Search results
1000 results found for “Phosphatase and Tensin”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
PITPNA HumanDescription:
Phosphatidylinositol Transfer Protein Alpha Human Recombinant
Phosphatidylinositol transfer protein alpha isoform, PI-TP-alpha, PtdIns transfer protein alpha, PtdInsTP alpha, PITPNA, PITPN, VIB1A, MGC99649, PI-TPalpha.
Product # :
PRO-044Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
PITPNA Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 290 amino acids (1-270 a.a.) and having a molecular mass of 33.9kDa. The PITPNA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PITPNA solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol, 1mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Phosphatidylinositol transfer protein alpha (PITPNA) is found in the cytoplasm, where it catalyzes the transfer of phosphatidylinositol (PI) and phosphatidylcholine (PC) between membranes. PITPNA belongs to a family of lipid-binding proteins which transfer molecules of phosphatidylinositol or phosphatidylcholine between membrane surfaces. PITPNA is implicated in phospholipase C signaling and in the production of phosphatidylinositol 3, 4, 5-trisphosphate (PIP3) by phosphoinositide-3-kinase.
-
Synonyms
Phosphatidylinositol transfer protein alpha isoform, PI-TP-alpha, PtdIns transfer protein alpha, PtdInsTP alpha, PITPNA, PITPN, VIB1A, MGC99649, PI-TPalpha.
-
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
MGSSHHHHHH SSGLVPRGSH MVLLKEYRVI LPVSVDEYQV GQLYSVAEAS KNETGGGEGV EVLVNEPYEK DGEKGQYTHK IYHLQSKVPT FVRMLAPEGA LNIHEKAWNA YPYCRTVITN EYMKEDFLIK IETWHKPDLG TQENVHKLEP EAWKHVEAVY IDIADRSQVL SKDYKAEEDP AKFKSIKTGR GPLGPNWKQE LVNQKDCPYM CAYKLVTVKF KWWGLQNKVE NFIHKQERRL FTNFHRQLFC WLDKWVDLTM DDIRRMEEET KRQLDEMRQK DPVKGMTADD.
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 :
IVD HumanDescription:
Isovaleryl Coenzyme A Dehydrogenase Human Recombinant
FLJ12715, isovaleryl-CoA dehydrogenase mitochondrial, FLJ34849, EC 1.3.99.10, IVD, ACAD2.
Product # :
ENZ-490Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
IVD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 415 amino acids (33-426 a.a.) and having a molecular mass of 45.3 kDa. The IVD is fused to a 20 amino acid his tag at N-terminus and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The IVD protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
IVD is a mitochondrial matrix enzyme that is part of the cyl-CoA dehydrogenase family which catalyzes the third step in leucine catabolism. The genetic deficiency of IVD leads to a buildup of isovaleric acid, which is toxic to the central nervous system and results in isovaleric acidemia. IVD is a homotetrameric flavoenzyme which catalyzes the conversion of isovaleryl-CoA to 3-methylcrotonyl-CoA.
-
Synonyms
FLJ12715, isovaleryl-CoA dehydrogenase mitochondrial, FLJ34849, EC 1.3.99.10, IVD, ACAD2.
-
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
MGSSHHHHHH SSGLVPRGSH MHSLLPVDDA INGLSEEQRQ LRQTMAKFLQ EHLAPKAQEI DRSNEFKNLR EFWKQLGNLG VLGITAPVQY GGSGLGYLEH VLVMEEISRA SGAVGLSYGA HSNLCINQLV RNGNEAQKEK YLPKLISGEY IGALAMSEPN AGSDVVSMKL KAEKKGNHYI LNGNKFWITN GPDADVLIVY AKTDLAAVPA SRGITAFIVE KGMPGFSTSK KLDKLGMRGS NTCELIFEDC KIPAANILGH ENKGVYVLMS GLDLERLVLA GGPLGLMQAV LDHTIPYLHV REAFGQKIGH FQLMQGKMAD MYTRLMACRQ YVYNVAKACD EGHCTAKDCA GVILYSAECA TQVALDGIQC FGGNGYINDF PMGRFLRDAK LYEIGAGTSE VRRLVIGRAF NADFH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TNNI1 HumanDescription:
Troponin I Type 1 Human Recombinant
DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle ,Troponin I, slow-twitch isoform.
Product # :
PRO-1269Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TNNI1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (1-187 a.a.) and having a molecular mass of 23.8kDa.TNNI1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNNI1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Troponin I, (TNNI1) is a member of the troponin I family. Troponin complex has 3 subunits, TNNI1 known as the inhibitory Subunit which prevents the actin-myosin interactions and thus mediating striated muscle relaxation. TNNI1 combines with tropomyosin and regulates calcium sensitivity of striated muscles by structural modifications in actin-myosin complexes.
-
Synonyms
DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle ,Troponin I, slow-twitch isoform.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPEVERKPKI TASRKLLLKS LMLAKAKECW EQEHEEREAE KVRYLAERIP TLQTRGLSLS ALQDLCRELH AKVEVVDEER YDIEAKCLHN TREIKDLKLK VMDLRGKFKR PPLRRVRVSA DAMLRALLGS KHKVSMDLRA NLKSVKKEDT EKERPVEVGD WRKNVEAMSG MEGRKKMFDA AKSPTSQ
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 :
POU5F1 HumanDescription:
POU Class 5 Homeobox 1 Human Recombinant
POU domain class 5 transcription factor 1, Octamer-binding protein 3, Oct-3, Octamer-binding protein 4, Oct-4, Octamer-binding transcription factor 3, OTF-3, POU5F1, OCT3, OCT4, OTF3, OTF4, MGC22487.
Product # :
PRO-088Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
POU5F1 Human Recombinant produced in E. coli is a single polypeptide chain containing 285 amino acids (1-265) and having a molecular mass of 32.2 kDa.POU5F1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The POU5F1 solution 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
-
Introduction
POU5F1 is a homeodomain transcription factor of the POU family, expressed in embryonic stem (ES) cells and embryonic carcinoma (EC) cells.POU5F1 is significantly involved in the signaling pathway for maintaining self-renewal and pluripotency of ES cells. POU5F1 has 2 distinct DNA binding domains which independently bind half-sites of the canonical octamer motif. This flexibility allows POU5F1 to bind with distinct DNA motifs by forming heterodimers with other transcription factors or by forming homodimers in several conformations. Human POU5F1 contains a 75aa POU specific (POUS) domain and a 60aa POU-Homeo-(POUH) domain connected by a linker region. The Human POU5F1 specifically interacts with Octamer motif ATGCAAAT. In addition, 2 proline-rich domains in the N-terminal and C-terminal regions are vital for POU5F1 transactivation. POU5F1 regulates a number of target genes and has been shown to work jointly with other transcription factors including Sox2 as well as Nanog to sustain stem cell potency and self-renewal.
-
Synonyms
POU domain class 5 transcription factor 1, Octamer-binding protein 3, Oct-3, Octamer-binding protein 4, Oct-4, Octamer-binding transcription factor 3, OTF-3, POU5F1, OCT3, OCT4, OTF3, OTF4, MGC22487.
-
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
MGSSHHHHHH SSGLVPRGSH MHFYRLFLGA TRRFLNPEWK GEIDNWCVYV LTSLLPFKIQ SQDIKALQKE LEQFAKLLKQ KRITLGYTQA DVGLTLGVLF GKVFSQTTIC RFEALQLSFK NMCKLRPLLQ KWVEEADNNE NLQEICKAET LVQARKRKRT SIENRVRGNL ENLFLQCPKP TLQQISHIAQ QLGLEKDVVR VWFCNRRQKG KRSSSDYAQR EDFEAAGSPF SGGPVSFPLA PGPHFGTPGY GSPHFTALYS SVPFPEGEAF PPVSVTTLGS PMHSN.
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 :
PPIF HumanDescription:
Cyclophilin-F Human Recombinant
Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.
Product # :
ENZ-385Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
PPIF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 198 amino acids (30-207) and having a molecular mass of 21 kDa. The PPIF is fused to a 20 amino acid His tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PPIF solution containing 20mM Tris-HCl pH-7.5, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 250 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.More Info
-
Introduction
PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.
-
Synonyms
Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.
-
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
MGSSHHHHHH SSGLVPRGSH CSKGSGDPSS SSSSGNPLVY LDVDANGKPL GRVVLELKAD VVPKTAENFR ALCTGEKGFG YKGSTFHRVI PSFMCQAGDF TNHNGTGGKS IYGSRFPDEN FTLKHVGPGV LSMANAGPNT NGSQFFICTI KTDWLDGKHV VFGHVKEGMD VVKKIESFGS KSGRTSKKIV ITDCGQLS.
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 :
TPX E.coliDescription:
Thiol Peroxidase E.Coli Recombinant
Thiol peroxidase, Scavengase P20, tpx, yzzJ, b1324, JW1317.
Product # :
ENZ-135Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TPX produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-168 a.a.) and having a molecular mass of 19.9kDa.TPX is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Recombinant TPX solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Lipid hydroperoxide peroxidase (TPX) belongs to the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. TPX has an imperative role in thioredoxin peroxidase activity.
-
Synonyms
Thiol peroxidase, Scavengase P20, tpx, yzzJ, b1324, JW1317.
-
Physical Appearance
Sterile filtered liquid formulation 1 mg/ml.
-
Stability
TPX E.Coli Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSQTVHFQGN PVTVANSIPQ AGSKAQTFTL VAKDLSDVTL GQFAGKRKVL NIFPSIDTGV CAASVRKFNQ LATEIDNTVV LCISADLPFA QSRFCGAEGL NNVITLSTFR NAEFLQAYGV AIADGPLKGL AARAVVVIDE NDNVIFSQLV DEITTEPDYE AALAVLKA.
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 :
TSFM HumanDescription:
Ts Translation Elongation Factor Mitochondrial Human Recombinant
Elongation factor Ts, mitochondrial, Ts Translation Elongation Factor Mitochondrial, TSFM, EF-Ts, EF-TsMt, COXPD3.
Product # :
PRO-1971Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TSFM Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (46-346 a.a) and having a molecular mass of 32.9kDa.TSFM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TSFM protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
TSFM is a mitochondrial translation elongation factor which is linked with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. TSFM stays bound to the aminoacyl-tRNA.EF-Tu.GTP complex until the GTP hydrolysis stage on the ribosome. Mutations in TSFM are related with combined oxidative phosphorylation deficiency-3 syndrome.
-
Synonyms
Elongation factor Ts, mitochondrial, Ts Translation Elongation Factor Mitochondrial, TSFM, EF-Ts, EF-TsMt, COXPD3.
-
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
MSKELLMKLR RKTGYSFVNC KKALETCGGD LKQAEIWLHK EAQKEGWSKA AKLQGRKTKE GLIGLLQEGN TTVLVEVNCE TDFVSRNLKF QLLVQQVALG TMMHCQTLKD QPSAYSKVQW LTPVNLALWE AEAGGSLEGF LNSSELSGLP AGPDREGSLK DQLALAIGKL GENMILKRAA WVKVPSGFYV GSYVHGAMQS PSLHKLVLGK YGALVICETS EQKTNLEDVG RRLGQHVVGM APLSVGSLDD EPGGEAETKM LSQPYLLDPS ITLGQYVQPQ GVSVVDFVRF ECGEGEEAAE TE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TTC32 HumanDescription:
Tetratricopeptide Repeat Domain 32 Human Recombinant
Tetratricopeptide Repeat Domain 32, Tetratricopeptide Repeat Protein 32, TPR Repeat Protein 32.
Product # :
PRO-1246Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TTC32 Human Recombinant produced in E. coli is a single polypeptide chain containing 174 amino acids (1-151) and having a molecular mass of 19.7 kDa. TTC32 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TTC32 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 2mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
TTC32 contains 3 TPR repeats. The tetratricopeptide repeat (TPR) is a structural motif. TPR is observed in organized 3–16 motifs, which form scaffolds to mediate protein–protein interactions and frequently the assembly of multiprotein complexes. TPR-containing proteins include the anaphase-promoting complex subunits cdc16, cdc23 and cdc27, the NADPH oxidase subunit p67-phox, hsp90-binding immunophilins, transcription factors, the major receptor for peroxisomal matrix protein import PEX5, the PKR protein kinase inhibitor and mitochondrial import proteins.
-
Synonyms
Tetratricopeptide Repeat Domain 32, Tetratricopeptide Repeat Protein 32, TPR Repeat Protein 32.
-
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
MGSSHHHHHH SSGLVPRGSH MGSMEGQRQE SHATLTLAQA HFNNGEYAEA EALYSAYIRR CACAASSDES PGSKCSPEDL ATAYNNRGQI KYFRVDFYEA MDDYTSAIEV QPNFEVPYYN RGLILYRLGY FDDALEDFKK VLDLNPGFQD ATLSLKQTIL DKEEKQRRNV AKNY.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TYW5 HumanDescription:
tRNA-yW Synthesizing Protein 5 Human Recombinant
tRNA wybutosine-synthesizing protein 5, hTYW5, TYW5, C2orf60.
Product # :
PRO-1315Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TYW5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 338 amino acids (1-315 a.a.) and having a molecular mass of 38.9kDa.TYW5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TYW5 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
tRNA wybutosine-synthesizing protein 5 (TYW5) functions as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position closest to the anticodon of eukaryotic phenylalanine tRNA. TYW5 catalyzes the hydroxylation of 7-(a-amino-a-carboxypropyl)wyosine (yW-72) into undermodified hydroxywybutosine (OHyW). OHyW is a derivative of wybutosine observed in higher eukaryotes.
-
Synonyms
tRNA wybutosine-synthesizing protein 5, hTYW5, TYW5, C2orf60.
-
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
MGSSHHHHHH SSGLVPRGSH MGSMAGQHLP VPRLEGVSRE QFMQHLYPQR KPLVLEGIDL GPCTSKWTVD YLSQVGGKKE VKIHVAAVAQ MDFISKNFVY RTLPFDQLVQ RAAEEKHKEF FVSEDEKYYL RSLGEDPRKD VADIRKQFPL LKGDIKFPEF FKEEQFFSSV FRISSPGLQL WTHYDVMDNL LIQVTGKKRV VLFSPRDAQY LYLKGTKSEV LNIDNPDLAK YPLFSKARRY ECSLEAGDVL FIPALWFHNV ISEEFGVGVN IFWKHLPSEC YDKTDTYGNK DPTAASRAAQ ILDRALKTLA ELPEEYRDFY ARRMVLHIQD KAYSKNSE.
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 :
PSMA2 HumanDescription:
Proteasome Subunit Alpha Type 2 Human Recombinant
Proteasome subunit alpha type-2, Macropain subunit C3, Multicatalytic endopeptidase complex subunit C3, Proteasome component C3, PSMA2, HC3, PSC3, MU, PSC2.
Product # :
ENZ-175Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
PSMA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 254 amino acids (1-234 a.a.) and having a molecular mass of 28kDa.PSMA2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PSMA2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.1M NaCl, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Proteasome subunit alpha type-2 (PSMA2) 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. PSMA2 is a 20S core alpha subunit of proteasome belonging to the peptidase T1A family. PSMA2 functions as a docking domain for the regulatory particles and exterior gates blocking unregulated access to the inner cavity.
-
Synonyms
Proteasome subunit alpha type-2, Macropain subunit C3, Multicatalytic endopeptidase complex subunit C3, Proteasome component C3, PSMA2, HC3, PSC3, MU, PSC2.
-
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
MGSSHHHHHH SSGLVPRGSH MAERGYSFSL TTFSPSGKLV QIEYALAAVA GGAPSVGIKA ANGVVLATEK KQKSILYDER SVHKVEPITK HIGLVYSGMG PDYRVLVHRA RKLAQQYYLV YQEPIPTAQL VQRVASVMQE YTQSGGVRPF GVSLLICGWN EGRPYLFQSD PSGAYFAWKA TAMGKNYVNG KTFLEKRYNE DLELEDAIHT AILTLKESFE GQMTEDNIEV GICNEAGFRR LTPTEVKDYL AAIA.
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 :
GSTA1 HumanDescription:
Glutathione S-Transferase Alpha-1 Human Recombinant
GST2, GSTA1-1, GTH1, GSTA-1, GSTAI, GSTA-I, EC 2.5.1.18, Glutathione S-transferase A1, GST HA subunit 1, GST-epsilon, GST class-alpha member 1, GSTA1, MGC131939.
Product # :
ENZ-469Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
GSTA1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 222 amino acids (1-222 a.a.) and having a molecular mass of 25.6 kDa. The GSTA1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GSTA1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is 35,000 pmol/min/ug, and is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25°C.
More Info
-
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.
-
Synonyms
GST2, GSTA1-1, GTH1, GSTA-1, GSTAI, GSTA-I, EC 2.5.1.18, Glutathione S-transferase A1, GST HA subunit 1, GST-epsilon, GST class-alpha member 1, GSTA1, MGC131939.
-
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
MAEKPKLHYF NARGRMESTR WLLAAAGVEF EEKFIKSAED LDKLRNDGYL MFQQVPMVEI DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYIEGIA DLGEMILLLP VCPPEEKDAK LALIKEKIKN RYFPAFEKVL KSHGQDYLVG NKLSRADIHL VELLYYVEEL DSSLISSFPL LKALKTRISN LPTVKKFLQP GSPRKPPMDE KSLEEARKIF RF.
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 :
GULP1 HumanDescription:
GULP1 Human Recombinant
GULP, Engulfment Adaptor PTB Domain Containing 1, PTB Domain Adapter Protein CED-6, Cell Death Protein 6 Homolog, CED6, GULP, PTB Domain Adaptor Protein CED-6 Engulfment Adapter Protein, Protein GULP, CED-6.
Product # :
PRO-1398Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GULP1 Human Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (1-304a.a) and having a molecular mass of 36.9kDa.GULP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GULP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
PTB domain-containing engulfment adapter protein 1 (GULP1) is an evolutionarily conserved adaptor protein essential for efficient phagocytosis of apoptotic cells by phagocytes. Furthermore, GULP1 helps modulate cellular glycosphingolipid and cholesterol transport. In addition, GULP1 may have a role in the internalization and endosomal trafficking of various LRP1 ligands, such as PSAP. Increased cytoplasmic levels of GULP1 are linked with increases in cellular levels of GTP-bound ARF6.
-
Synonyms
GULP, Engulfment Adaptor PTB Domain Containing 1, PTB Domain Adapter Protein CED-6, Cell Death Protein 6 Homolog, CED6, GULP, PTB Domain Adaptor Protein CED-6 Engulfment Adapter Protein, Protein GULP, CED-6.
-
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
MGSSHHHHHH SSGLVPRGSH MGSMNRAFSR KKDKTWMHTP EALSKHFIPY NAKFLGSTEV EQPKGTEVVR DAVRKLKFAR HIKKSEGQKI PKVELQISIY GVKILEPKTK EVQHNCQLHR ISFCADDKTD KRIFTFICKD SESNKHLCYV FDSEKCAEEI TLTIGQAFDL AYRKFLESGG KDVETRKQIA GLQKRIQDLE TENMELKNKV QDLENQLRIT QVSAPPAGSM TPKSPSTDIF DMIPFSPISH QSSMPTRNGT QPPPVPSRST EIKRDLFGAE PFDPFNCGAA DFPPDIQSKL DEMQEGFKMG LTLEGTVFCL DPLDSRC.
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 :
RCHY1 HumanDescription:
Ring Finger & CHY Zinc Finger Domain Containing 1 Human Recombinant
ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.
Product # :
PRO-1536Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
RCHY1 Human Recombinant produced in E. coli is a single polypeptide chain containing 284 amino acids (1-261) and having a molecular mass of 32.5kDa. RCHY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RCHY1 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
-
Introduction
Ring Finger & CHY Zinc Finger Domain Containing 1 (RCHY1) acts as an ubiquitin ligase. RCHY1 mediates E3-dependent ubiquitination and proteasomal degradation of target proteins which among them are TP53, HDAC1 and CDKN1B, consequently regulating their levels and cell cycle progression. RCHY1 is also increases AR transcription factor activity.
-
Synonyms
ARNIP, CHIMP, hARNIP, PIRH2, PIRH2E, PIRH2F, PRO1996, RNF199, ZNF363, RING finger and CHY zinc finger domain-containing protein 1, Androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, E3 ubiquitin-protein ligase Pirh2, RING finger protein 199, Zinc finger protein 363, p53-induced RING-H2 protein, hPirh2, RCHY1.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAATARE DGASGQERGQ RGCEHYDRGC LLKAPCCDKL YTCRLCHDNN EDHQLDRFKV KEVQCINCEK IQHAQQTCEE CSTLFGEYYC DICHLFDKDK KQYHCENCGI CRIGPKEDFF HCLKCNLCLA MNLQGRHKCI ENVSRQNCPI CLEDIHTSRV VAHVLPCGHL LHRTCYEEML KEGYRCPLCM HSALDMTRYW RQLDDEVAQT PMPSEYQNMT VDILCNDCNG RSTVQFHILG MKCKICESYN TAQAGGRRIS LDQQ.
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 :
REXO1 HumanDescription:
RNA Exonuclease 1 Human Recombinant
RNA exonuclease 1 homolog, Elongin-A-binding protein 1, EloA-BP1, Transcription elongation factor B polypeptide 3-binding protein 1, REXO1, ELOABP1, KIAA1138, TCEB3BP1.
Product # :
ENZ-767Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
REXO1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (1060-1221a.a) and having a molecular mass of 22.3kDa. REXO1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The REXO1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
REXO1 is an exonuclease domain-containing protein which binds to Elongin. The Elongin complex stimulates the rate of transcription elongation by RNA polymerase II by suppressing the transient pausing of the polymerase at many sites along the DNA template. REXO1 is composed of 1221 amino acids and its mRNA is ubiquitously expressed. REXO1 is a putative stem cell marker and is highly expressed in embryonic and adult stem cells.
-
Synonyms
RNA exonuclease 1 homolog, Elongin-A-binding protein 1, EloA-BP1, Transcription elongation factor B polypeptide 3-binding protein 1, REXO1, ELOABP1, KIAA1138, TCEB3BP1.
-
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSIYAL DCEMSYTTYG LELTRVTVVD TDVHVVYDTF VKPDNEIVDY NTRFSGVTEA DLADTSVTLR DVQAVLLSMF SADTILIGHS LESDLLALKV IHSTVVDTSV LFPHRLGLPY KRSLRNLMAD YLRQIIQDNV DGHSSSEDAG ACMHLVIWKV REDAKTKR.
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 :
RPP30 HumanDescription:
Ribonuclease P/MRP 30kDa Subunit Human Recombinant
Ribonuclease P protein subunit p30, RNaseP protein p30, RNase P subunit 2, RPP30, RNASEP2, TSG15, FLJ38491, RP11-320F15.1.
Product # :
ENZ-040Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
RPP30 Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 291 amino acids (1-268 a.a.) and having a molecular mass of 31.8kDa. The RPP30 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RPP30 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 5mM DTT, 200mM NaCl and 1mM EDTA.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Ribonuclease P protein subunit p30 (RPP30) is a member of the eukaryotic/archaeal RNase P protein component 3 family. RPP30 is component of ribonuclease P, which is a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Ribonuclease P (RNase P) is small nuclear ribonucleoprotein (snRNPs) which acts on RNA substrates in vitro. In addition, RNase P which accumulate in the nucleolus, have a similar RNA component and several protein subunits in common.
-
Synonyms
Ribonuclease P protein subunit p30, RNaseP protein p30, RNase P subunit 2, RPP30, RNASEP2, TSG15, FLJ38491, RP11-320F15.1.
-
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
MGSSHHHHHH SSGLVPRGSH MGSMAVFADL DLRAGSDLKA LRGLVETAAH LGYSVVAINH IVDFKEKKQE IEKPVAVSEL FTTLPIVQGK SRPIKILTRL TIIVSDPSHC NVLRATSSRA RLYDVVAVFP KTEKLFHIAC THLDVDLVCI TVTEKLPFYF KRPPINVAID RGLAFELVYS PAIKDSTMRR YTISSALNLM QICKGKNVII SSAAERPLEI RGPYDVANLG LLFGLSESDA KAAVSTNCRA ALLHGETRKT AFGIISTVKK PRPSEGDEDC LPASKKAKCE G.
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 :
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
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
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
-
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.
-
Synonyms
AChE, ACEE, ACES_HUMAN, Acetylcholinesterase, ACHE, ARACHE, N-ACHE, VT, Acetylcholinesterase isoform E4-E6
-
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
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.
- View Data Sheet
Name :
MINA HumanDescription:
MYC Induced Nuclear Antigen Human Recombinant
MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.
Product # :
PRO-2078Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
MINA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 485 amino acids (1-465 a.a) and having a molecular mass of 54.9kDa. MINA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MINA 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
-
Introduction
MYC Induced Nuclear Antigen, also known as MINA is an oxygenase which can function both as a histone lysine demethylase and a ribosomal histidine hydroxylase. MINA is involved in the demethylation of trimethylated Lys-9 on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. MINA also catalyzes the hydroxylation of 60S ribosomal protein L27a on His-39. In addition, MINA plays a significant role in cell growth and survival. MINA is implicated in ribosome biogenesis, probably in the duration of the assembly process of pre-ribosomal particles.
-
Synonyms
MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPKKAKPTGS GKEEGPAPCK QMKLEAAGGP SALNFDSPSS LFESLISPIK TETFFKEFWE QKPLLIQRDD PALATYYGSL FKLTDLKSLC SRGMYYGRDV NVCRCVNGKK KVLNKDGKAH FLQLRKDFDQ KRATIQFHQP QRFKDELWRI QEKLECYFGS LVGSNVYITP AGSQGLPPHY DDVEVFILQL EGEKHWRLYH PTVPLAREYS VEAEERIGRP VHEFMLKPGD LLYFPRGTIH QADTPAGLAH STHVTISTYQ NNSWGDFLLD TISGLVFDTA KEDVELRTGI PRQLLLQVES TTVATRRLSG FLRTLADRLE GTKELLSSDM KKDFIMHRLP PYSAGDGAEL STPGGKLPRL DSVVRLQFKD HIVLTVLPDQ DQSDETQEKM VYIYHSLKNS RETHMMGNEE ETEFHGLRFP LSHLDALKQI WNSPAISVKD LKLTTDEEKE SLVLSLWTEC LIQVV.
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 :
ADAM10 Human, Sf9Description:
A Disintegrin and Metalloproteinase Domain 10 Human Recombinant, Sf9
Kuz, AD10, MADM, CD156c, HsT18717, ADAM metallopeptidase domain 10, A disintegrin and metalloproteinase domain 10, Mammalian disintegrin-metalloprotease, Kuzbanian protein homolog, CDw156, ADAM 10, ADAM10.
Product # :
PRO-2359Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ADAM10 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 467 amino acids (214-672 aa) and having a molecular mass of 51.6kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions).ADAM10 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ADAM10 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
ADAM10 is part of the ADAM family which are cell surface proteins with a distinctive structure possessing both potential adhesion and protease domains. ADAM10 cleaves many proteins including TNF-alpha and E-cadherin. ADAM10 cleaves the membrane-bound precursor of tnf-alpha at 76- ala-|-val-77 to its mature soluble form. ADAM10 is in charge for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-a2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein ADAM10 is involved in the normal cleavage of the cellular prion protein. ADAM10 is involved in the cleavage of the adhesion molecule l1 at the cell surface and in the release of membrane vesicles, suggesting a vesicle-based protease activity. ADAM10 controls the proteolytic processing of notch and mediates lateral inhibition during neurogenesis.
-
Synonyms
Kuz, AD10, MADM, CD156c, HsT18717, ADAM metallopeptidase domain 10, A disintegrin and metalloproteinase domain 10, Mammalian disintegrin-metalloprotease, Kuzbanian protein homolog, CDw156, ADAM 10, ADAM10.
-
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
TTSAEKNTCQ LYIQTDHLFF KYYGTREAVI AQISSHVKAI DTIYQTTDFS GIRNISFMVK RIRINTTADE KDPTNPFRFP NIGVEKFLEL NSEQNHDDYC LAYVFTDRDF DDGVLGLAWV GAPSGSSGGI CEKSKLYSDG KKKSLNTGII TVQNYGSHVP PKVSHITFAH EVGHNFGSPH DSGTECTPGE SKNLGQKENG NYIMYARATS GDKLNNNKFS LCSIRNISQV LEKKRNNCFV ESGQPICGNG MVEQGEECDC GYSDQCKDEC CFDANQPEGR KCKLKPGKQC SPSQGPCCTA QCAFKSKSEK CRDDSDCARE GICNGFTALC PASDPKPNFT DCNRHTQVCI NGQCAGSICE KYGLEECTCA SSDGKDDKEL CHVCCMKKMD PSTCASTGSV QWSRHFSGRT ITLQPGSPCN DFRGYCDVFM RCRLVDADGP LARLKKAIFS PELYENIAEL EHHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
NEIL1 HumanDescription:
Nei Endonuclease VIII-Like 1 Human Recombinant
Endonuclease 8-like 1, DNA glycosylase/AP lyase Neil1, DNA-(apurinic or apyrimidinic site) lyase Neil1, Endonuclease VIII-like 1, FPG1, Nei homolog 1, NEH1, Nei-like protein 1, NEIL1, NEI1, hFPG1.
Product # :
ENZ-220Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NEIL1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (1-390) and having a molecular mass of 45.8kDa.NEIL1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NEIL1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
NEIL1 is a member of a class of DNA glycosylases homologous to the bacterial Fpg/Nei family. These glycosylases initiate the first step in base excision repair by cleaving bases damaged by reactive oxygen species and introducing a DNA strand break via the associated lyase reaction. NEIL1 participates in the DNA repair pathway by initiating base excision repair by removing damaged bases, primarily oxidized pyrimidines.
-
Synonyms
Endonuclease 8-like 1, DNA glycosylase/AP lyase Neil1, DNA-(apurinic or apyrimidinic site) lyase Neil1, Endonuclease VIII-like 1, FPG1, Nei homolog 1, NEH1, Nei-like protein 1, NEIL1, NEI1, hFPG1.
-
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
MGSSHHHHHH SSGLVPRGSH MPEGPELHLA SQFVNEACRA LVFGGCVEKS SVSRNPEVPF ESSAYRISAS ARGKELRLIL SPLPGAQPQQ EPLALVFRFG MSGSFQLVPR EELPRHAHLR FYTAPPGPRL ALCFVDIRRF GRWDLGGKWQ PGRGPCVLQE YQQFRENVLR NLADKAFDRP ICEALLDQRF FNGIGNYLRA EILYRLKIPP FEKARSVLEA LQQHRPSPEL TLSQKIRTKL QNPDLLELCH SVPKEVVQLG GKGYGSESGE EDFAAFRAWL RCYGMPGMSS LQDRHGRTIW FQGDPGPLAP KGRKSRKKKS KATQLSPEDR VEDALPPSKA PSRTRRAKRD LPKRTATQRP EGTSLQQDPE APTVPKKGRR KGRQAASGHC RPRKVKADIP SLEPEGTSAS.
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 :
GATC HumanDescription:
Glutamyl-TRNA Amidotransferase, Subunit C Human Recombinant
Glutamyl-TRNA(Gln) Amidotransferase Subunit C, Glu-AdT Subunit C, 15E1.2, Glutamyl-TRNA(Gln) Amidotransferase Subunit C Homolog (Bacterial), Glutamyl-TRNA(Gln) Amidotransferase Subunit C Mitochondrial, Glutamyl-TRNA(Gln) Amidotransferase Subunit C Homolog, EC 6.3.5, Protein 15E1.2.
Product # :
ENZ-722Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GATC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 159 amino acids (1-136 a.a) and having a molecular mass of 17.5kDa (Molecular size on SDS-PAGE will appear higher).GATC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GATC protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Glutamyl-TRNA Amidotransferase, Subunit C also known as GATC allows the formation of properly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction occurs in the attendance of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). In addition, GATC is subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A (QRSL1), B (PET112) and C (GATC) subunits.
-
Synonyms
Glutamyl-TRNA(Gln) Amidotransferase Subunit C, Glu-AdT Subunit C, 15E1.2, Glutamyl-TRNA(Gln) Amidotransferase Subunit C Homolog (Bacterial), Glutamyl-TRNA(Gln) Amidotransferase Subunit C Mitochondrial, Glutamyl-TRNA(Gln) Amidotransferase Subunit C Homolog, EC 6.3.5, Protein 15E1.2.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMWSRLVW LGLRAPLGGR QGFTSKADPQ GSGRITAAVI EHLERLALVD FGSREAVARL EKAIAFADRL RAVDTDGVEP MESVLEDRCL YLRSDNVVEG NCADELLQNS HRVVEEYFVA PPGNISLPKL DEQEPFPHS
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 :
GLO1 MouseDescription:
Glyoxalase-I Mouse Recombinant
Lactoylglutathione lyase, Aldoketomutase, Glyoxalase I, Glx I, Ketone-aldehyde mutase, Methylglyoxalase, S-D-lactoylglutathione methylglyoxal lyase.
Product # :
ENZ-953Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
GLO1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 192 amino acids (1-184a.a.) and having a molecular mass of 21.8kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). GLO1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
GLO1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 210 units/mg, and is defined as the amount of enzyme that will form 1.0 µmol of S-lactoylglutathione from methylglyoxal and reduced glutathione per minute at pH 6.5 at 25C.More Info
-
Introduction
GLO1 is involved in the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation and reduced glutatione. GLO1 is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere. GLO1 enzyme is ubundantly expressed and present in numerous tumor cell lines, in which its concentration is often upregulated ubiquitisly. GLO1 is a major susceptible gene for autism in an ethnic Chinese population from Taiwan. GLO1 might be involved in the pathophysiology of mood disorders. GLO1 plays a role in the pathophysiology of mood disorders. Overexpression of GLO1 is associated with kidney tumor.
-
Synonyms
Lactoylglutathione lyase, Aldoketomutase, Glyoxalase I, Glx I, Ketone-aldehyde mutase, Methylglyoxalase, S-D-lactoylglutathione methylglyoxal lyase.
-
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
MAEPQPASSG LTDETAFSCC SDPDPSTKDF LLQQTMLRIK DPKKSLDFYT RVLGLTLLQK LDFPAMKFSL YFLAYEDKND IPKDKSEKTA WTFSRKATLE LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKI ATIILEHHHH 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.
- View Data Sheet
Name :
PDIA3 MouseDescription:
Protein Disulfide Isomerase A3 Mouse Recombinant
ERp57, ERp60, ERp61, GRP57, GRP58, HsT17083, P58, PI-PLC, ER60, Protein disulfide-isomerase A3, Disulfide isomerase ER-60, Endoplasmic reticulum resident protein 60, ER protein 60, 58 kDa microsomal protein, Endoplasmic reticulum resident protein 57, ER protein 57, 58 kDa glucose-regulated protein, PDIA3.
Product # :
ENZ-1051Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
PDIA3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 505 amino acids (25-505 a.a) and having a molecular mass of 56.8kDa. PDIA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PDIA3 protein solution (1mg/ml) containing 20 mM Tris-HCl buffer (pH8.0), 1mM DTT, 0.1M NaCl and 10% glycerol .
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >15 A650/cm/min/mg,obtained by measuring the increase of insulin precipitation in absorbance at 650nm resulting from the reduction of insulin.
More Info
-
Introduction
PDIA3 is an enzyme that belongs to the endoplasmic reticulum and interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. PDIA3 has protein disulfide isomerase activity. Complexes of lectins and PDIA3 mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates. PDIA3 is expressed in the lumbar spinal cord from rats submitted to peripheral lesion during neonatal period. PDIA3 interacts with thiazide-sensitive sodium-chloride cotransporter in the kidney and is induced by glucose deprivation. PDIA3 is part of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which is important for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface.
-
Synonyms
ERp57, ERp60, ERp61, GRP57, GRP58, HsT17083, P58, PI-PLC, ER60, Protein disulfide-isomerase A3, Disulfide isomerase ER-60, Endoplasmic reticulum resident protein 60, ER protein 60, 58 kDa microsomal protein, Endoplasmic reticulum resident protein 57, ER protein 57, 58 kDa glucose-regulated protein, PDIA3.
-
Physical Appearance
Sterile filtered colourless 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
MGSSHHHHHH SSGLVPRGSH MGSMSDVLEL TDENFESRVS DTGSAGLMLV EFFAPWCGHC KRLAPEYEAA ATRLKGIVPL AKVDCTANTN TCNKYGVSGY PTLKIFRDGE EAGAYDGPRT ADGIVSHLKK QAGPASVPLR TEEEFKKFIS DKDASVVGFF RDLFSDGHSE FLKAASNLRD NYRFAHTNIE SLVKEYDDNG EGITIFRPLH LANKFEDKTV AYTEKKMTSG KIKKFIQDSI FGLCPHMTED NKDLIQGKDL LTAYYDVDYE KNAKGSNYWR NRVMMVAKKF LDAGHKLNFA VASRKTFSHE LSDFGLESTT GEVPVVAIRT AKGEKFVMQE EFSRDGKALE QFLQEYFDGN LKRYLKSEPI PESNEGPVKV VVAENFDDIV NEEDKDVLIE FYAPWCGHCK NLEPKYKELG EKLSKDPNIV IAKMDATAND VPSPYEVKGF PTIYFSPANK KLTPKKYEGG RELNDFISYL QREATNPPII QEEKPKKKKK AQEDL.
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 :
FGF 2 Human, sf9Description:
Fibroblast Growth Factor-Basic Human Recombinant, Sf9
Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.
Product # :
CYT-365Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in Sf9 insect cells is a single, glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of 17353 Dalton.The FGF-basic is purified by proprietary chromatographic techniques.
Source
Baculovirus.
Formulation
The sterile protein solution (0.5mg/ml) contains 20mM Tris pH=7.9, 100mM KCl, 1mM DTT and 20% glycerol.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.More Info
-
Introduction
Basic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
-
Synonyms
Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.
-
Physical Appearance
Sterile Filtered liquid formulation.
-
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
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ala-Gly-Ser-Ile.
-
Background
What is the molecular weight/Mw of FGF 2 Protein?
FGF 2 Protein has a total Mw of 17.3kDa.
What is the source or expression system of FGF 2 Protein?
Baculovirus.
What is the Purity of FGF 2 Protein?
FGF 2 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF 2 Protein?
The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.
What is the amino acid sequence of FGF 2 Protein?
FGF 2 Protein is composed from155 amino acids.
What applications can FGF 2 Protein be used in?
FGF 2 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF 2 Protein?
The endotoxin level is minimal, FGF 2 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ING2 HumanDescription:
Inhibitor of Growth Family, Member 2 Human Recombinant
Inhibitor Of Growth Family Member 2, ING1L, Inhibitor Of Growth 1-Like Protein, P33ING2, ING1Lp, P32, Inhibitor Of Growth Family Member 1-Like, Inhibitor Of Growth Protein 2, ING2.
Product # :
PRO-1739Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ING2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (1-280 a.a) and having a molecular mass of 35.2kDa.ING2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ING2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Inhibitor of Growth Family, Member 2 (ING2) belongs to the inhibitor of growth (ING) family. ING family members associate with and modulate the activity of histone acetyltransferase (HAT) and histone deacetylase (HDAC) complexes and serve in DNA repair and apoptosis. ING2 appears to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, most likely by enhancing acetylation of p53/TP53. ING2 is a component of an mSin3A-like corepressor complex, which is probably involved in deacetylation of nucleosomal histones. ING2 activity is modulated by binding to phosphoinositides (PtdInsPs).
-
Synonyms
Inhibitor Of Growth Family Member 2, ING1L, Inhibitor Of Growth 1-Like Protein, P33ING2, ING1Lp, P32, Inhibitor Of Growth Family Member 1-Like, Inhibitor Of Growth Protein 2, ING2.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMLGQQQQ QLYSSAALLT GERSRLLTCY VQDYLECVES LPHDMQRNVS VLRELDNKYQ ETLKEIDDVY EKYKKEDDLN QKKRLQQLLQ RALINSQELG DEKIQIVTQM LELVENRARQ MELHSQCFQD PAESERASDK AKMDSSQPER SSRRPRRQRT SESRDLCHMA NGIEDCDDQP PKEKKSKSAK KKKRSKAKQE REASPVEFAI DPNEPTYCLC NQVSYGEMIG CDNEQCPIEW FHFSCVSLTY KPKGKWYCPK CRGDNEKTMD KSTEKTKKDR RSR.
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.