancer, since it is found in around 50% of all breast cancer specimens. PIP is expressed in exocrine glands, in pathologic conditions, in breast cysts and breast cancers exhibiting apocrine features. PIP and prostate specific antigen are co-expressed in androgen receptor-positive breast tumours.
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Synonyms
Prolactin-inducible protein, Gross cystic disease fluid protein 15, GCDFP-15, Prolactin-induced protein, Secretory actin-binding protein, SABP, gp17, GCDFP15, GPIP4, PIP.
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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 MGSQDNTRKI IIKNFDIPKS VRPNDEVTAV LAVQTELKEC MVVKTYLISS IPLQGAFNYK YTACLCDDNP KTFYWDFYTN RTVQIAAVVD VIRELGICPD DAAVIPIKNN RFYTIEILKV E.
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 :
PTGDS HumanDescription:
Prostaglandin D2 Synthase Human Recombinant
Prostaglandin-H2 D-isomerase, Beta-trace protein, Cerebrin-28, Glutathione-independent PGD synthase, Lipocalin-type prostaglandin-D synthase, Prostaglandin-D2 synthase, PGD2 synthase, PGDS, PGDS2, PTGDS, PDS, PGD2, LPGDS, L-PGDS.
Product # :
ENZ-109Price :
Quantity :
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Shipped with Ice Packs
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Description
PTGDS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (23-190 a.a.) and having a molecular mass of 20.9kDa.PTGDS is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PTGDS solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol, 1mM EDTA and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Prostaglandin-H2 D-isomerase (PTGDS) is a glutathione-independent prostaglandin D synthase which catalyzes the conversion of prostaglandin H2 (PGH2) to postaglandin D2 (PGD2). PTGDS is may have vital roles in both maturation and maintenance of the central nervous system and male reproductive system. PTGDS is the most abundant protein in the cerebral spinal fluid and recent evidence suggests that PTGDS acts as a beta-amyloid chaperone and may play a role in the deposition of Ab plaques in Alzheimer’s disease.
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Synonyms
Prostaglandin-H2 D-isomerase, Beta-trace protein, Cerebrin-28, Glutathione-independent PGD synthase, Lipocalin-type prostaglandin-D synthase, Prostaglandin-D2 synthase, PGD2 synthase, PGDS, PGDS2, PTGDS, PDS, PGD2, LPGDS, L-PGDS.
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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 MAPEAQVSVQ PNFQQDKFLG RWFSAGLASN SSWLREKKAA LSMCKSVVAP ATDGGLNLTS TFLRKNQCET RTMLLQPAGS LGSYSYRSPH WGSTYSVSVV ETDYDQYALL YSQGSKGPGE DFRMATLYSR TQTPRAELKE KFTAFCKAQG FTEDTIVFLP QTDKCMTEQ.
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 :
HSD17B11 HumanDescription:
Hydroxysteroid (17-beta) Dehydrogenase 11 Human Recombinant
17-beta-hydroxysteroid dehydrogenase 11, 17-beta-HSD 11, 17bHSD11, 17betaHSD11, 17-beta-hydroxysteroid dehydrogenase XI, 17-beta-HSD XI, 17betaHSDXI, Cutaneous T-cell lymphoma-associated antigen HD-CL-03, CTCL-associated antigen HD-CL-03, Dehydrogenase/reductase SDR family member 8, Retinal short-chain dehydrogenase/reductase 2, retSDR2, HSD17B11, DHRS8, PAN1B, SDR16C2, 17BHSD11.
Product # :
ENZ-049Price :
Quantity :
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Description
HSD17B11 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 287 amino acids (20-285 a.a.) and having a molecular mass of 31.4kDa. The HSD17B11 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HSD17B11 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Dehydrogenase/reductase SDR family member 8 (HSD17B11) is a member of the HSD17B family of proteins, which regulate the availability of steroids within various tissues throughout the body. HSD17B11 is widely expressed with the highest levels found in the retina, pancreas, kidney, liver, lung, adrenal, small intestine, ovary and heart as well as in steroidogenic cells. HSD17B11 converts androstan-3-?,17-?-diol (3-?-diol) to androsterone, suggesting it may participate in androgen metabolism during steroidogenesis.
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Synonyms
17-beta-hydroxysteroid dehydrogenase 11, 17-beta-HSD 11, 17bHSD11, 17betaHSD11, 17-beta-hydroxysteroid dehydrogenase XI, 17-beta-HSD XI, 17betaHSDXI, Cutaneous T-cell lymphoma-associated antigen HD-CL-03, CTCL-associated antigen HD-CL-03, Dehydrogenase/reductase SDR family member 8, Retinal short-chain dehydrogenase/reductase 2, retSDR2, HSD17B11, DHRS8, PAN1B, SDR16C2, 17BHSD11.
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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 MESFVKLFIP KRRKSVTGEI VLITGAGHGI GRLTAYEFAK LKSKLVLWDI NKHGLEETAA KCKGLGAKVH TFVVDCSNRE DIYSSAKKVK AEIGDVSILV NNAGVVYTSD LFATQDPQIE KTFEVNVLAH FWTTKAFLPA MTKNNHGHIV TVASAAGHVS VPFLLAYCSS KFAAVGFHKT LTDELAALQI TGVKTTCLCP NFVNTGFIKN PSTSLGPTLE PEEVVNRLMH GILTEQKMIF IPSSIAFLTT LERILPERFL AVLKQKI.
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 :
ENTPD3 Human, sf9 BioactiveDescription:
Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant, sf9 Bioactive
Ectonucleoside Triphosphate Diphosphohydrolase 3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, CD39L3, HB6, NTPDase-3, EC 3.6.1, Ectonucleoside triphosphate diphosphohydrolase 3, NTPDase 3, CD39 antigen-like 3, Ecto-ATP diphosphohydrolase 3, Ecto-ATPDase 3, Ecto-ATPase 3, Ecto-apyrase 3, HB6.
Product # :
ENZ-1020Price :
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Description
ENTPD3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 451 amino acids (44-485a.a.) and having a molecular mass of 50.7kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).ENTPD3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ENTPD3 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 250,000 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze ATP per minute at pH 7.5 at 37C.More Info
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Introduction
Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.
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Synonyms
Ectonucleoside Triphosphate Diphosphohydrolase 3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, CD39L3, HB6, NTPDase-3, EC 3.6.1, Ectonucleoside triphosphate diphosphohydrolase 3, NTPDase 3, CD39 antigen-like 3, Ecto-ATP diphosphohydrolase 3, Ecto-ATPDase 3, Ecto-ATPase 3, Ecto-apyrase 3, HB6.
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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
ADLQIHKQEV LPPGLKYGIV LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS SYGNNPQDVP RAFEECMQKV KGQVPSHLHG STPIHLGATA GMRLLRLQNE TAANEVLESI QSYFKSQPFD FRGAQIISGQ EEGVYGWITA NYLMGNFLEK NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS DIMQVSLYGY VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ ETCSFDGVYQ PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS QNWSQLPLLL PKFDEVYARS YCFSANYIYH LFVNGYKFTE ETWPQIHFEK EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL PIEPPHHHHHH.
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 :
OTC HumanDescription:
Ornithine Carbamoyltransferase Human Recombinant
Ornithine carbamoyltransferase mitochondrial, Ornithine transcarbamylase, OTCase, OCTD, EC 2.1.3.3.
Product # :
ENZ-596Price :
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Description
OTC Recombinant produced in E. coli is a single polypeptide chain containing 347 amino acids (33-354) and having a molecular mass of 38.9kDa.OTC is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The OTC solution (0.5mg/ml) contains 20mM MES buffer (pH 6.0), 100mM Nacl, 2mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
OTC is a member of the ATCase/OTCase family. OTC has a key part in the urea cycle, catalyzing the second step in this pathway: the transformation of L-orthinine and carbamoyl phosphate to L-citrulline. In humans, the urea cycle is a vital pathway to detoxification of ammonia. Alterations in the gene encoding OTC are linked to the X-linked disorder OTCD (ornithine carbamoyltransferase deficiency). OTCD disorder of the urea cycle is characterized by hyperammonemia.
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Synonyms
Ornithine carbamoyltransferase mitochondrial, Ornithine transcarbamylase, OTCase, OCTD, EC 2.1.3.3.
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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).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMNKVQL KGRDLLTLKN FTGEEIKYML WLSADLKFRI KQKGEYLPLL QGKSLGMIFE KRSTRTRLST ETGFALLGGH PCFLTTQDIH LGVNESLTDT ARVLSSMADA VLARVYKQSD LDTLAKEASI PIINGLSDLY HPIQILADYL TLQEHYSSLK GLTLSWIGDG NNILHSIMMS AAKFGMHLQA ATPKGYEPDA SVTKLAEQYA KENGTKLLLT NDPLEAAHGG NVLITDTWIS MGQEEEKKKR LQAFQGYQVT MKTAKVAASD WTFLHCLPRK PEEVDDEVFY SPRSLVFPEA ENRKWTIMAV MVSLLTDYSP QLQKPKF.
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 :
IMPDH1 HumanDescription:
IMP Dehydrogenase 1 Human Recombinant
EC 1.1.1.205, IMP (inosine monophosphate) dehydrogenase 1, LCA11, RP10, IMPDH 1, IMPD 1, IMPDH-I, SwSS2608, DKFZp781N0678.
Product # :
ENZ-525Price :
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Shipped with Ice Packs
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Description
IMPDH1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 534 amino acids (1-514 a.a.) and having a molecular mass of 57.5 kDa. The IMPDH1 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IMPDH1 Human solution containing 20mM Tris-HCl pH-8, 1mM DTT & 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
IMPDH1 is a rate limiting enzyme in the de novo synthesis of guanine nucleotides and consequently participates in the regulation of cell growth. IMPDH1 takes part in the development of malignancy and the growth progression of some tumors. IMPDH1 performs as a homotetramer to regulate cell growth. IMPDH1 catalyzes the synthesis of xanthine monophosphate (XMP) from inosine-5''-monophosphate (IMP). Defects in this gene are a cause of retinitis pigmentosa type 10 (RP10).
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Synonyms
EC 1.1.1.205, IMP (inosine monophosphate) dehydrogenase 1, LCA11, RP10, IMPDH 1, IMPD 1, IMPDH-I, SwSS2608, DKFZp781N0678.
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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 MADYLISGGT GYVPEDGLTA QQLFASADGL TYNDFLILPG FIDFIADEVD LTSALTRKIT LKTPLISSPM DTVTEADMAI AMALMGGIGF IHHNCTPEFQ ANEVRKVKKF EQGFITDPVV LSPSHTVGDV LEAKMRHGFS GIPITETGTM GSKLVGIVTS RDIDFLAEKD HTTLLSEVMT PRIELVVAPA GVTLKEANEI LQRSKKGKLP IVNDCDELVA IIARTDLKKN RDYPLASKDS QKQLLCGAAV GTREDDKYRL DLLTQAGVDV IVLDSSQGNS VYQIAMVHYI KQKYPHLQVI GGNVVTAAQA KNLIDAGVDG LRVGMGCGSI CITQEVMACG RPQGTAVYKV AEYARRFGVP IIADGGIQTV GHVVKALALG ASTVMMGSLL AATTEAPGEY FFSDGVRLKK YRGMGSLDAM EKSSSSQKRY FSEGDKVKIA QGVSGSIQDK GSIQKFVPYL IAGIQHGCQD IGARSLSVLR SMMYSGELKF EKRTMSAQIE GGVHGLHSYE KRLY.
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 :
CBR3 HumanDescription:
Carbonyl Reductase-3 Human Recombinant
Carbonyl reductase [NADPH] 3, NADPH-dependent carbonyl reductase 3, CBR3, carbonyl reductase 3, hCBR3, SDR21C2.
Product # :
ENZ-428Price :
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Description
Recombinant Human CBR3 fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated polypeptide chain containing 297 amino acids (1-277 a.a) and having a molecular mass of 33kDa. CBR3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CBR3 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
CBR3 catalyzes the reduction of a large number of biologically and pharmacologically active carbonyl compounds to their corresponding alcohols. CBR3 is one of several monomeric NADPH-dependent oxidoreductases. Furthermore, CBR3 contains 3 exons spanning 11.2 kilobases and is strongly linked to another carbonyl reductase gene, the CBR1. It was suggested that CBR3 mediates 9-cis-retinoic acid-induced cytostatis and is a potential prognostic marker for oral malignancy.
CBR3 is identified in the ovary, pancreas, intestine, colon, kidney, brain, thymus, lung, heart, liver, spleen, leukocyte, prostate and the testis.
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Synonyms
Carbonyl reductase [NADPH] 3, NADPH-dependent carbonyl reductase 3, CBR3, carbonyl reductase 3, hCBR3, SDR21C2.
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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 MSSCSRVALV TGANRGIGLA IARELCRQFS GDVVLTARDV ARGQAAVQQL QAEGLSPRFH QLDIDDLQSI RALRDFLRKE YGGLNVLVNN AAVAFKSDDP MPFDIKAEMT LKTNFFATRN MCNELLPIMK PHGRVVNISS LQCLRAFENC SEDLQERFHS ETLTEGDLVD LMKKFVEDTK NEVHEREGWP NSPYGVSKLG VTVLSRILAR RLDEKRKADR ILVNACCPGP VKTDMDGKDS IRTVEEGAET PVYLALLPPD ATEPQGQLVH DKVVQNW.
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 :
PSMB1 HumanDescription:
Proteasome Subunit Beta Type 1 Human Recombinant
HC5, PSC5, PMSB1, FLJ25321, KIAA1838, PSMB1, Proteasome subunit beta type-1, Proteasome component C5, Macropain subunit C5, Multicatalytic endopeptidase complex subunit C5, Proteasome gamma chain.
Product # :
ENZ-405Price :
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Description
PSMB1 Human Recombinant fused to a 37 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 250 amino acids (30-241) and having a molecular mass of 27.7 kDa. The PSMB1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PSMB1 solution contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PSMB1 is part of the proteasome B-type family, also identified as the T1B family, that is a 20S core beta subunit. PSMB1 is tightly linked to the TBP (TATA-binding protein) gene in human and in mouse, and is transcribed in the opposite orientation in both species.The main function of PSMB1 is its degradation activity of unnecessary or damaged proteins by proteolysis. PSMB1 is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with arg, phe, tyr, leu, and glu adjacent to the leaving group at neutral or slightly basic ph. the proteasome has an atp-dependent proteolytic activity.
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Synonyms
HC5, PSC5, PMSB1, FLJ25321, KIAA1838, PSMB1, Proteasome subunit beta type-1, Proteasome component C5, Macropain subunit C5, Multicatalytic endopeptidase complex subunit C5, Proteasome gamma chain.
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Physical Appearance
Sterile Filtered clear colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMFS PYVFNGGTIL AIAGEDFAIV ASDTRLSEGF SIHTRDSPKC YKLTDKTVIG CSGFHGDCLT LTKIIEARLK MYKHSNNKAM TTGAIAAMLS TILYSRRFFP YYVYNIIGGL DEEGKGAVYS FDPVGSYQRD SFKAGGSASA MLQPLLDNQV GFKNMQNVEH VPLSLDRAMR LVKDVFISAA ERDVYTGDAL RICIVTKEGI REETVSLRKD.
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 :
PSME1 HumanDescription:
Proteasome Activator Subunit 1 Human Recombinant
REG-alpha, PA28alpha, PA28a, Proteasome Activator subunit-1, Proteasome Activator 28 subunit alpha.
Product # :
PRO-266Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
PSME1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 269 amino acids (1-249a.a.) and having a molecular mass of 30.8kDa.PSME1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PSME1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
PSME1 is a Proteasome Activator 28 subunit alpha essential for presentation of certain major histocompatibility (MHC) class I antigens. The PSME1 complex is an alternate proteasome activator which operates with no use of ubiquitin. The PSME1 complex is made out of two homologous subunits, alpha and beta, that functions in similar catalytic properties and is connected to a hexameric ring.
-
Synonyms
REG-alpha, PA28alpha, PA28a, Proteasome Activator subunit-1, Proteasome Activator 28 subunit alpha.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAMLRVQPEA QAKVDVFRED LCTKTENLLG SYFPKKISEL DAFLKEPALN EANLSNLKAP LDIPVPDPVK EKEKEERKKQ QEKEDKDEKK KGEDEDKGPP CGPVNCNEKI VVLLQRLKPE IKDVIEQLNL VTTWLQLQIP RIEDGNNFGV AVQEKVFELM TSLHTKLEGF HTQISKYFSE RGDAVTKAAK QPHVGDYRQL VHELDEAEYR DIRLMVMEIR NAYAVLYDII LKNFEKLKKP RGETKGMIY
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 :
KLK8 MouseDescription:
Kallikrein-8 Mouse Recombinant
Ovasin, PRSS19, TADG14, NRPN, NP, Kallikrein 8 (Neuropsin/Ovasin) 2 EC 3.4.21.118, Kallikrein-8, Neuropsin, EC 3.4.21 61, HNP, HK8
Product # :
ENZ-1014Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
KLK8 Mouse Recombinant produced in Sf9 is a single, glycosylated polypeptide chain containing 240 amino acids (29-260) and having a molecular mass of 26.5kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). The KLK8 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
KLK8 protein 0.5mg/ml is supplied in PBS, pH-7.4, and 10% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Kallikrein-8 is a serine protease which degrades various proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. Kallikrein-8 takes part in the formation and maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway, regulates Schaffer-collateral long-term potentiation in the hippocampus and is essential for memory acquisition and synaptic plasticity. Kallikrein-8 participates in the secondary phase of pathogenesis following spinal cord injury and also takes part in skin desquamation and keratinocyte proliferation.
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Synonyms
Ovasin, PRSS19, TADG14, NRPN, NP, Kallikrein 8 (Neuropsin/Ovasin) 2 EC 3.4.21.118, Kallikrein-8, Neuropsin, EC 3.4.21 61, HNP, HK8
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
QGSKILEGRE CIPHSQPWQA ALFQGERLIC GGVLVGDRWV LTAAHCKKQK YSVRLGDHSL QSRDQPEQEI QVAQSIQHPC YNNSNPEDHS HDIMLIRLQN SANLGDKVKP VQLANLCPKV GQKCIISGWG TVTSPQENFP NTLNCAEVKI YSQNKCERAY PGKITEGMVC AGSSNGADTC QGDSGGPLVC DGMLQGITSW GSDPCGKPEK PGVYTKICRY TTWIKKTMDN RDLEHHHHHH.
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 :
Streptavidin ProteinDescription:
Streptavidin
Product # :
PRO-283Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- More Info
Description
Streptavidin is a protein produced by Streptomyces avidinii and isolated by purification from fermentation broth. The pure, homogeneous protein shows predominantly one single band in SDS PAGE. Streptavidin consists of 4 identical subunits, each bearing an active binding site for biotin. Streptavidin has a molecular weight of 55kDa.
Source
Bacterium Streptomyces avidinii.
Formulation
The Streptavidin was lyophilized from a 25mg/ml solution in 10 mM potassium phosphate buffer pH 6.5
More Info
-
Introduction
Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is wilyde used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.
-
Physical Appearance
Sterile Filtered lyophilized powder.
-
Stability
Streptavidin although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. For longer storage in dissolved form add 1mM EDTA and/or 0.02 % NaN3 or pass the solution through a sterile filter.Please prevent freeze-thaw cycles.
-
Solubility
Gives a clear solution at 10mg/ml in 4.0 mM potassium phosphate pH 6.5
-
Specific Activity
The biological activity is 16.8 U/mg, 1 unit binds 1µg biotin.
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 :
Protein-L CysDescription:
Protein L Cys Recombinant
Product # :
PRO-1931Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- purity
- More Info
- sds-page, HPLC
Description
Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at C-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 366 amino acids in total and having a molecular mass of 40.6kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein-L was lyophilized without any additives.
Purity
Greater than 96.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.sds-page, HPLC
More Info
-
Introduction
The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Protein-L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-L 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.
-
Solubility
It is recommended to reconstitute the lyophilized Protein-L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPE EKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAGC.
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 :
GPT Human, ActiveDescription:
Glutamic-Pyruvate Transaminase Human Recombinant, Active
Alanine aminotransferase 1, ALT1, EC 2.6.1.2, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1, GPT, AAT1, GPT1.
Product # :
ENZ-280Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Alanine Aminotransferase Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 495a.a and having a molecular mass of 54,479 Dalton. The amino acid sequence is the same as that of native form of human liver ALT.The ALT is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was dialyzed against 40mM sodium acetate buffer (pH 5.5), 1mM DTT,1mM EDTA, 5mM 2-oxoglutarate and 0.1mM pyridoxal-5'-phosphate.
Purity
Greater than 95.0% as determined by Analysis by SDS-PAGE.
Biological Activity
The specific activity was found to be 839 U/mg.
More Info
-
Introduction
Alanine transaminase or ALT is a transaminaseenzyme.
ALT is found in serumand in various bodily tissues, but is most commonly associated with the liver; It catalyzes the transfer of an aminogroup from alanineto a-ketoglutarate, the products of this reversible transaminationreaction being pyruvateand glutamatealanine+ a-ketoglutarate= pyruvate+ glutamate
It is commonly measured clinically as a part of a diagnostic liver function test, to determine liver health. It is also called serum glutamate pyruvate transaminase (SGPT) or alanine aminotransferase (ALAT). Diagnostically, it is almost always measured in units/litre (U/L). -
Synonyms
Alanine aminotransferase 1, ALT1, EC 2.6.1.2, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1, GPT, AAT1, GPT1.
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Physical Appearance
Sterile liquid formulation.
-
Stability
AAT1 although stable at 10°C for 5 days, should be stored below -18°C.Please prevent freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PON1 HumanDescription:
Paraoxonase-1 Human Recombinant
Serum paraoxonase, arylesterase 1, EC 3.1.1.2, EC 3.1.8.1, PON 1, Serum aryldialkylphosphatase 1, A-esterase 1, Aromatic esterase 1, K-45, ESA, PON.
Product # :
ENZ-299Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Paraoxonase-1 Isoform Human Recombinant is expressed in E. coli, fused to a 7 amino acid c- terminal hexahistidine tag, containing 362 amino acids and ( 1-355 a.a.) having a total molecular weight of 40.68kDa. The PON1 purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
lyophilized from 0.5 mg/mL in 20mM Tris buffer, 50 mM NaCl, pH 7.5
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Paraoxonase 1 also called Esterase-A is involved in the detoxification of organophosphate insecticides such as parathion. Paraoxonase 1 may also confer protection against coronary artery disease by destroying proinflammatory oxidized lipids present in oxidized low-density lipoproteins (LDLs).
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Synonyms
Serum paraoxonase, arylesterase 1, EC 3.1.1.2, EC 3.1.8.1, PON 1, Serum aryldialkylphosphatase 1, A-esterase 1, Aromatic esterase 1, K-45, ESA, PON.
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Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized PON1 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
MAKLIALTLLGMGLALFRNHQSSYQTRLNALREVQPVELPNCNLVKGIETGSEDLEILPNGL
AFISSGLKYPGIKSFNPNSPGKILLMDLNEEDPTVLELGITGSKFDVSSFNPHGISTFTDEDNA
MYLLVVNHPDAKSTVELFKFQEEEKSLLHLKTIRHKLLPNLNDIVAVGPEHFYGTNDHYFLD
PYLQSWEMYLGLAWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYVYIAELLAHKIHVYEK
HANWTLTPLKSLDFNTLVDNISVDPETGDLWVGCHPNGMKIFFYDSENPPASEVLRIQNILT
EEPKVTQVYAENGTVLQGSTVASVYKGKLLIGTVFHKALYCELEHHHHHH.
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 :
Streptolysin-ODescription:
Streptolysin-O Streptococcus Pyogenes Recombinant
Streptolysin O, Thiol-activated cytolysin, slo.
Product # :
PRO-2302Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Streptococcus Pyogenes Streptolysin-O produced in E.coli is a single, non-glycosylated, polypeptide chain containing 538 amino acids and having a molecular mass of 60.1kDa.The Streptolysin-O is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Streptolysin-O protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Streptolysin-O is a sulfhydryl-activated toxin which causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the Streptolysin-O protein undergoes a major conformation change, leading to its insertion in the host membrane and creation of an oligomeric pore complex. Cholesterol may be needed for binding to host membranes, membrane insertion and pore formation. Streptolysin-O can be reversibly inactivated by oxidation.
-
Synonyms
Streptolysin O, Thiol-activated cytolysin, slo.
-
Physical Appearance
Sterile Filtered white lyophilized powder.
-
Stability
Lyophilized Streptolysin-O although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Streptolysin-O 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.
-
Solubility
It is recommended to reconstitute the lyophilized Streptolysin-O in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
NKQNTASTET TTTNEQPKPE SSELTTEKAG QKTDDMLNSN DMIKLAPKEM PLESAEKEEK KSEDKKKSEE DHTEEINDKI YSLNYNELEV LAKNGETIEN FVPKEGVKKA DKFIVIERKK KNINTTPVDI SIIDSVTDRT YPAALQLANK GFTENKPDAV VTKRNPQKIH IDLPGMGDKA TVEVNDPTYA NVSTAIDNLV NQWHDNYSGG NTLPARTQYT ESMVYSKSQI EAALNVNSKI LDGTLGIDFK SISKGEKKVM IAAYKQIFYT VSANLPNNPA DVFDKSVTFK ELQRKGVSNE APPLFVSNVA YGRTVFVKLE TSSKSNDVEA AFSAALKGTD VKTNGKYSDI LENSSFTAVV LGGDAAEHNK VVTKDFDVIR NVIKDNATFS RKNPAYPISY TSVFLKNNKI AGVNNRTEYV ETTSTEYTSG KINLSHQGAY VAQYEILWDE INYDDKGKEV ITKRRWDNNW YSKTSPFSTV IPLGANSRNI RIMARECTGL AWEWWRKVID ERDVKLSKEI NVNISGSTLS PYGSITYK.
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 :
Luciferase Firefly, ActiveDescription:
Luciferin 4-Monooxygenase Firefly Recombinant, Active
Luciferase-like monooxygenase, LUC, EC 1.13.12.7.
Product # :
ENZ-1035Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
Luciferase produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-311 a.a) and having a molecular mass of 38.5kDa. Luciferase is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Luciferase solution (0.5mg/ml) contains 20mM Tris-HCl (pH8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >1x109 light units/mg. One luciferase enzyme units will produce one Relative Light Unit (RLU) at pH7.5 at 25°C.
More Info
-
Introduction
Luciferase is a general term for the class of oxidative enzymes used in bioluminescence and is distinct from a photoprotein. Luciferase catalyzes a bioluminescent reaction which involves the substrate luciferin as well as Mg2+ and ATP, produces green light with a wavelength of 562 nm. Luciferase from firefly is broadly used as a reporter for studying gene regulation and function, and for pharmaceutical screening.
-
Synonyms
Luciferase-like monooxygenase, LUC, EC 1.13.12.7.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMTSKVY DPEQRKRMIT GPQWWARCKQ MNVLDSFINY YDSEKHAENA VIFLHGNAAS SYLWRHVVPH IEPVARCIIP DLIGMGKSGK SGNGSYRLLD HYKYLTAWFE LLNLPKKIIF VGHDWGACLA FHYSYEHQDK IKAIVHAESV VDVIESWDEW PDIEEDIALI KSEEGEKMVL ENNFFVETML PSKIMRKLEP EEFAAYLEPF KEKGEVRRPT LSWPREIPLV KGGKPDVVQI VRNYNAYLRA SDDLPKMFIE SDPGFFSNAI VEGAKKFPNT EFVKVKGLHF SQEDAPDEMG KYIKSFVERV LKNEQ.
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 :
TrxR YeastDescription:
Thioredoxin Reductase (NADPH) Yeast Recombinant
Thioredoxin Reductase (NADPH), NTR, TrxR.
Product # :
ENZ-278Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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Description
Thioredoxin Reductase (NADPH) Yeast Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 36 kDa. Thioredoxin Reductase is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Each mg of protein contains 20mM phosphate buffer pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The specific activity was found to be 5.8 IU/mg.
More Info
-
Introduction
Thioredoxin reductase (TrxR/NTR), an enzyme belonging to the flavoprotein family of pyridine nucleotide-disulfide oxidoreductases. Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses.
-
Synonyms
Thioredoxin Reductase (NADPH), NTR, TrxR.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
NTR although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized NTR in sterile 18MΩ-cm H2O.
-
Unit Definition
One unit equals the change in absorbance at 412 nm per minute at 25°C using 0.2mM NADPH containing 5mM DTNB (pH 7.0).
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 :
GNMT Human, ActiveDescription:
Glycine N-Methyltransferase Human Recombinant , Active
Glycine N-methyltransferase, GNMT, Glycine N-Methyltransferase, EC 2.1.1.20Epididymis Secretory Sperm Binding Protein Li 182mP, HEL-S-182mP.
Product # :
ENZ-1059Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GNMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-295 a.a) and having a molecular mass of 34.9kDa.GNMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GNMT protein solution (1mg/ml) containing 20 mM Tris-HCl buffer (pH 8.0) and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 100 nmol/min/mg, and is defined as the amount of enzyme that transfer 1.0 nmole of methyl group per minute at 37C.
More Info
-
Introduction
GNMT is an enzyme that catalyzes the conversion of S-adenosyl-L-methionine with glycine to S-adenosyl-L-homocysteine and sarcosine. GNMT is located in the cytoplasm and acts as a homotetramer. Defects in the GNMT gene causes of GNMT deficiency (hypermethioninemia). GNMT affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine and is involved in the detoxification pathway in liver cells. GNMT expression is diminished in human hepatocellular carcinoma (HCC). GNMT catalyzes the methylation of glycine by using s- adenosylmethionine (adomet) to form n-methylglycine (sarcosine) with the concomitant production of s-adenosylhomocysteine (adohcy). GNMT plays an essential role in the regulation of tissue concentration of adomet and of metabolism of methionine.
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Synonyms
Glycine N-methyltransferase, GNMT, Glycine N-Methyltransferase, EC 2.1.1.20
Epididymis Secretory Sperm Binding Protein Li 182mP, HEL-S-182mP. -
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVDSVYRTRS LGVAAEGLPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL GLLRQHGCQR VLDVACGTGV DSIMLVEEGF SVTSVDASDK MLKYALKERW NRRHEPAFDK WVIEEANWMT LDKDVPQSAE GGFDAVICLG NSFAHLPDCK GDQSEHRLAL KNIASMVRAG GLLVIDHRNY DHILSTGCAP PGKNIYYKSD LTKDVTTSVL IVNNKAHMVT LDYTVQVPGA GQDGSPGLSK FRLSYYPHCL ASFTELLQAA FGGKCQHSVL GDFKPYKPGQ TYIPCYFIHV LKRTD.
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 :
Cystatin-C ProteinDescription:
Cystatin-C Human Recombinant
Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.
Product # :
PRO-2601Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
- formulation
- purity
- More Info
Description
Cystatin-C Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 120 amino acids and having a molecular mass of 13.3kDa. Cystatin-C is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Cystatin-C is supplied as a 0.2 μm filtered solution containing 20mM Tris-HCl, 50 % glycerol, pH 8.0 and 300mM NaCl.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and subsequently, the atherosclerosis and abdominal aortic aneurysm.
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Synonyms
Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.
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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
SSPGKPPRLV GGPMDASVEE EGVRRALDFA VGEYNKASND MYHSRALQVV RARKQIVAGV NYFLDVELGR TTCTKTQPNL DNCPFHDQPH LKRKAFCSFQ IYAVPWQGTM TLSKSTCQDA.
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 :
UCHL1 (1-126) HumanDescription:
Ubiquitin Carboxyl-Terminal Hydrolase L1 (1-126) Human Recombinant
PGP 9.5, UCHL1, PGP9.5, PARK5.
Product # :
PRO-2823Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The UCHL1 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The UCHL1 His-Tagged Fusion Protein, produced in E. coli, is a 19kDa protein containing 126 amino acid residues of the UCHL1 Human, 1-126 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
PGP 9.5, UCHL1, PGP9.5, PARK5.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized UCHL1 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
Human Ubiquitin Carboxyl-Terminal Hydrolase L1 (UCH-L1) is an important enzyme involved in the ubiquitin-proteasome system, which regulates protein degradation and turnover in cells.
UCHL1 Function:
UCHL1 mainly removes ubiquitin molecules from proteins, thereby recycling ubiquitin and regulating protein stability. This action is important for controlling various cellular processes and maintaining cellular homeostasis and.
UCHL1 Structure
UCHL1 is characterized by a catalytic domain which facilitates its hydrolase activity, allowing it to cleave ubiquitin from substrates.
UCHL1 Role in Neurodegeneration
UCHL1 has been implicated in neurodegenerative diseases, such as Parkinson’s and Alzheimer's disease. Its expression levels and activity can affect neuronal survival and function.
UCH-L1 is also studied in the context of cancer. Altered levels of UCHL1 may affect on tumour progression and response to therapy.
UCHL1 Biomarker Potential
UCHL1 is being investigated as a potential biomarker for diseases, especially neurodegenerative disorders due to its involvement in various pathologies.
UCHL1 Research
Ongoing studies focus on understanding its role in various cellular contexts, its regulation, and its potential as a therapeutic target.
In conclusion, UCHL1 is a very important component of cellular regulation, with implications in health and disease.
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 :
PLA2G1B HumanDescription:
Secreted Phospholipase A2-IB Human Recombinant
Phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase, Group IB phospholipase A2, PLA2, PLA2A, PPLA2, sPLA2-IB,MGC119834, MGC119835, PLA2G1B.
Product # :
ENZ-325Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
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Description
Secreted Phospholipase A2-IB Human Recombinant is manufactured with N-terminal fusionf HisTag. PLA2G1B His-Tagged Fusion Protein is 16 kDa containing 126 amino acid residues of the human secreted phospholipase A2-IB and 16 additional amino acid residues - HisTag (underlined).
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Group IB secretory phospholipase A2 (sPLA2-IB) mediates cell proliferation, cell migration, hormone release and eicosanoid production via its receptor in peripheral tissues. In the CNS, high-affinity binding sites of sPLA2-IB have been documented. sPLA2-IB induced neuronal cell death in a concentrationdependent manner depending on PGD2 metabolites, especially Delta12-PGJ2 that might mediate sPLA2-IB-induced apoptosis. The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of lowmolecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.
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Synonyms
Phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase, Group IB phospholipase A2, PLA2, PLA2A, PPLA2, sPLA2-IB,MGC119834, MGC119835, PLA2G1B.
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Physical Appearance
Lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited. Product 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
MRGSHHHHHH GMASHMAVWQ FRKMIKCVIP GSDPFLEYNN YGCYCGLGGS GTPVDELDKC CQTHDNCYDQ AKKLDSCKFL LDNPYTHTYS YSCSGSAITC SSKNKECEAF ICNCDRNAAI CFSKAPYNKA HKNLDTKKYC QS.
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 :
PPP1CC Human, ActiveDescription:
Protein Phosphatase 1, Catalytic Subunit Gamma Human Recombinant, Active
Protein phosphatase 1 catalytic subunit gamma isozyme/isoform, Protein phosphatase 1C catalytic subunit, serine/threonine phosphatase 1 gamma, serine/threonine-protein phosphatase PP1-gamma catalytic subunit, PP1gamma, PPP1G, EC 3.1.3.16.
Product # :
ENZ-1042Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- biological activity
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Description
PPP1CC produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-323a.a.) and having a molecular mass of 39.1kDa.PPP1CC is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PPP1CC protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT and 50% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 700 units/mg, and is defined as the amount of enzyme that hydrolyzes 1.0 nmole of p-nitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37°C.
More Info
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Introduction
PPP1CC is vital for cell division and takes part in the regulation of protein synthesis, muscle contractility and glycogen metabolism. Additionally, PPP1CC has a role in long-term synaptic plasticity and regulation of ionic conductance, and has a significant role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II.
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Synonyms
Protein phosphatase 1 catalytic subunit gamma isozyme/isoform, Protein phosphatase 1C catalytic subunit, serine/threonine phosphatase 1 gamma, serine/threonine-protein phosphatase PP1-gamma catalytic subunit, PP1gamma, PPP1G, EC 3.1.3.16.
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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 MADLDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE KKKPNATRPV TPPRGMITKQ AKK.
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.