Search results
1000 results found for “sulfatase”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
DUSP23 Human, ActiveDescription:
Dual Specificity Phosphatase 23 Human Recombinant, Active
Dual specificity protein phosphatase 23, Low molecular mass dual specificity phosphatase 3, LDP-3, VH1-like phosphatase Z, DUSP23, LDP3, VHZ, VH1-Like Member Z, EC 3.1.3.16, EC 3.1.3.48, DUSP25, MOSP, LDP3, Dual Specificity Phosphatase 23, VH1-Like Phosphatase Z, LDP-3, VHZ, Low-Molecular-Mass Dual-Specificity Phosphatase 3, Low Molecular Mass Dual Specificity Phosphatase 3, Dual Specificity Protein, Phosphatase 23, Testicular Tissue Protein Li 59.
Product # :
ENZ-1043Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
DUSP23 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (1-150 a.a) and having a molecular mass of 18.8kDa.DUSP23 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DUSP23 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 200 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.
Citations
More Info
-
Introduction
DUSP23 is a member of the protein-tyrosine phosphatase family. DUSP23 is a protein phosphatase which facilitates dephosphorylation of phosphorylated proteins on Tyr and Ser/Thr residues. In vitro, DUSP23 dephosphorylate p44-ERK1 (MAPK3) but not p54 SAPK-beta (MAPK10). In addition, DUSP23 enhances activation of JNK and p38(MAPK14).
-
Synonyms
Dual specificity protein phosphatase 23, Low molecular mass dual specificity phosphatase 3, LDP-3, VH1-like phosphatase Z, DUSP23, LDP3, VHZ, VH1-Like Member Z, EC 3.1.3.16, EC 3.1.3.48, DUSP25, MOSP, LDP3, Dual Specificity Phosphatase 23, VH1-Like Phosphatase Z, LDP-3, VHZ, Low-Molecular-Mass Dual-Specificity Phosphatase 3, Low Molecular Mass Dual Specificity Phosphatase 3, Dual Specificity Protein, Phosphatase 23, Testicular Tissue Protein Li 59.
-
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 MGVQPPNFSW VLPGRLAGLA LPRLPAHYQF LLDLGVRHLV SLTERGPPHS DSCPGLTLHR LRIPDFCPPA PDQIDRFVQI VDEANARGEA VGVHCALGFG RTGTMLACYL VKERGLAAGD AIAEIRRLRP GSIETYEQEK AVFQFYQRTK.
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 :
melA E. coliDescription:
Alpha-Galactosidase E.coli Recombinant
Mel-7, Alpha-galactosidase, b4119, JW4080.
Product # :
ENZ-609Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
melA E. coli Recombinant produced in E. coli is a single polypeptide chain containing 474 amino acids (1-451) and having a molecular mass of 53.0kDa.melA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The melA solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
melA is a member of the glycosyl hydrolase 4 family. melA catalyze the hydrolysis of saccharides containing o-1,6,-galactoside bonds. melA catalyze the same reaction in E.coli, human and yeast but is found in different cellular sections: The E.coli melA is a cytoplasmic protein and the human and yeast melA are secretory proteins. Thus, even though the active enzyme from all three species has almost an equal molecular weight, structural resemblances, as well as dissimilarities, are probable.
-
Synonyms
Mel-7, Alpha-galactosidase, b4119, JW4080.
-
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 MGSMMSAPKI TFIGAGSTIF VKNILGDVFH REALKTAHIA LMDIDPTRLE ESHIVVRKLM DSAGASGKIT CHTQQKEALE DADFVVVAFQ IGGYEPCTVT DFEVCKRHGL EQTIADTLGP GGIMRALRTI PHLWQICEDM TEVCPDATML NYVNPMAMNT WAMYARYPHI KQVGLCHSVQ GTAEELARDL NIDPATLRYR CAGINHMAFY LELERKTADG SYVNLYPELL AAYEAGQAPK PNIHGNTRCQ NIVRYEMFKK LGYFVTESSE HFAEYTPWFI KPGREDLIER YKVPLDEYPK RCVEQLANWH KELEEYKKAS RIDIKPSREY ASTIMNAIWT GEPSVIYGNV RNDGLIDNLP QGCCVEVACL VDANGIQPTK VGTLPSHLAA LMQTNINVQT LLTEAILTEN RDRVYHAAMM DPHTAAVLGI DEIYALVDDL IAAHGDWLPG WLHR.
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 :
MSRB2 HumanDescription:
Methionine Sulfoxide Reductase B2 Human Recombinant
CBS-1, PILB, Pilin-like Transcription Factor, MSRB, CGI-131, Mmethionine Sulfoxide Reductase B2, Methionine-R-Sulfoxide Reductase B2 Mitochondrial, MGC26104, MsrB2. EC 1.8.4.
Product # :
ENZ-036Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
MSRB2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (21-182a.a.) and having a molecular mass of 19.5kDa.MSRB2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MSRB2 protein solution (1mg/1ml) is formulated in In 20 mM Tris-HCl Buffer (pH 7.5), 1 mM DTT, 0.1 mM PMSF and 10% Glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
MSRB2 is a member of the methionine sulfoxide reductases(MSRs) family which are antioxidant repair enzymes. MSRB2 protein catalyzes the decrease of free and protein-bound methionine sulfoxide to methionine. MSRB2 has a part in protecting against oxidative stress in numerous organs.
-
Synonyms
CBS-1, PILB, Pilin-like Transcription Factor, MSRB, CGI-131, Mmethionine Sulfoxide Reductase B2, Methionine-R-Sulfoxide Reductase B2 Mitochondrial, MGC26104, MsrB2. EC 1.8.4.
-
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 MVRGQAGGGG PGTGPGLGEA GSLATCELPL AKSEWQKKLT PEQFYVTREK GTEPPFSGIY LNNKEAGMYH CVCCDSPLFS SEKKYCSGTG WPSFSEAHGT SGSDESHTGI LRRLDTSLGS ARTEVVCKQC EAHLGHVFPD GPGPNGQRFC INSVALKFKP RKH
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 :
PGAM2 HumanDescription:
Phosphoglycerate Mutase 2 Human Recombinant
Phosphoglycerate mutase 2, BPG-dependent PGAM 2, Muscle-specific phosphoglycerate mutase, Phosphoglycerate mutase isozyme M, PGAM-M, PGAM2, PGAMM, GSD10.
Product # :
ENZ-578Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
PGAM2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 273 amino acids (1-253) and having a molecular mass of 30.9kDa.PGAM2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PGAM2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Phosphoglycerate mutase 2 (PGAM2) is a member of the phosphoglycerate mutase family. PGAM is a dimeric enzyme which contains in separate tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM (Phosphoglycerate mutase) catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM2 gene mutations cause muscle phosphoglycerate mutase efficiency, otherwise known as glycogen storage disease X.
-
Synonyms
Phosphoglycerate mutase 2, BPG-dependent PGAM 2, Muscle-specific phosphoglycerate mutase, Phosphoglycerate mutase isozyme M, PGAM-M, PGAM2, PGAMM, GSD10.
-
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 MATHRLVMVR HGESTWNQEN RFCGWFDAEL SEKGTEEAKR GAKAIKDAKM EFDICYTSVL KRAIRTLWAI LDGTDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD IPPPPMDEKH PYYNSISKER RYAGLKPGEL PTCESLKDTI ARALPFWNEE IVPQIKAGKR VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL NKELKPTKPM QFLGDEETVR KAMEAVAAQG KAK.
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 :
GSTT2 HumanDescription:
Glutathione S-Transferase Theta-2 Human Recombinant
Glutathione S-transferase theta 2, GST class-theta-2, GSTT2B, Glutathione S-transferase theta-2B, EC 2.5.1.18.
Product # :
ENZ-593Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
GSTT2 Recombinant produced in E. coli is a single polypeptide chain containing 264 amino acids (1-244) and having a molecular mass of 29.6kDa.GSTT2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GSTT2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl,
1mM DTT and 10% glycerol.Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
GSTT2 belongs to the glutathione s-transferase (GST) family of proteins. There are eight GST proteins families, named alpha, kappa, mu, omega, pi, sigma, theta and zeta. Each one of the GST families has several proteins with different functions throughout the cell. The theta type members GSTT1 and GSTT2 have a 55% aa sequence homology and hold a vital role in human carcinogenesis. The theta genes are structurally similar – each has five exons with identical exon/intron boundaries.
-
Synonyms
Glutathione S-transferase theta 2, GST class-theta-2, GSTT2B, Glutathione S-transferase theta-2B, EC 2.5.1.18.
-
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 MGLELFLDLV SQPSRAVYIF AKKNGIPLEL RTVDLVKGQH KSKEFLQINS LGKLPTLKDG DFILTESSAI LIYLSCKYQT PDHWYPSDLQ ARARVHEYLG WHADCIRGTF GIPLWVQVLG PLIGVQVPEE KVERNRTAMD QALQWLEDKF LGDRPFLAGQ QVTLADLMAL EELMQPVALG YELFEGRPRL AAWRGRVEAF LGAELCQEAH SIILSILEQA AKKTLPTPSP EAYQAMLLRI ARIP
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 :
ACPP Human, Sf9Description:
Acid Phosphatase Prostate, Human Recombinant, sf9
Acid Phosphatase, Prostate, Thiamine Monophosphatase, Ecto-5-Nucleotidase, 5-Nucleotidase, EC 3.1.3.2, TMPase, 5-NT, Prostatic Acid Phosphatase, Prostatic Acid Phosphotase, EC 3.1.3.5, ACP-3 , ACP3, PAP.
Product # :
ENZ-968Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
ACPP produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 360 amino acids (33-386 a.a.) and having a molecular mass of 41.8kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). ACPP is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ACPP protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Acid phosphatase, prostate (ACPP) is a non-specific tyrosine phosphatase, which dephosphorylates a varied number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. ACPP has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma.
-
Synonyms
Acid Phosphatase, Prostate, Thiamine Monophosphatase, Ecto-5-Nucleotidase, 5-Nucleotidase, EC 3.1.3.2, TMPase, 5-NT, Prostatic Acid Phosphatase, Prostatic Acid Phosphotase, EC 3.1.3.5, ACP-3 , ACP3, PAP.
-
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
KELKFVTLVF RHGDRSPIDT FPTDPIKESS WPQGFGQLTQ LGMEQHYELG EYIRKRYRKF LNESYKHEQV YIRSTDVDRT LMSAMTNLAA LFPPEGVSIW NPILLWQPIP VHTVPLSEDQ LLYLPFRNCP RFQELESETL KSEEFQKRLH PYKDFIATLG KLSGLHGQDL FGIWSKVYDP LYCESVHNFT LPSWATEDTM TKLRELSELS LLSLYGIHKQ KEKSRLQGGV LVNEILNHMK RATQIPSYKK LIMYSAHDTT VSGLQMALDV YNGLLPPYAS CHLTELYFEK GEYFVEMYYR NETQHEPYPL MLPGCSPSCP LERFAELVGP VIPQDWSTEC MTTNSHQGTE DSTDHHHHHH.
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 :
GSTP2 Mouse, HisDescription:
Glutathione S-Transferase pi 2 Mouse Recombinant, His Tag
Glutathione S-transferase P 2 (EC:2.5.1.18), Gst P2, GST YF-YF, GST class-pi, GST-piA, Gstp2, Gstpia.
Product # :
ENZ-928Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
GSTP2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a) and having a molecular mass of 25.9kDa. GSTP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GSTP2 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Gltathione S-transferase PI 2, also known as GSTP2 is multifunctional enzyme which is involved in theprotection of cellular components against anti-cancer drugs or peroxidative stress. Furthermore, down regulation of GSTP2induces an increase of oxidative damage in the pyramidal cells of the CA1&CA3 regions as well as in the granular layer ofthe dentate gyrus, which at the end leads to structural and functional damage.
-
Synonyms
Glutathione S-transferase P 2 (EC:2.5.1.18), Gst P2, GST YF-YF, GST class-pi, GST-piA, Gstp2, Gstpia.
-
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 MGSMPPYTIV YFPSPGRCEA MRMLLADQGQ SWKEEVVTID TWMQGLLKPT CLYGQLPKFE DGDLTLYQSN AILRHLGRSL GLYGKNQREA AQVDMVNDGV EDLRGKYGTM IYRNYENGKN DYVKALPGHL KPFETLLSQN QGGKAFIVGD QISFADYNLL DLLLIHQVLA PGCLDNFPLL SAYVARLSAR PKIKAFLSSP EHVNRPINGN GKQ.
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 :
CTSD MouseDescription:
Cathepsin-D Mouse Recombinant
Ctsd, CatD, CD, Cathepsin D.
Product # :
ENZ-1017Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
CTSD produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 398 amino acids (21-410 a.a.) and having a molecular mass of 44.0kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CTSD is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CTSD protein solution (0.25mg/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 > 1,000 pmol/min/ug in which one unit will convert 1.0 pmole of Mca-PLGL-Dpa-AR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25C.Citations
More Info
-
Introduction
Cathepsin D is synthesized as a 54kDa precursor, which is proteolytically processed to an intermediate 48kDa single chain, which matures into more stable 34kDa and 14kDa two chain form. It is an estrogen-regulated lysosomal protease that has been suggested to facilitate cancer cell migration and invasion by digesting the basement membrane, extracellular matrix, and xonnective tissue. Because of its mitogenic and proteolytic activities, it has been implicated as a prognostic marker in many tumor types. Cathepsin D is expressed in epithelial cells as well as in macrophages.
-
Synonyms
Ctsd, CatD, CD, Cathepsin D.
-
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
IIRIPLRKFT SIRRTMTEVG GSVEDLILKG PITKYSMQSS PKTTEPVSEL LKNYLDAQYY GDIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KILDIACWVH HKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC KSDQSKARGI KVEKQIFGEA TKQPGIVFVA AKFDGILGMG YPHISVNNVL PVFDNLMQQK LVDKNIFSFY LNRDPEGQPG GELMLGGTDS KYYHGELSYL NVTRKAYWQV HMDQLEVGNE LTLCKGGCEA IVDTGTSLLV GPVEEVKELQ KAIGAVPLIQ GEYMIPCEKV SSLPTVYLKL GGKNYELHPD KYILKVSQGG KTICLSGFMG MDIPPPSGPL WILGDVFIGS YYTVFDRDNN RVGFANAVVL LEHHHHHH.
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 :
ELANE MouseDescription:
Elastase-2 Mouse Recombinant
Elane, Ela2, F430011M15Rik, NE, Neutrophil elastase, Elastase-2, Leukocyte elastase.
Product # :
ENZ-1105Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
ELANE Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain (27-265a.a.) fused to a 6 aa His Tag at C-terminus containing 245 amino acids and having a molecular mass of 26.8kDa.ELANE shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
ELANE protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 30% Glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Elastase-2 (ELANE) is a serine protease that belongs to the chymotrypsin family. ELANE breaks down elastin, an elastic fiber together with collagen and controls the mechanical properties of connective tissue. The neutrophil form breaks down the Outer membrane protein A (OmpA) of E. coli and other Gram-negative bacteria. ELANEis inhibited by the acute-phase protein alpha 1-antitrypsin (A1AT), which binds almost irreversibly to the active site of elastase and trypsin.A1AT is usually secreted by the liver cells into the serum. A1AD leads to uninhibited destruction of elastic fiber by elastase.
-
Synonyms
Elane, Ela2, F430011M15Rik, NE, Neutrophil elastase, Elastase-2, Leukocyte elastase.
-
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
SEIVGGRPAR PHAWPFMASL QRRGGHFCGA TLIARNFVMS AAHCVNGLNF RSVQVVLGAH
DLRRQERTRQ TFSVQRIFEN GFDPSQLLND IVIIQLNGSA TINANVQVAQ LPAQGQGVGD
RTPCLAMGWG RLGTNRPSPS VLQELNVTVV TNMCRRRVNV CTLVPRRQAG ICFGDSGGPL
VCNNLVQGID SFIRGGCGSG LYPDAFAPVA EFADWINSII RSHNDHLLTH PKDREGRTNH HHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GSTM5 Human, ActiveDescription:
Glutathione S-Transferase MU 5 Human Recombinant, Active
Glutathione S-transferase mu 5, GSTM5-5, GST class-mu 5, GTM5, glutathione S-alkyltransferase M5, S-(hydroxyalkyl) glutathione lyase M5, EC 2.5.1.18.
Product # :
ENZ-997Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
GSTM5 Human Recombinant produced in E. coli is a single polypeptide chain containing 242 amino acids (1-218) and having a molecular mass of 28.2 kDa.GSTM5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GSTM5 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 90,000 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 25C.Citations
More Info
-
Introduction
Glutathione S-transferase mu 5 (GSTM5) belongs to the glutathione s-transferase (GST) family of proteins. There are 8 families of GST proteins, specifically alpha, kappa, mu, omega, pi, sigma, theta and zeta, each of which is comprised of proteins which have various functions throughout the cell. GSTM5 belongs to the mu class of enzymes which function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. GSTM5 has an imperative role in detoxification. GSTM5 conjugates reduced glutathione to a large number of exogenous and endogenous hydrophobic electrophiles.
-
Synonyms
Glutathione S-transferase mu 5, GSTM5-5, GST class-mu 5, GTM5, glutathione S-alkyltransferase M5, S-(hydroxyalkyl) glutathione lyase M5, EC 2.5.1.18.
-
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 MGSHMPMTLG YWDIRGLAHA IRLLLEYTDS SYVEKKYTLG DAPDYDRSQW LNEKFKLGLD FPNLPYLIDG AHKITQSNAI LRYIARKHNL CGETEEEKIR VDILENQVMD NHMELVRLCY DPDFEKLKPK YLEELPEKLK LYSEFLGKRP WFAGDKITFV DFLAYDVLDM KRIFEPKCLD AFLNLKDFIS RFEGLKKISA YMKSSQFLRG LLFGKSATWN SK.
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 :
CTH HumanDescription:
Cystathionase Human Recombinant
Cystathionine gamma-lyase, Cysteine-protein sulfhydrase, Gamma-cystathionase, CTH.
Product # :
ENZ-212Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
CTH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 425 amino acids (1-405) and having a molecular mass of 46.7kDa.CTH is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CTH solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Cystathionine gamma-lyase or cystathionase (CTH) is a member of the trans-sulfuration enzymes family. CTH is an enzyme which breaks down cystathionine into cysteine and alpha-ketobutyrate. The CTH catalyzes the last step in the transsulfuration pathway from methionine to cysteine. Glutathione synthesis in the liver is dependent upon the availability of cysteine. Mutations in the CTH gene cause cystathioninuria.
-
Synonyms
Cystathionine gamma-lyase, Cysteine-protein sulfhydrase, Gamma-cystathionase, CTH.
-
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 MQEKDASSQG FLPHFQHFAT QAIHVGQDPE QWTSRAVVPP ISLSTTFKQG APGQHSGFEY SRSGNPTRNC LEKAVAALDG AKYCLAFASG LAATVTITHL LKAGDQIICM DDVYGGTNRY FRQVASEFGL KISFVDCSKI KLLEAAITPE TKLVWIETPT NPTQKVIDIE GCAHIVHKHG DIILVVDNTF MSPYFQRPLA LGADISMYSA TKYMNGHSDV VMGLVSVNCE SLHNRLRFLQ NSLGAVPSPI DCYLCNRGLK TLHVRMEKHF KNGMAVAQFL ESNPWVEKVI YPGLPSHPQH ELVKRQCTGC TGMVTFYIKG TLQHAEIFLK NLKLFTLAES LGGFESLAEL PAIMTHASVL KNDRDVLGIS DTLIRLSVGL EDEEDLLEDL DQALKAAHPP SGSHS.
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 :
ALDOC MouseDescription:
Aldolase C Fructose-Bisphosphate Mouse Recombinant
Aldolase 3, Brain-type aldolase, Scrapie-responsive protein 2, Zebrin II, Aldo3, Scrg2, Fructose-bisphosphate aldolase C, ALDOC.
Product # :
ENZ-868Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
ALDOC Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-363 a.a) and having a molecular mass of 41.9kDa.ALDOC is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ALDOC solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Aldolase C Fructose-Bisphosphate (ALDOC) belongs to the class I fructose-bisphosphate aldolase family. ALDOC is a glycolytic enzyme which catalyzes the reversible aldol cleavage of fructose-1,6-biphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehydes respectively. ALDOC is expressed exclusively in the hippocampus and Purkinje cells of the brain.
-
Synonyms
Aldolase 3, Brain-type aldolase, Scrapie-responsive protein 2, Zebrin II, Aldo3, Scrg2, Fructose-bisphosphate aldolase C, ALDOC.
-
Physical Appearance
Sterile Filtered clear 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 MGSHMPHSYP ALSAEQKKEL SDIALRIVTP GKGILAADES VGSMAKRLSQ IGVENTEENR RLYRQVLFSA DDRVKKCIGG VIFFHETLYQ KDDNGVPFVR TIQDKGILVG IKVDKGVVPL AGTDGETTTQ GLDGLLERCA QYKKDGADFA KWRCVLKISD RTPSALAILE NANVLARYAS ICQQNGIVPI VEPEILPDGD HDLKRCQYVT EKVLAAVYKA LSDHHVYLEG TLLKPNMVTP GHACPIKYSP EEIAMATVTA LRRTVPPAVP GVTFLSGGQS EEEASLNLNA INRCPLPRPW ALTFSYGRAL QASALNAWRG QRDNAGAATE EFIKRAEMNG LAAQGRYEGS GDGGAAAQSL YIANHAY
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 :
NPL HumanDescription:
N-acetylneuraminate Pyruvate Lyase Human Recombinant
N-acetylneuraminate lyase, NALase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, Sialate lyase, Sialate-pyruvate lyase, Sialic acid aldolase, Sialic acid lyase, NPL, C1orf13, NAL, C112, NPL1.
Product # :
ENZ-125Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
NPL produced in E.Coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (1-320 a.a.) and having a molecular mass of 37.3kDa.NPL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NPL protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
N-acetylneuraminate lyase (NPL) is an enzyme which catalyzes the chemical reaction (N-acetylneuraminate ->N-acetyl-D-mannosamine + pyruvate). NPL is a member of a family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. NPL participates in amino sugars metabolism.
-
Synonyms
N-acetylneuraminate lyase, NALase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, Sialate lyase, Sialate-pyruvate lyase, Sialic acid aldolase, Sialic acid lyase, NPL, C1orf13, NAL, C112, NPL1.
-
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 MAFPKKKLQG LVAATITPMT ENGEINFSVI GQYVDYLVKE QGVKNIFVNG TTGEGLSLSV SERRQVAEEW VTKGKDKLDQ VIIHVGALSL KESQELAQHA AEIGADGIAV IAPFFLKPWT KDILINFLKE VAAAAPALPF YYYHIPALTG VKIRAEELLD GILDKIPTFQ GLKFSDTDLL DFGQCVDQNR QQQFAFLFGV DEQLLSALVM GATGAVGSTY NYLGKKTNQM LEAFEQKDFS LALNYQFCIQ RFINFVVKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKASR EFTDSAEAKL KSLDFLSFTD LKDGNLEAGS.
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 :
GLB1 E.ColiDescription:
Galactosidase-Beta 1 E.coli Recombinant
lacZ, beta-gal, β-gal.
Product # :
ENZ-041Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
The E.Coli derived recombinant protein Beta-galactosidase (114 kDa) is enzymatically inactive and Non-reactive with human serum.
Source
Escherichia Coli.
Formulation
Beta-Galactosidase (1mg/1ml) is formulated in 8M urea, 20mM Tris-HCl pH 8.0, and 10mM beta-mercaptoethanol
Purity
Protein is >95% pure as determined by SDS-PAGE, by measuring optical density at 280 nm and by method of Bradford et al.
Citations
More Info
-
Introduction
Beta-galactosidase is a hydrolase enzyme that catalyzes the hydrolysis of Beta-galactosides into monosaccharides. Substrates of different Beta-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Beta-galactosidase is produced In E. coli by activation of the lac operon as the lacZ gene.
-
Synonyms
lacZ, beta-gal, β-gal.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Protein should be stored for Short Term at 4°C and for long term at -20°C.
-
Purification Method
Purified by proprietary chromatographic technique.
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 :
FOLH1 HumanDescription:
Folate Hydrolase 1 Human Recombinant
Glutamate carboxypeptidase 2 isoform 1,Cell growth-inhibiting gene 27 protein, Folate hydrolase 1, Folylpolygamma-glutamate carboxypeptidase, Glutamate carboxypeptidase II, Membrane glutamate carboxypeptidase, Nacetylated-alpha-linked acidic dipeptidase I, Prostate-specific membrane antigen, Pteroylpoly-gamma glutamate carboxypeptidase, Folh1, FGCP, FOLH, GCP2, GCPII, mGCP, NAALAD1, NAALAdase, PSM, PSMA
Product # :
ENZ-1170Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
FOLH1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 717 amino acids (44-750 a.a) and having a molecular mass of 80.7kDa.FOLH1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
FOLH1 protein solution (0.25mg/ml) contains Phosphate buffered saline (pH 7.4) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
FOLH1, also known as glutamate carboxypeptidase 2 (GCPII), is a single pass type 2 membrane protein which belongs to the peptidase M28 family. FOLH1 is highly produced in prostate epithelium. FOLH1 is also found in ovary, live, stomach, small intestine colon, urinary bladder, kidney, testis, and the capillary endothelium of a variety of tumours. Therefore, it plays a role in directed imaging and therapy of recurrent of metastatic disease. FOLH1 is a zinc metalloenzyme that resides in membranes and catalyses the hydrolysis of N-acetylaspartylglutamate to glutamate and N-acetylaspartate.
-
Synonyms
Glutamate carboxypeptidase 2 isoform 1,Cell growth-inhibiting gene 27 protein, Folate hydrolase 1, Folylpolygamma-glutamate carboxypeptidase, Glutamate carboxypeptidase II, Membrane glutamate carboxypeptidase, Nacetylated-alpha-linked acidic dipeptidase I, Prostate-specific membrane antigen, Pteroylpoly-gamma glutamate carboxypeptidase, Folh1, FGCP, FOLH, GCP2, GCPII, mGCP, NAALAD1, NAALAdase, PSM, PSMA
-
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
ADPMKSSNEA TNITPKHNMK AFLDELKAEN IKKFLYNFTQ IPHLAGTEQN FQLAKQIQSQ WKEFGLDSVE LAHYDVLLSY PNKTHPNYIS IINEDGNEIF NTSLFEPPPP GYENVSDIVP PFSAFSPQGM PEGDLVYVNY ARTEDFFKLE RDMKINCSGK IVIARYGKVF RGNKVKNAQL AGAKGVILYS DPADYFAPGV KSYPDGWNLP GGGVQRGNIL NLNGAGDPLT PGYPANEYAY RRGIAEAVGL PSIPVHPIGY YDAQKLLEKM GGSAPPDSSW RGSLKVPYNV GPGFTGNFST QKVKMHIHST NEVTRIYNVI GTLRGAVEPD RYVILGGHRD SWVFGGIDPQ SGAAVVHEIV RSFGTLKKEG WRPRRTILFA SWDAEEFGLL GSTEWAEENS RLLQERGVAY INADSSIEGN YTLRVDCTPL MYSLVHNLTK ELKSPDEGFE GKSLYESWTK KSPSPEFSGM PRISKLGSGN DFEVFFQRLG IASGRARYTK NWETNKFSGY PLYHSVYETY ELVEKFYDPM FKYHLTVAQV RGGMVFELAN SIVLPFDCRD YAVVLRKYAD KIYSISMKHP QEMKTYSVSF DSLFSAVKNF TEIASKFSER LQDFDKSNPI VLRMMNDQLM FLERAFIDPL GLPDRPFYRH VIYAPSSHNK YAGESFPGIY DALFDIESKV DPSKAWGEVK RQIYVAAFTV QAAAETLSEV AHHHHHH
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 :
MMP23B HumanDescription:
Matrix Metallopeptidase 23B Human Recombinant
Matrix Metallopeptidase 23B, MMP23B, MMP22, Matrix Metalloproteinase 23B, Matrix Metalloproteinase 22, Matrix Metalloproteinase In The Female Reproductive Tract, Matrix Metalloproteinase-21, Matrix Metalloproteinase-22, MIFR-1, MMP-21, MMP-22, MMP-23, MIFR, MMP23A, Matrix Metalloproteinase-23, EC 3.4.24.-, Femalysin, MMP21.
Product # :
ENZ-793Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
MMP23B Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 199 amino acids (79-254) and having a molecular mass of 22.6kDa.MMP23B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MMP23B solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Matrix Metallopeptidase 23B (MMP23B) belongs to the matrix metalloproteinase (MMP) family, and it is section of a duplicated region of chromosome 1p36.3. MMP23B is a protease. MMP23B regulates the surface expression of some potassium channels by holding them in the endoplasmic reticulum. Members of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis.
-
Synonyms
Matrix Metallopeptidase 23B, MMP23B, MMP22, Matrix Metalloproteinase 23B, Matrix Metalloproteinase 22, Matrix Metalloproteinase In The Female Reproductive Tract, Matrix Metalloproteinase-21, Matrix Metalloproteinase-22, MIFR-1, MMP-21, MMP-22, MMP-23, MIFR, MMP23A, Matrix Metalloproteinase-23, EC 3.4.24.-, Femalysin, MMP21.
-
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 MGSYTLTPAR LRWDHFNLTY RILSFPRNLL SPRETRRALA AAFRMWSDVS PFSFREVAPE QPSDLRIGFY PINHTDCLVS ALHHCFDGPT GELAHAFFPP HGGIHFDDSE YWVLGPTRYS WKKGVWLTDL VHVAAHEIGH ALGLMHSQHG RALMHLNATL RGWKALSQDE LWGLHRLYG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GSTA4 HumanDescription:
Glutathione S-Transferase Alpha 4 Human Recombinant
Glutathione S-transferase A4, GST class-alpha member 4, Glutathione S-transferase A4-4, GSTA4, GSTA4-4.
Product # :
ENZ-600Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
GSTA4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-222) and having a molecular mass of 28.3kDa.GSTA4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GSTA4 solution (1mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 20% glycerol, 2mM DTT and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Glutathione S-transferase A4 (GSTA4) is a member of the GST superfamily. The GSTA4 enzyme is involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. GSTA4 shows an especially high activity with reactive carbonyl compounds such as alk-2-enals. GSTA4 is extremely effective in catalyzing the conjugate addition of reduced glutathione to 4-hydroxynonenal, which is an important product of peroxidative degradation of arachidonic acid and a frequently used biomarker for oxidative damage in tissue. The GSTA4 enzyme is expressed at a high level in the brain, placenta, and skeletal muscle and much lower in the lung and liver.
-
Synonyms
Glutathione S-transferase A4, GST class-alpha member 4, Glutathione S-transferase A4-4, GSTA4, GSTA4-4.
-
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 MGSHMAARPK LHYPNGRGRM ESVRWVLAAA GVEFDEEFLE TKEQLYKLQD GNHLLFQQVP MVEIDGMKLV QTRSILHYIA DKHNLFGKNL KERTLIDMYV EGTLDLLELL IMHPFLKPDD QQKEVVNMAQ KAIIRYFPVF EKILRGHGQS FLVGNQLSLA
DVILLQTILA LEEKIPNILS AFPFLQEYTV KLSNIPTIKR FLEPGSKKKP PPDEIYVRTV YNIFRP.
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 :
CTSA MouseDescription:
Cathepsin-A Mouse Recombinant
Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.
Product # :
ENZ-945Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
CTSA produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 459 amino acids (24-474 a.a.) and having a molecular mass of 52.4kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CTSA is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9 Insect cells.
Formulation
CTSA protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Cathepsin-A (CTSA) is a protective protein which is crucial for both the activity of beta-galactosidase and neuraminidase, CTSA associates with these enzymes and exerts a protective function required for their stability and activity. The CTSA protein is also a carboxypeptidase and can deamidate tachykinins. CTSA is a component of the lysosomal multienzyme complex along with beta-galactosidase and sialidase Neu1. CTSA is a multicatalytic enzyme with deamidase and esterase in addition to carboxypeptidase activities.
-
Synonyms
Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.
-
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
APDQDEIDCL PGLAKQPSFR QYSGYLRASD SKHFHYWFVE SQNDPKNSPV VLWLNGGPGC SSLDGLLTEH GPFLIQPDGV TLEYNPYAWN LIANVLYIES PAGVGFSYSD DKMYVTNDTE VAENNYEALK DFFRLFPEYK DNKLFLTGES YAGIYIPTLA VLVMQDPSMN LQGLAVGNGL ASYEQNDNSL VYFAYYHGLL GNRLWTSLQT HCCAQNKCNF YDNKDPECVN NLLEVSRIVG KSGLNIYNLY APCAGGVPGR HRYEDTLVVQ DFGNIFTRLP LKRRFPEALM RSGDKVRLDP PCTNTTAPSN YLNNPYVRKA LHIPESLPRW DMCNFLVNLQ YRRLYQSMNS QYLKLLSSQK YQILLYNGDV DMACNFMGDE WFVDSLNQKM EVQRRPWLVD YGESGEQVAG FVKECSHITF LTIKGAGHMV PTDKPRAAFT MFSRFLNKEP YVEHHHHHH.
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 :
MTHFD2 HumanDescription:
MTHFD2 Human Recombinant
Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial, NAD-dependent methylenetetrahydrofolate dehydrogenase, Methenyltetrahydrofolate cyclohydrolase, NMDMC, MTHFD2.
Product # :
ENZ-853Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
MTHFD2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (30-350) and having a molecular mass of 37.2kDa.MTHFD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MTHFD2 solution (1mg/ml) contains Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
MTHFD2 plays a role as a homodimer which requires magnesium and inorganic phosphate. MTHFD2 has a pseudogene on chromosome 7 and owns 3 different enzymatic activities. Each of the activities catalyzes 1 of 3 sequential reactions in the interconversion of 1-carbon derivatives of tetrahydrofolate, which are substrates for methionine, thymidylate, and de novo purine syntheses.
-
Synonyms
Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial, NAD-dependent methylenetetrahydrofolate dehydrogenase, Methenyltetrahydrofolate cyclohydrolase, NMDMC, MTHFD2.
-
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 MGSLAAVRNE AVVISGRKLA QQIKQEVRQE VEEWVASGNK RPHLSVILVG ENPASHSYVL NKTRAAAVVG INSETIMKPA SISEEELLNL INKLNNDDNV DGLLVQLPLP EHIDERRICN AVSPDKDVDG FHVINVGRMC LDQYSMLPAT PWGVWEIIKR TGIPTLGKNV VVAGRSKNVG MPIAMLLHTD GAHERPGGDA TVTISHRYTP KEQLKKHTIL ADIVISAAGI PNLITADMIK EGAAVIDVGI NRVHDPVTAK PKLVGDVDFE GVRQKAGYIT PVPGGVGPMT VAMLMKNTII AAKKVLRLEE REVLKSKELG VATN.
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 :
PCOLCE HumanDescription:
Procollagen C-Endopeptidase Enhancer Human Recombinant
Procollagen C-Endopeptidase Enhancer, Procollagen C-Proteinase Enhancer 1, Type I Procollagen COOH-Terminal Proteinase Enhancer, Type 1 Procollagen C-Proteinase Enhancer Protein, Procollagen COOH-Terminal Proteinase Enhancer 1, PCPE-1, PCPE1, Procollagen, Type 1, COOH-Terminal Proteinase Enhancer, Procollagen C-Endopeptidase Enhancer 1, COOH-Terminal Proteinase Enhancer, Procollagen, Type 1, PCPE, Procollagen C-endopeptidase enhancer 1.
Product # :
ENZ-863Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
PCOLCE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids (26-449 a.a) and having a molecular mass of 47.9kDa. PCOLCE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PCOLCE protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Procollagen C-endopeptidase enhancer 1, also known as PCOLCE binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity. In addition, C-terminal processed part of PCPE (CT-PCPE) has a metalloproteinase inhibitory activity. Among the diseases which are associated with PCOLCE: bone fracture & oculopharyngeal muscular dystrophy.
-
Synonyms
Procollagen C-Endopeptidase Enhancer, Procollagen C-Proteinase Enhancer 1, Type I Procollagen COOH-Terminal Proteinase Enhancer, Type 1 Procollagen C-Proteinase Enhancer Protein, Procollagen COOH-Terminal Proteinase Enhancer 1, PCPE-1, PCPE1, Procollagen, Type 1, COOH-Terminal Proteinase Enhancer, Procollagen C-Endopeptidase Enhancer 1, COOH-Terminal Proteinase Enhancer, Procollagen, Type 1, PCPE, Procollagen C-endopeptidase enhancer 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 MGSQTPNYTR PVFLCGGDVK GESGYVASEG FPNLYPPNKE CIWTITVPEG QTVSLSFRVF DLELHPACRY DALEVFAGSG TSGQRLGRFC GTFRPAPLVA PGNQVTLRMT TDEGTGGRGF LLWYSGRATS GTEHQFCGGR LEKAQGTLTT PNWPESDYPP GISCSWHIIA PPDQVIALTF EKFDLEPDTY CRYDSVSVFN GAVSDDSRRL GKFCGDAVPG SISSEGNELL VQFVSDLSVT ADGFSASYKT LPRGTAKEGQ GPGPKRGTEP KVKLPPKSQP PEKTEESPSA PDAPTCPKQC RRTGTLQSNF CASSLVVTAT VKSMVREPGE GLAVTVSLIG AYKTGGLDLP SPPTGASLKF YVPCKQCPPM KKGVSYLLMG QVEENRGPVL PPESFVVLHR PNQDQILTNL SKRKCPSQPV RAAASQD.
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 :
Chymotrypsin PorcineDescription:
Alpha Chymotrypsin Porcine
a-chymotrypsin, alpha chymotrypsin.
Product # :
ENZ-1195Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- biological activity
- More Info
- Citations
Description
Chymotrypsin purified from porcine pancreas, CAS: 9004-07-3, EC: 3.4.21.1 having a molecular mass of ~25kDa.
Source
Porcine Pancreas.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Biological Activity
Greater than 1500 USP U/mg.
Citations
More Info
-
Synonyms
a-chymotrypsin, alpha chymotrypsin.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Chymotrypsin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Chymotrypsin 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 Chymotrypsin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Background
Porcine chymotrypsin, derived from the pancreas of pigs, stands as a cornerstone in enzymology, serving as a paradigmatic model for understanding proteolytic mechanisms and substrate specificity. Renowned for its catalytic prowess and structural intricacies, porcine chymotrypsin has garnered significant attention from researchers across various scientific disciplines.
The fascination with porcine chymotrypsin stems from its ability to cleave peptide bonds selectively after large hydrophobic amino acids, such as tryptophan, tyrosine, and phenylalanine.
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 :
ALPP Human, ActiveDescription:
Alkaline Phosphatase Placental Human Recombinant, BioActive
3 ALPP, Alkaline phosphatase Regan isozyme, Placental alkaline phosphatase 1, PLAP-1, ALP, PLAP, Alkaline phosphatase placental type, EC 3.1.3.1, PLAP-1, Alkaline phosphatase Regan isozyme.
Product # :
ENZ-1133Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
ALPP Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 494 amino acids (23-506 a.a.) and having a molecular mass of 53.9kDa. ALPP is expressed with a 10 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ALPP 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 > 2,500unit/mg, and is defined as the amount of enzyme that hydrolyze 1.0nmole of pnitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37C.
Citations
More Info
-
Introduction
Placental alkaline phosphatase also known as PLAP is a membranal siaglycoprotein enzyme typicallyfoundin high concentration in syncytiotrophoblasts in the placenta amid the 3th trimester of gestation. The expression of PLAP was at firstconsidered to be onlyin the term placenta, though, a human PLAP-like variant has been found,thathas more than 85% homology with PLAP itself. PLAP is expressed strictly in normal term placenta, endocervix & fallopian tube and in ovarian and proximal gastrointestinal tumors. It is also widely expressed in germ cell tumors and more recently found in seminomas.
-
Synonyms
3 ALPP, Alkaline phosphatase Regan isozyme, Placental alkaline phosphatase 1, PLAP-1, ALP, PLAP, Alkaline phosphatase placental type, EC 3.1.3.1, PLAP-1, Alkaline phosphatase Regan isozyme.
-
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
ADLMIIPVEE ENPDFWNREA AEALGAAKKL QPAQTAAKNL IIFLGDGMGV STVTAARILK GQKKDKLGPE LPLAMDRFPY VALSKTYNVD KHVPDSGATA TAYLCGVKGN FQTIGLSAAA RFNQCNTTRG NEVISVMNRA KKAGKSVGVV TTTRVQHASP AGTYAHTVNR NWYSDADVPA SARQEGCQDI ATQLISNMDI DVILGGGRKY MFRMGTPDPE YPDDYSQGGT RLDGKNLVQE WLAKRQGARY VWNRTELMQA SLDPSVTHLM GLFEPGDMKY EIHRDSTLDP SLMEMTEAAL RLLSRNPRGF FLFVEGGRID HGHHESRAYR ALTETIMFDD AIERAGQLTS EEDTLSLVTA DHSHVFSFGG YPLRGSSIFG LAPGKARDRK AYTVLLYGNG PGYVLKDGAR PDVTESESGS PEYRQQSAVP LDEETHAGED VAVFARGPQA HLVHGVQEQT FIAHVMAFAA CLEPYTACDL APPAGTTDHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CNDP1 Human, ActiveDescription:
CNDP Dipeptidase 1 Human Recombinant, Active
Carnosine Dipeptidase 1 (Metallopeptidase M20 Family), Glutamate Carboxypeptidase-Like Protein 2, CNDP Dipeptidase 1, Serum Carnosinase, Carnosinase 1, CPGL2, CN1, Carnosine Dipeptidase 1, EC 3.4.13.20, HsT2308.
Product # :
ENZ-1022Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
CNDP1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 489 amino acids (27-507 a.a.) and having a molecular mass of 54.9kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions).CNDP1 is expressed with a 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
CNDP1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >3,000 pmol/min/ug, and as measured by the hydrolysis of carnosine per minute at pH6.8 at 25°C.Citations
More Info
-
Introduction
CNDP Dipeptidase 1, also known as CNDP1 is a member of the peptidase M20A family. CNDP1 Mannheim which is the shortest allelic form has been more common in the absence of nephropathy in addition to being associated with lower serum carnosinase levels. Furthermore, Carnosine inhibited the increased production of fibronectin as well as collagen type VI in podocytes and the increased production of TGF-beta in mesangial cells. Diabetic patients with the CNDP1 Mannheim variant are less at risk for nephropathy. In addition, on renal cells carnosine protects against the adverse effects of high glucose levels.
-
Synonyms
Carnosine Dipeptidase 1 (Metallopeptidase M20 Family), Glutamate Carboxypeptidase-Like Protein 2, CNDP Dipeptidase 1, Serum Carnosinase, Carnosinase 1, CPGL2, CN1, Carnosine Dipeptidase 1, EC 3.4.13.20, HsT2308.
-
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
SPSPPPALLE KVFQYIDLHQ DEFVQTLKEW VAIESDSVQP VPRFRQELFR MMAVAADTLQ RLGARVASVD MGPQQLPDGQ SLPIPPVILA ELGSDPTKGT VCFYGHLDVQ PADRGDGWLT DPYVLTEVDG KLYGRGATDN KGPVLAWINA VSAFRALEQD LPVNIKFIIE GMEEAGSVAL EELVEKEKDR FFSGVDYIVI SDNLWISQRK PAITYGTRGN SYFMVEVKCR DQDFHSGTFG GILHEPMADL VALLGSLVDS SGHILVPGIY DEVVPLTEEE INTYKAIHLD LEEYRNSSRV EKFLFDTKEE ILMHLWRYPS LSIHGIEGAF DEPGTKTVIP GRVIGKFSIR LVPHMNVSAV EKQVTRHLED VFSKRNSSNK MVVSMTLGLH PWIANIDDTQ YLAAKRAIRT VFGTEPDMIR DGSTIPIAKM FQEIVHKSVV LIPLGAVDDG EHSQNEKINR WNYIEGTKLF AAFFLEMAQL HLEHHHHHH.
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 :
FUT5 HumanDescription:
Fucosyltransferase 5 Human Recombinant
FUT-5
Product # :
ENZ-1199Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
The FUT5 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The FUT5 His-Tagged Fusion Protein produced in E. coli, is a 30kDa protein containing 172 amino acid residues of the FUT5 Human, 203-374 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.
Citations
More Info
-
Synonyms
FUT-5
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized FUT5 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.
-
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.
-
Background
Fucosyltransferase 5 also known as FUT5 is a glycosyltransferase which takes part in the biosynthesis of glycolipids and glycoproteins. FUT5 mainly catalyzes the transfer of fucose (a monosaccharide) to the type 2 chain of oligosaccharides (Galβ1-4GlcNAc). FUT5 takes an important part in various biological processes which include regulation of inflammation, cell-cell interactions and immune response modulation. FUT5 is expressed mainly in tissues such as the pancreas, liver and various immune cells.
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.