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1000 results found for “protease”
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Name :
LCAT HumanDescription:
Lecithin-Cholesterol Acyltransferase Human Recombinant
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.
Product # :
ENZ-380Price :
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Shipped with Ice Packs
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Description
LCAT Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 441 amino acids (25-440) which includes a 25 amino acid His Tag fused at N-terminus and having a total molecular mass of 49.8 kDa. LCAT Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LCAT protein solution (0.5mg/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
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Introduction
LCAT is an extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. LCAT is a essential enzyme in the extracellular metabolism of plasma lipoproteins.
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Synonyms
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMFWLLN VLFPPHTTPK AELSNHTRPV ILVPGCLGNQ LEAKLDKPDV VNWMCYRKTE DFFTIWLDLN MFLPLGVDCW IDNTRVVYNR SSGLVSNAPG VQIRVPGFGK TYSVEYLDSS KLAGYLHTLV QNLVNNGYVR DETVRAAPYD WRLEPGQQEE YYRKLAGLVE EMHAAYGKPV FLIGHSLGCL HLLYFLLRQP QAWKDRFIDG FISLGAPWGG SIKPMLVLAS GDNQGIPIMS SIKLKEEQRI TTTSPWMFPS RMAWPEDHVF ISTPSFNYTG RDFQRFFADL HFEEGWYMWL QSRDLLAGLP APGVEVYCLY GVGLPTPRTY IYDHGFPYTD PVGVLYEDGD DTVATRSTEL CGLWQGRQPQ PVHLLPLHGI QHLNMVFSNL TLEHINAILL GAYRQGPPAS PTASPEPPPP E.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HYAL1Description:
Hyaluronidase
Hyaluronidase-1, EC 3.2.1.35, Hyal-1, Hyaluronoglucosaminidase-1, LUCA-1.
Product # :
ENZ-323Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Hyaluronidase is an enzyme that temporarily and reversibly breaks down the polysaccharide, hyaluronic acid, which is found between the cells of connective tissue. Hyaluronic acid may be thought of as the "glue" that holds cells together. Hyaluronic acid is a mucopolysaccharide that exists in the human tissue matrix. It can constrain the diffusion of the extracellular fluid. Hyaluronidase makes the glucoseamine of the hyaluronic acid molecules hydrolyzed and depolymerized, thus decreases the viscosity of the body fluids and increases the flow and diffusion of the intercellular fluids. In this way the physic liquor, exudates or blood in local areas can be more easily diffused, and the drug can be more easily absorbed. Thus the local tissue tension and pains can be relieved. And it will also be easier for the edema and inflammatory exudates to be absorbed and dissolved. This product is a basic component of the articular cartilage. It can nourish, protect and maintain the functions of the joints.
Source
Bovine Testis.
Formulation
The enzyme was lyophilized 1xPBS and 2% sucrose.
More Info
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Synonyms
Hyaluronidase-1, EC 3.2.1.35, Hyal-1, Hyaluronoglucosaminidase-1, LUCA-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Hyaluronidase although although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Hyaluronidase should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Hyaluronidase in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Specific Activity
300 IU/mg.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Cyclophilin C HumanDescription:
Cyclophilin-C Human Recombinant
Peptidylprolyl Isomerase C (Cyclophilin C), Cyclophilin C, Rotamase C, EC 5.2.1.8, PPIase C, CYPC, Peptidyl-Prolyl Cis-Trans Isomerase C, Parvulin, PPIC.
Product # :
ENZ-809Price :
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Shipped at Room temp
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Description
Cyclophilin-C Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Phe29-Trp212) containing 194 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 21.3kDa.
Source
Escherichia Coli.
Formulation
Cyclophilin-C was filtered (0.4 µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Cyclophilin-C belongs to the peptidyl-prolyl cis-trans isomerase (PPIase)) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Like other PPIases, the Cyclophilin-C protein can bind immunosuppressant cyclosporin A.
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Synonyms
Peptidylprolyl Isomerase C (Cyclophilin C), Cyclophilin C, Rotamase C, EC 5.2.1.8, PPIase C, CYPC, Peptidyl-Prolyl Cis-Trans Isomerase C, Parvulin, PPIC.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Cyclophilin-C is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASFRKRGPSVTA KVFFDVRIGD KDVGRIVIGL FGKVVPKTVE NFVALATGEK GYGYKGSKFH RVIKDFMIQG GDITTGDGTG GVSIYGETFP DENFKLKHYG IGWVSMANAG PDTNGSQFFI TLTKPTWLDG KHVVFGKVID GMTVVHSIEL QATDGHDRPL TNCSIINSGK IDVKTPFVVE IADW.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TPST2 HumanDescription:
Tyrosylprotein Sulfotransferase 2 Human Recombinant
Protein-tyrosine sulfotransferase 2, EC 2.8.2.20, Tyrosylprotein sulfotransferase 2, TPST-2, TPST2, TANGO13B.
Product # :
ENZ-707Price :
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Description
TPST2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 375 amino acids (26-377) and having a molecular mass of 41kDa.TPST2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TPST2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Tyrosylprotein Sulfotransferase 2 (TPST2) is a member of the protein sulfotransferase family. TPST2 is a widely expressed protein, which catalyzes the O-sulfation of tyrosine residues within acidic regions of proteins. The TPST2 protein is a type II integral membrane protein located in the Golgi body.
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Synonyms
Protein-tyrosine sulfotransferase 2, EC 2.8.2.20, Tyrosylprotein sulfotransferase 2, TPST-2, TPST2, TANGO13B.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQQVLECR AVLAGLRSPR GAMRPEQEEL VMVGTNHVEY RYGKAMPLIF VGGVPRSGTT LMRAMLDAHP EVRCGEETRI IPRVLAMRQA WSKSGREKLR LDEAGVTDEV LDAAMQAFIL EVIAKHGEPA RVLCNKDPFT LKSSVYLSRL FPNSKFLLMV RDGRASVHSM ITRKVTIAGF DLSSYRDCLT KWNKAIEVMY AQCMEVGKEK CLPVYYEQLV LHPRRSLKLI LDFLGIAWSD AVLHHEDLIG KPGGVSLSKI ERSTDQVIKP VNLEALSKWT GHIPGDVVRD MAQIAPMLAQ LGYDPYANPP NYGNPDPFVI NNTQRVLKGD YKTPANLKGY FQVNQNSTSS HLGSS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NTMT1 HumanDescription:
N-Terminal Xaa-Pro-Lys N-Methyltransferase 1 Human Recombinant
NTMT1, N-Terminal Xaa-Pro-Lys N-Methyltransferase 1, X-Pro-Lys N-Terminal Protein Methyltransferase 1A, Alpha N-Terminal Protein Methyltransferase 1A , Methyltransferase-Like Protein 11A , N-Terminal RCC1 Methyltransferase, METTL11A, C9orf32, NTM1A, NRMT, Chromosome 9 Open Reading Frame 32, Methyltransferase Like 11A, EC 2.1.1.244, AD-003, HOMT1A, NRMT1.
Product # :
ENZ-929Price :
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Shipped with Ice Packs
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Description
NTMT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 248 amino acids (1-223 a.a) and having a molecular mass of 28.1kDa. NTMT1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NTMT1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
N-terminal Xaa-Pro-Lys N-methyltrasferase1, also known as NTMT1 belongs to the methyltransferase superfamily. NTMT1 catalyzesthe transfer of the methyl group from the S-adenosyl-l-methionine to the protein ?-amine, resulting in the formation of S-adenosyl-l-homocysteine and ?-N-methylated proteins. NTMT1 is a remarkable potential anticancer targetsince it is overexpressed in gastrointestinal cancers in addition to his essential function in cell mitosis.
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Synonyms
NTMT1, N-Terminal Xaa-Pro-Lys N-Methyltransferase 1, X-Pro-Lys N-Terminal Protein Methyltransferase 1A, Alpha N-Terminal Protein Methyltransferase 1A , Methyltransferase-Like Protein 11A , N-Terminal RCC1 Methyltransferase, METTL11A, C9orf32, NTM1A, NRMT, Chromosome 9 Open Reading Frame 32, Methyltransferase Like 11A, EC 2.1.1.244, AD-003, HOMT1A, NRMT1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFMTSEV IEDEKQFYSK AKTYWKQIPP TVDGMLGGYG HISSIDINSS RKFLQRFLRE GPNKTGTSCA LDCGAGIGRI TKRLLLPLFR EVDMVDITED FLVQAKTYLG EEGKRVRNYF CCGLQDFTPE PDSYDVIWIQ WVIGHLTDQH LAEFLRRCKGSLRPNGIIVI KDNMAQEGVI LDDVDSSVCR DLDVVRRIIC SAGLSLLAEE RQENLPDEIY HVYSFALR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ACAT2 HumanDescription:
Acetyl-Coenzyme A acetyltransferase 2 Human Recombinant
Acetyl-CoA acetyltransferase cytosolic, Cytosolic acetoacetyl-CoA thiolase, ACAT2, Acetyl CoA transferase-like protein, ACAT-2.
Product # :
ENZ-295Price :
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Description
ACAT2 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-397 a.a.) and having a molecular mass of 45.4 kDa. The ACAT2 is fused to 36 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ACAT2 Human solution containing 20mM Tris pH-8, 0.1M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ACAT2 enzyme participates in lipid metabolism. ACAT2 takes part in lipoprotein assembly, catalyzing cholesterol esterification in mammalian cells. ACAT2 is an integral membrane protein that localizes to the endoplasmic reticulum of human intestinal cells. ACAT2 deficiency contributes to severe mental retardation and hypotonus.
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Synonyms
Acetyl-CoA acetyltransferase cytosolic, Cytosolic acetoacetyl-CoA thiolase, ACAT2, Acetyl CoA transferase-like protein, ACAT-2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMNAG SDPVVIVSAA RTIIGSFNGA LAAVPVQDLG STVIKEVLKR ATVAPEDVSE
VIFGHVLAAG CGQNPVRQAS VGAGIPYSVP AWSCQMICGS GLKAVCLAVQ SIGIGDSSIV VAGGMENMSK APHLAYLRTG VKIGEMPLTD SILCDGLTDA FHNCHMGITA ENVAKKWQVS REDQDKVAVL SQNRTENAQK AGHFDKEIVP VLVSTRKGLI EVKTDEFPRH GSNIEAMSKL KPYFLTDGTG TVTPANASGI NDGAAAVVLM KKSEADKRGL TPLARIVSWS QVGVEPSIMG IGPIPAIKQA VTKAGWSLED VDIFEINEAF AAVSAAIVKE LGLNPEKVNI EGGAIALGHP LGASGCRILV TLLHTLERMG RSRGVAALCI GGGMGIAMCV QR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CA10 HumanDescription:
Carbonic Anhydrase X Human Recombinant
Carbonic anhydrase-related protein 10, Carbonic anhydrase-related protein X, CA-RP X, CARP X, carbonic anhydrase X, Cerebral protein 15, hucep-15, epididymis secretory sperm binding protein, UNQ533/PRO1076.
Product # :
ENZ-1189Price :
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Description
CA10 Human Recombinant is a single, glycosylated polypeptide chain containing 317 amino acids (22-328a.a) and having a molecular mass of 36.3kDa (calculated). CA10 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
CA10 protein solution (0.5mg/ml) is filtered in Phosphate-Buffered Saline pH 7.4 and 10% (w/v) glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 150 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1pmole of pnitrophenyl acetate to p-nitrophenol per minute at pH8.0 at 37℃.
More Info
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Synonyms
Carbonic anhydrase-related protein 10, Carbonic anhydrase-related protein X, CA-RP X, CARP X, carbonic anhydrase X, Cerebral protein 15, hucep-15, epididymis secretory sperm binding protein, UNQ533/PRO1076.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
DGSMQQNSPK IHEGWWAYKE VVQGSFVPVP SFWGLVNSAW NLCSVGKRQS PVNIETSHMI FDPFLTPLRI NTGGRKVSGT MYNTGRHVSL RLDKEHLVNI SGGPMTYSHR LEEIRLHFGS EDSQGSEHLL NGQAFSGEVQ LIHYNHELYT NVTEAAKSPN GLVVVSIFIK VSDSSNPFLN RMLNRDTITR ITYKNDAYLL QGLNIEELYP ETSSFITYDG SMTIPPCYET ASWIIMNKPV YITRMQMHSL RLLSQNQPSQ IFLSMSDNFR PVQPLNNRCI RTNINFSLQG KDCPNNRAQK LQYRVNEWLL KHHHHHH
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Background
Carbonic anhydrases (CAs) are a family of enzymes that play a crucial role in regulating pH balance and carbon dioxide transport in various tissues and organs. Carbonic anhydrase X (CA10) is a less-studied member of this family, and this research aims to explore its structure, function, and implications in metabolism and disease. Understanding the molecular mechanisms and regulatory roles of CA10 can provide valuable insights into its potential as a therapeutic target for various disorders.
Structure and Expression of Carbonic Anhydrase X:
CA10, also known as mitochondrial carbonic anhydrase, is a membrane-associated protein predominantly found in the mitochondria of various tissues, including the liver, kidney, and brain. It possesses the characteristic zinc-binding catalytic domain found in other CAs. However, CA10 has distinct features, including a unique N-terminal mitochondrial targeting sequence, suggesting its specific role within mitochondria.
Role of Carbonic Anhydrase X in Metabolism:
CA10 is involved in the regulation of pH and bicarbonate concentrations within the mitochondrial matrix, impacting mitochondrial metabolism. It catalyzes the reversible hydration of carbon dioxide to bicarbonate, facilitating the exchange of carbon dioxide between the mitochondria and the cytoplasm. This process is vital for maintaining acid-base homeostasis and efficient energy production through oxidative phosphorylation.
Implications of Carbonic Anhydrase X in Disease:
Emerging evidence suggests that CA10 may be implicated in various pathological conditions. Alterations in CA10 expression or activity have been associated with metabolic disorders, including obesity and diabetes. Furthermore, dysregulation of mitochondrial function and pH homeostasis, in which CA10 plays a role, have been linked to neurodegenerative diseases, cancer, and cardiovascular disorders. Elucidating the precise contributions of CA10 in these pathologies is an area of active investigation.
Therapeutic Potential of Carbonic Anhydrase X:
The unique properties and expression patterns of CA10 make it an intriguing target for therapeutic interventions. Modulating CA10 activity or expression could have implications in metabolic disorders, where the manipulation of mitochondrial function and pH regulation could offer therapeutic benefits. Developing selective inhibitors or activators of CA10 could be explored to regulate its enzymatic activity and modulate mitochondrial metabolism.
Challenges and Future Directions:
Although CA10 shows promise as a therapeutic target, several challenges remain. The elucidation of the precise regulatory mechanisms and signaling pathways involving CA10 within mitochondria is necessary for a comprehensive understanding of its function. Additionally, the development of specific modulators that selectively target CA10 without affecting other CAs or disrupting physiological processes is a critical consideration.
Conclusion:
The study of CA10 protein provides valuable insights into its distinct role in mitochondrial metabolism and disease pathogenesis. Understanding the molecular mechanisms and functional implications of CA10 opens avenues for the development of targeted therapies for metabolic disorders, neurodegenerative diseases, cancer, and cardiovascular disorders. Further research on CA10, its interactions, and its modulation in pathological conditions will contribute to the development of novel therapeutic interventions to improve patient outcomes.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HSA ProteinDescription:
HSA Human Protein
HSA, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
Product # :
PRO-354Price :
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Description
HSA contains 584 amino acid residues derived from the prototypicalHSA sequence.
Source
Human Serum.
Formulation
0.2gr/ml solution containing no additives.
Purity
Greater than 97.0% as determined by SDS-PAGE.
More Info
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Introduction
HSA is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted HSA. HSA is a soluble, monomeric protein which comprises about one-half of the blood serum protein. HSA functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. HSA is a globular unglycosylated serum protein of molecular weight 65,000. The human HSA gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood.
Suitable for use in biochemical, excipient (an inert substance used as a diluent or vehicle for a drug), culture media and chromatographic applications. -
Synonyms
HSA, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
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Physical Appearance
Sterile Filtered clear yellowish solution.
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Stability
HSA although stable at room temperature for 2 weeks should be stored at 4°C.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CES2E MouseDescription:
Carboxylesterase 2E Mouse Recombinant
9030624L02Rik, Ces5, Ces2e.
Product # :
ENZ-1141Price :
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Description
CES2E Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 541 amino acids ( 27-559 aa) and having a molecular mass of 60.5kDa.CES2E is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The CES2E solution (0.25 mg/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 > 30unit/mg, and is defined as the amount of enzyme that hydrolyze 1.0 umole of pnitrophenyl acetate to p-nitrophenol per minute at pH 7.5 at 25C˚.
More Info
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Introduction
Carboxylesterase 2E or CES2E is an enzyme that hydrolyzes various carboxylic acid esters. This enzyme can be found mainly in mammalian liver cells. CES2E is taking part in chemical reactions, especially in carboxylic ester and water catalyzation to alcohol & carboxylate.
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Synonyms
9030624L02Rik, Ces5, Ces2e.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
QDSASPIRNT HTGQVRGSLV HVKDTDIAVH TFLGIPFAKP PVGPLRFAPP EAPEPWSGVR DGTSHPNMCL QNDNLMGSED LKMMNLILPP ISMSEDCLYL NIYVPAHAHE GSNLPVMVWI HGGALTVGMA SMYDGSMLAA TEDVVVVAIQ YRLGVLGFFS TGDQHAKGNW GYLDQVAALR WVQQNIVHFG GNPDRVTIFG ESAGGTSVSS HVVSPMSQGL FHGAIMESGV AVLPDLISSS
SEMVHRIVAN LSGCAAVNSE TLMCCLRGKN EAEMLAINKV FKIIPGVVDG EFLPKHPQEL MASKDFHPVP SIIGINNDEY GWILPTIMDP AQKIEEITRK TLPAVLKSTA LKMMLPPECG DLLMEEYMGD TEDPETLQAQ FREMKGDFMF VIPALQVAHF QRSHAPVYFY EFQHRPSFFK DFRPPYVKAD HGDEIFLVFG YQFGNIKLPY TEEEEQLSRR IMKYWANFAR HGNPNSEGLP YWPVMDHDEQ YLQLDIQPSV GRALKARRLQ FWTKTLPQKI QELKGSQERH KELLEHHHHH H
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HK2 HumanDescription:
Hexokinase-2 Human Recombinant
Hexokinase-2, EC 2.7.1.1, HK2, Hexokinase type II, HK II, Muscle form hexokinase, HXK2, DKFZp686M1669.
Product # :
PKA-227Price :
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Description
HK2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 1-917) fused to a 20 His tag at the N-terminal encoding the sequence of 937 amino acids in total and having a molecular mass of 104.1 kDa.HXK2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) contains 20mM Tris-HCl pH8.0 and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is 3-4 units/ml obtained by measuring the increase of NADPH in absorbance at 340 nm resulting from the reduction of NADP. In the coupled mode, one unit will produce 1.0 umole of NADPH per minute as glucose is phosphorylated by ATP at pH 7.4 at 30C.More Info
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Introduction
Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Hexokinase 2 is the predominant form found in skeletal muscle. It localizes to the outer membrane of mitochondria. Expression of this gene is insulin-responsive, and studies in rat suggest that it is involved in the increased rate of glycolysis seen in rapidly growing cancer cells.
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Synonyms
Hexokinase-2, EC 2.7.1.1, HK2, Hexokinase type II, HK II, Muscle form hexokinase, HXK2, DKFZp686M1669.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MIASHLLAYF FTELNHDQVQ KVDQYLYHMR LSDETLLEIS KRFRKEMEKG LGATTHPTAA VKMLPTFVRS TPDGTEHGEF LALDLGGTNF RVLWVKVTDN GLQKVEMENQ IYAIPEDIMR GSGTQLFDHI AECLANFMDK LQIKDKKLPL GFTFSFPCHQTKLDESFLVS WTKGFKSSGV EGRDVVALIR KAIQRRGDFD IDIVAVVNDT VGTMMTCGYD DHNCEIGLIV GTGSNACYME EMRHIDMVEG DEGRMCINME WGAFGDDGSL NDIRTEFDQE IDMGSLNPGK QLFEKMISGM YMGELVRLIL VKMAKEELLF GGKLSPELLN TGRFETKDISDIEGEKDGIR KAREVLMRLG LDPTQEDCVA THRICQIVST RSASLCAATL AAVLQRIKENKGEERLRSTI GVDGSVYKKH PHFAKRLHKT VRRLVPGCDV RFLRSEDGSG KGAAMVTAVAYRLADQHRAR QKTLEHLQLS HDQLLEVKRR MKVEMERGLS KETHASAPVK MLPTYVCATPDGTEKGDFLA LDLGGTNFRV LLVRVRNGKW GGVEMHNKIY AIPQEVMHGT GDELFDHIVQ CIADFLEYMG MKGVSLPLGF TFSFPCQQNS LDESILLKWT KGFKASGCEG EDVVTLLKEA IHRREEFDLD VVAVVNDTVG TMMTCGFEDP HCEVGLIVGT GSNACYMEEM RNVELVEGEE GRMCVNMEWG AFGDNGCLDD FRTEFDVAVD ELSLNPGKQR FEKMISGMYL GEIVRNILID FTKRGLLFRG RISERLKTRG IFETKFLSQI ESDCLALLQV RAILQHLGLE STCDDSIIVK EVCTVVARRA AQLCGAGMAA VVDRIRENRG LDALKVTVGV DGTLYKLHPH FAKVMHETVK DLAPKCDVSF LQSEDGSGKG AALITAVACR IREAGQR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TGM2 Human, Sf9Description:
Tissue Transglutaminase Human Recombinant, Sf9
Protein-glutamine gamma-glutamyltransferase 2, EC 2.3.2.13, Tissue transglutaminase, TGase C, TGC, TG(C), Transglutaminase-2, TGase-H, TG2, TGM2.
Product # :
ENZ-303Price :
Quantity :
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Description
Tissue Transglutaminase Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a molecular mass of 83 kDa. tTG is expressed with a -6xHis tag and purified by proprietary chromatographic techniques. By point mutation of the active center the catalytic transglutaminase activity has been eliminated, resulting in increased stability during storage and coating.
Source
Sf9 insect cells.
Formulation
TGM2 is supplied in 16mM HEPES buffer pH-8.0, 320mM NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Celiac disease is an enteropathy that is characterized by intestinal lesions of variable severity. Tissue-type transglutaminase (tTG) is believed to be the predominant autoantigen for celiac disease and the corresponding autoantibodies show higher sensitivity and specificity than anti-gliadin antibodies. Highly pure recombinant human tTG is now available to replace the traditionally used tTG fraction from guinea pig.
Tissue-type transglutaminase antigens have been specifically modified for improved handling: exchange of an active site amino acid eliminates the protein cross-linking activity of the enzyme, while maintaining the native three-dimensional structure and the enzyme's secondary GTPase activity. This engineering assures reproducible properties of the antigen preparations through the absence of variable and ill-defined covalent aggregates of tTG antigen and host cell proteins. -
Synonyms
Protein-glutamine gamma-glutamyltransferase 2, EC 2.3.2.13, Tissue transglutaminase, TGase C, TGC, TG(C), Transglutaminase-2, TGase-H, TG2, TGM2.
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Stability
Store at 4°C if entire vial will be used within 2-4weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
UGP2 HumanDescription:
UDP-Glucose Pyrophosphorylase 2 Human Recombinant
UDP-Glucose Pyrophosphorylase 2,UDP-Glucose Pyrophosphorylase 1, EC 2.7.7.9, UGPP2, UDPGP, UGP1, UTP--Glucose-1-Phosphate Uridylyltransferase 2Uridyl Diphosphate Glucose Pyrophosphorylase-1, Uridyl Diphosphate Glucose Pyrophosphorylase 2, UTP--Glucose-1-Phosphate Uridylyltransferase , UTP-Glucose-1-Phosphate, Uridyltransferase, UDP-Glucose Pyrophosphorylase , UDP-Glucose Diphosphorylase, UGPase 2, UDPGP2, PHC379, UGPase, UGPP1, UDPG.
Product # :
ENZ-832Price :
Quantity :
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Description
UGP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 531 amino acids (1-508 a.a) and having a molecular mass of 59.3kDa.UGP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UGP2 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4) 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
UDP-Glucose Pyrophosphorylase 2, also known as UGP2 is an essential intermediary in mammalian carbohydrate inter conversions. UGP2 transfers a glucose moiety from glucose-1-phosphate to MgUTP and forms UDP-glucose and MgPPi. UDP-glucose is a direct precursor of glycogen in the liver and muscle tissue, moreover in lactating mammary gland it is converted to UDP-galactose which is next converted to lactose.
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Synonyms
UDP-Glucose Pyrophosphorylase 2,UDP-Glucose Pyrophosphorylase 1, EC 2.7.7.9, UGPP2, UDPGP, UGP1, UTP--Glucose-1-Phosphate Uridylyltransferase 2Uridyl Diphosphate Glucose Pyrophosphorylase-1, Uridyl Diphosphate Glucose Pyrophosphorylase 2, UTP--Glucose-1-Phosphate Uridylyltransferase , UTP-Glucose-1-Phosphate, Uridyltransferase, UDP-Glucose Pyrophosphorylase , UDP-Glucose Diphosphorylase, UGPase 2, UDPGP2, PHC379, UGPase, UGPP1, UDPG.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSRFVQD LSKAMSQDGA SQFQEVIRQE LELSVKKELE KILTTASSHE FEHTKKDLDG FRKLFHRFLQ EKGPSVDWGK IQRPPEDSIQ PYEKIKARGL PDNISSVLNK LVVVKLNGGL GTSMGCKGPK SLIGVRNENT FLDLTVQQIE HLNKTYNTDV PLVLMNSFNT DEDTKKILQK YNHCRVKIYT FNQSRYPRIN KESLLPVAKD VSYSGENTEA WYPPGHGDIY ASFYNSGLLD TFIGEGKEYI FVSNIDNLGA TVDLYILNHL MNPPNGKRCE FVMEVTNKTR ADVKGGTLTQ YEGKLRLVEI AQVPKAHVDE FKSVSKFKIF NTNNLWISLA AVKRLQEQNA IDMEIIVNAK TLDGGLNVIQ LETAVGAAIK SFENSLGINV PRSRFLPVKT TSDLLLVMSN LYSLNAGSLT MSEKREFPTV PLVKLGSSFT KVQDYLRRFE SIPDMLELDH LTVSGDVTFG KNVSLKGTVI IIANHGDRID IPPGAVLENK IVSGNLRILD H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PCSK9 HumanDescription:
Proprotein Convertase Subtilisin/Kexin Type 9 Human Recombinant
Proprotein Convertase Subtilisin/Kexin Type 9, NARC1, Subtilisin/Kexin-Like Protease PC9, HCHOLA3, LDLCQ1, NARC-1, FH3, PC9, Convertase Subtilisin/Kexin Type 9 Preproprotein, Hypercholesterolemia, Autosomal Dominant 3, Neural Apoptosis Regulated Convertase 1, Neural Apoptosis-Regulated Convertase 1, Proprotein Convertase 9, EC 3.4.21.111, EC 3.4.21, EC 3.4.21, PCSK9.
Product # :
PRO-2043Price :
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Description
PCSK9 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Gln31-Gln692) containing a total of 672 amino acids, having a calculated molecular mass of 72.4kDa and fused to a 10 aa His tag at C-Terminus.
Source
HEK 293.
Formulation
PCSK9 filtered (0.4µm) solution at a concentration of 0.25-0.7mg/ml in phosphate buffered saline and 20 % (w/v) glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Proprotein Convertase Subtilisin/Kexin Type 9 (PCSK9) belongs to the subtilisin-like proprotein convertase family, which includes proteases that process protein and peptide precursors trafficking via regulated or constitutive branches of the secretory pathway. PCSK9 protein goes through an autocatalytic processing event with its prosegment in the ER and is constitutively secreted as an inactive protease into the extracellular matrix and trans-Golgi network. PCSK9 is expressed in the liver, intestine and kidney tissues and escorts specific receptors for lysosomal degradation. PCSK has a role in cholesterol and fatty acid metabolism. PCSK9 gene mutations are linked with autosomal dominant familial hypercholesterolemia.
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Synonyms
Proprotein Convertase Subtilisin/Kexin Type 9, NARC1, Subtilisin/Kexin-Like Protease PC9, HCHOLA3, LDLCQ1, NARC-1, FH3, PC9, Convertase Subtilisin/Kexin Type 9 Preproprotein, Hypercholesterolemia, Autosomal Dominant 3, Neural Apoptosis Regulated Convertase 1, Neural Apoptosis-Regulated Convertase 1, Proprotein Convertase 9, EC 3.4.21.111, EC 3.4.21, EC 3.4.21, PCSK9.
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Physical Appearance
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
QEDEDGDYEE LVLALRSEED GLAEAPEHGT TATFHRCAKD PWRLPGTYVV VLKEETHLSQ SERTARRLQA QAARRGYLTK ILHVFHGLLP GFLVKMSGDL LELALKLPHV DYIEEDSSVF AQSIPWNLER ITPPRYRADE YQPPDGGSLV EVYLLDTSIQ SDHREIEGRV MVTDFENVPE EDGTRFHRQA SKCDSHGTHL AGVVSGRDAG VAKGASMRSL RVLNCQGKGT VSGTLIGLEF IRKSQLVQPV GPLVVLLPLA GGYSRVLNAA CQRLARAGVV LVTAAGNFRD DACLYSPASA PEVITVGATN AQDQPVTLGT LGTNFGRCVD LFAPGEDIIG ASSDCSTCFV SQSGTSQAAA HVAGIAAMML SAEPELTLAE LRQRLIHFSA KDVINEAWFP EDQRVLTPNL VAALPPSTHG AGWQLFCRTV WSAHSGPTRM ATAVARCAPD EELLSCSSFS RSGKRRGERM EAQGGKLVCR AHNAFGGEGV YAIARCCLLP QANCSVHTAP PAEASMGTRV HCHQQGHVLT GCSSHWEVED LGTHKPPVLR PRGQPNQCVG HREASIHASC CHAPGLECKV KEHGIPAPQE QVTVACEEGW TLTGCSALPG TSHVLGAYAV DNTCVVRSRD VSTTGSTSEG AVTAVAICCR SRHLAQASQE LQHHHHHHHH 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 :
DCTD HumanDescription:
dCMP Deaminase Human Recombinant
Deoxycytidylate deaminase, EC 3.5.4.12, dCMP Deaminase, DCTD, MGC111062.
Product # :
ENZ-538Price :
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Description
DCTD Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (1-178 a.a.) and having a molecular mass of 22.1 kDa. The DCTD is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DCTD solution (0.5mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT, 1mM EDTA & 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
DCTD is an allosteric enzyme that exists as a homohexamer and is part of the cytidine and deoxycytidylate deaminase protein family. DTCD uses zinc as a cofactor to catalyze the deamination of dCMP to dUMP, thus making the nucleotide substrate (dUMP) that is used by thymidylate synthase.
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Synonyms
Deoxycytidylate deaminase, EC 3.5.4.12, dCMP Deaminase, DCTD, MGC111062.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSEVSCKKRD DYLEWPEYFM AVAFLSAQRS KDPNSQVGAC IVNSENKIVG IGYNGMPNGC SDDVLPWRRT AENKLDTKYP YVCHAELNAI MNKNSTDVKG CSMYVALFPC NECAKLIIQA GIKEVIFMSD KYHDSDEATA ARLLFNMAGV TFRKFIPKCS KIVIDFDSIN SRPSQKLQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
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 :
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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.
More Info
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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.
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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.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
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.
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Name :
B3GAT3 HumanDescription:
Beta-1,3-Glucuronyltransferase 3 Human Recombinant
Beta-1,3-glucuronyltransferase 3, GLCATI, Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3, Glucuronosyltransferase I, GlcAT-I, GlcUAT-I, B3GAT3, UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase.
Product # :
ENZ-711Price :
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Description
B3GAT3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 330 amino acids (29-335 a.a) and having a molecular mass of 36.4kDa. B3GAT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
B3GAT3 protein solution (1mg/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
Beta-1,3-glucuronyltransferase 3 (B3GAT3) is involved in forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate. B3GAT3 has a part in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins. B3GAT3 shows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Gal beta1-O-benzyl, Galbeta1-4GlcNAc and Galbeta1-4Glc.
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Synonyms
Beta-1,3-glucuronyltransferase 3, GLCATI, Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3, Glucuronosyltransferase I, GlcAT-I, GlcUAT-I, B3GAT3, UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQPCDCLP PLRAAAEQLR QKDLRISQLQ AELRRPPPAP AQPPEPEALP TIYVVTPTYA RLVQKAELVR LSQTLSLVPR LHWLLVEDAE GPTPLVSGLL AASGLLFTHL VVLTPKAQRL REGEPGWVHP RGVEQRNKAL DWLRGRGGAV GGEKDPPPPG TQGVVYFADD DNTYSRELFE EMRWTRGVSV WPVGLVGGLR FEGPQVQDGR VVGFHTAWEP SRPFPVDMAG FAVALPLLLD KPNAQFDSTA PRGHLESSLL SHLVDPKDLE PRAANCTRVL VWHTRTEKPK MKQEEQLQRQ GRGSDPAIEV.
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 :
OGG1 HumanDescription:
8-Oxoguanine DNA Glycosylase Human Recombinant
HMMH, HOGG1, MUTM, OGH1, AP lyase.
Product # :
ENZ-253Price :
Quantity :
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Description
OGG1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 368 amino acids (1-345 a.a.) and having a molecular mass of 41.2 kDa. The OGG1 is fused to 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
0.5mg/ml solution containing PBS (pH-7.4) and 40% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
OGG1 is a DNA glycosylase enzyme which takes part in base excision repair. OGG1 protein is the main enzyme accountable for the excision of 7,8-dihydro-8-oxoguanine (8-oxoG), a mutagenic base byproduct which arises as a result of exposure to reactive oxygen species (ROS). OGG1 shows beta lyase activity that nicks DNA 3'' to the lesion.
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Synonyms
HMMH, HOGG1, MUTM, OGH1, AP lyase.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH TGSMPARALL PRRMGHRTLA STPALWASIP CPRSELRLDL VLPSGQSFRW REQSPAHWSG VLADQVWTLT QTEEQLHCTV YRGDKSQASR PTPDELEAVR KYFQLDVTLA QLYHHWGSVD SHFQEVAQKF QGVRLLRQDP IECLFSFICS SNNNIARITG MVERLCQAFG PRLIQLDDVT YHGFPSLQAL AGPEVEAHLR KLGLGYRARY VSASARAILE EQGGLAWLQQ LRESSYEEAH KALCILPGVG TKVADCICLM ALDKPQAVPV DVHMWHIAQRDYSWHPTTSQ AKGPSPQTNK ELGNFFRSLW GPYAGWAQAV LFSADLRQCR HAQEPPAKRRKGSKGPEG.
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 :
HAAO HumanDescription:
3-Hydroxyanthranilate 3,4-Dioxygenase Human Recombinant
3-hydroxyanthranilate 3,4-dioxygenase, 3-hydroxyanthranilate oxygenase, 3-HAO, 3-hydroxyanthranilic acid dioxygenase, HAD, HAAO, HAO.
Product # :
ENZ-617Price :
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Description
HAAO Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 310 amino acids (1-286 a.a.) and having a molecular mass of 35kDa.HAAO is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HAAO protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
HAAO is a monomeric cytosolic protein which is a member of intramolecular dioxygenases family containing nonheme ferrous iron. The HAAO protein catalyzes the synthesis of quinolinic acid (QUIN) from 3-hydroxyanthranilic acid. QUIN is an excitotoxin whose toxicity is facilitated by its ability to activate glutamate N-methyl-D-aspartate receptors. Amplified cerebral levels of QUIN may contribute to the pathogenesis of neurologic and inflammatory disorders. HAAO is widely distributed in peripheral organs, such as liver and kidney, and is also present in low amounts in the central nervous system.
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Synonyms
3-hydroxyanthranilate 3,4-dioxygenase, 3-hydroxyanthranilate oxygenase, 3-HAO, 3-hydroxyanthranilic acid dioxygenase, HAD, HAAO, HAO.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMERRLG VRAWVKENRG SFQPPVCNKL MHQEQLKVMF IGGPNTRKDY HIEEGEEVFY QLEGDMVLRV LEQGKHRDVV IRQGEIFLLP ARVPHSPQRF ANTVGLVVER RRLETELDGL RYYVGDTMDV LFEKWFYCKD LGTQLAPIIQ EFFSSEQYRT GKPIPDQLLK EPPFPLSTRS IMEPMSLDAW LDSHHRELQA GTPLSLFGDT YETQVIAYGQ GSSEGLRQNV DVWLWQLEGS SVVTMGGRRL SLAPDDSLLV LAGTSYAWER TQGSVALSVT QDPACKKPLG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UBE2L6 HumanDescription:
Ubiquitin Conjugating Enzyme E2L 6 Human Recombinant
RIG-B, UBCH8, MGC40331, UBE2L6, Ubiquitin/ISG15-conjugating enzyme E2 L6, Ubiquitin-protein ligase L6, Ubiquitin carrier protein L6, Retinoic acid-induced gene B protein.
Product # :
ENZ-347Price :
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Description
UBE2L6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-152 a.a.) & having a molecular mass of 21.7 kDa. The UBE2L6 is fused to a 36 amino acid His Tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein contains 20mM Tris pH-8, 0.1mM PMSF, 1mM DTT, and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
UBE2L6 belongs to the E2 ubiquitin-conjugating enzyme family. UBE2L6 enzyme is very similar in its primary structure to the enzyme encoded by UBE2L3 gene. UBE2L6 catalyzes the covalent attachment of ubiquitin to other proteins. UBE2L6 functions in the e6/e6-ap-induced ubiquitination of p53/tp53.
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Synonyms
RIG-B, UBCH8, MGC40331, UBE2L6, Ubiquitin/ISG15-conjugating enzyme E2 L6, Ubiquitin-protein ligase L6, Ubiquitin carrier protein L6, Retinoic acid-induced gene B protein.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMASM RVVKELEDLQ KKPPPYLRNL SSDDANVLVW HALLLPDQPP YHLKAFNLRI SFPPEYPFKP PMIKFTTKIY HPNVDENGQI CLPIISSENW KPCTKTCQVL EALNVLVNRP NIREPLRMDL ADLLTQNPEL FRKNAEEFTL RFGVDRPS.
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 :
PSMA4 HumanDescription:
Proteasome Subunit Alpha Type 4 Human Recombinant
Proteasome subunit alpha type-4, Macropain subunit C9, Multicatalytic endopeptidase complex subunit C9, Proteasome component C9, Proteasome subunit L, PSMA4, HC9, PSC9, HsT17706.
Product # :
ENZ-222Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PSMA4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 285 amino acids (1-261) and having a molecular mass of 32kDa.PSMA4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The PSMA4 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Proteasome subunit alpha type 4 (PSMA4) belongs to the peptidase T1A family, which is a 20S core alpha subunit. The proteasome is a multicatalytic proteinase complex with an extremely ordered ring-shaped 20S core structure. The core structure is comprised of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. PSMA4 is dispersed throughout eukaryotic cells at a high concentration and cleaves peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway.
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Synonyms
Proteasome subunit alpha type-4, Macropain subunit C9, Multicatalytic endopeptidase complex subunit C9, Proteasome component C9, Proteasome subunit L, PSMA4, HC9, PSC9, HsT17706.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSRRYD SRTTIFSPEG RLYQVEYAME AIGHAGTCLG ILANDGVLLA AERRNIHKLL DEVFFSEKIY KLNEDMACSV AGITSDANVL TNELRLIAQR YLLQYQEPIP CEQLVTALCD IKQAYTQFGG KRPFGVSLLY IGWDKHYGFQ LYQSDPSGNY GGWKATCIGN NSAAAVSMLK QDYKEGEMTL KSALALAIKV LNKTMDVSKL SAEKVEIATL TRENGKTVIR VLKQKEVEQL IKKHEEEEAK AEREKKEKEQ KEKDK.
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 :
UFC1 HumanDescription:
Ubiquitin Fold Modifier Conjugating Enzyme 1 Human Recombinant
Ubiquitin-fold modifier-conjugating enzyme 1, Ufm1-conjugating enzyme 1, UFC1, CGI-126, HSPC155.
Product # :
ENZ-138Price :
Quantity :
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Shipped with Ice Packs
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Description
UFC1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (1-167 a.a.) and having a molecular mass of 21.6kDa.UFC1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UFC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
UFC1 is a member of the ubiquitin-conjugating enzyme family. UFC1 is an E2-like conjugating enzyme for ubiquitin-fold modifier-1. UFM1 is activated by UBA5 (a novel E1-like enzyme) by forming a high-energy thioester bond. Activated UFM1 is subsequently transferred to its cognate E2-like enzyme, UFC1, in a similar thioester linkage.
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Synonyms
Ubiquitin-fold modifier-conjugating enzyme 1, Ufm1-conjugating enzyme 1, UFC1, CGI-126, HSPC155.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
UFC1 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MADEATRRVV SEIPVLKTNA GPRDRELWVQ RLKEEYQSLI RYVENNKNAD NDWFRLESNK EGTRWFGKCW YIHDLLKYEF DIEFDIPITY PTTAPEIAVP ELDGKTAKMY RGGKICLTDH FKPLWARNVP KFGLAHLMAL GLGPWLAVEI PDLIQKGVIQ HKEKCNQ.
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 :
COAA E.ColiDescription:
Pantothenate Kinase E.Coli Recombinant
PanK, ts-9, rts.
Product # :
PKA-022Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
COAA E.Coli Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (1-316) and having a molecular mass of 38.9kDa.COAA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The COAA solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
COAA is a member of the prokaryotic pantothenate kinase family and it is the first enzyme in the Coenzyme A biosynthetic pathway. COAA phosphorylates pantothenate (vitamin B5) to form 4'-phosphopantothenate. The key factor controlling the intracellular CoA concentration is the regulation of COAA activity by feedback inhibition.
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Synonyms
PanK, ts-9, rts.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSIKEQ TLMTPYLQFD RNQWAALRDS VPMTLSEDEI ARLKGINEDL SLEEVAEIYL PLSRLLNFYI SSNLRRQAVL EQFLGTNGQR IPYIISIAGS VAVGKSTTAR VLQALLSRWP EHRRVELITT DGFLHPNQVL KERGLMKKKG FPESYDMHRL VKFVSDLKSG VPNVTAPVYS HLIYDVIPDG DKTVVQPDIL ILEGLNVLQS GMDYPHDPHH VFVSDFVDFS IYVDAPEDLL QTWYINRFLK FREGAFTDPD SYFHNYAKLT KEEAIKTAMT LWKEINWLNL KQNILPTRER ASLILTKSAN HAVEEVRLRK.
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 MouseDescription:
Folate Hydrolase 1 Mouse Recombinant
Folh1, GCP2, mopsm, Glutamate carboxypeptidase 2, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Naalad1.
Product # :
ENZ-957Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FOLH1 Mouse Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 717 amino acids (45-752a.a) and having a molecular mass of 80.5kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions). FOLH1 is fused to a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The FOLH1 solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Folate Hydrolase 1 (Folh1) is a single pass type 2 membrane protein which is expressed mainly in prostate epithelium. Folh1 which is a part of the peptidase M28 family and M28B subfamily has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase activity. Folh1 can be found in urinary bladder, kidney, testis, ovary, stomach, small intestine colon, and the capillary endothelium of various tumors. Therefore, Folh1 plays a role in directed imaging and therapy of recurrent of metastatic disease.
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Synonyms
Folh1, GCP2, mopsm, Glutamate carboxypeptidase 2, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Naalad1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPKPSNEAT GNVSHSGMKK EFLHELKAEN IKKFLYNFTR TPHLAGTQNN FELAKQIHDQ WKEFGLDLVE LSHYDVLLSY PNKTHPNYIS IINEDGNEIF KTSLSEQPPP GYENISDVVP PYSAFSPQGT PEGDLVYVNY ARTEDFFKLE REMKISCSGK IVIARYGKVF RGNMVKNAQL AGAKGMILYS DPADYFVPAV KSYPDGWNLP GGGVQRGNVL NLNGAGDPLT PGYPANEHAY RHELTNAVGL PSIPVHPIGY DDAQKLLEHM GGPAPPDSSW KGGLKVPYNV GPGFAGNFST QKVKMHIHSY TKVTRIYNVI GTLKGALEPD RYVILGGHRD AWVFGGIDPQ SGAAVVHEIV RSFGTLKKKG RRPRRTILFA SWDAEEFGLL GSTEWAEEHS RLLQERGVAY INADSSIEGN YTLRVDCTPL MYSLVYNLTK ELQSPDEGFE GKSLYDSWKE KSPSPEFIGM PRISKLGSGN DFEVFFQRLG IASGRARYTK NWKTNKVSSY PLYHSVYETY ELVVKFYDPT FKYHLTVAQV RGAMVFELAN SIVLPFDCQS YAVALKKYAD TIYNISMKHP QEMKAYMISF DSLFSAVNNF TDVASKFNQR LQELDKSNPI LLRIMNDQLM YLERAFIDPL GLPGRPFYRH IIYAPSSHNK YAGESFPGIY DALFDISSKV NASKAWNEVK RQISIATFTV QAAAETLREV 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 :
ACP1 HumanDescription:
Acid Phosphatase-1 Human Recombinant
HAAP, MGC3499, MGC111030, ACP1, Low molecular weight phosphotyrosine protein phosphatase, LMW-PTPase, LMW-PTP, Low molecular weight cytosolic acid phosphatase, Red cell acid phosphatase 1, Adipocyte acid phosphatase.
Product # :
ENZ-408Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human ACP1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 178 amino acids (1-158 a.a.) and having a molecular mass of 20.1 kDa. ACP1 is fused to a 20 amino acid His-Tag at N-Terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The ACP1 protein solution contains 20mM MES, pH-6, 0.1mM PMSF, 2mM EDTA and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ACP1 is part of the phosphotyrosine protein. ACP1 functions as an acid phosphatase and a protein tyrosine phosphatase (PTPase) existing in all human tissues, including adipocytes. ACP1 enzyme hydrolyzes protein tyrosine phosphate to protein tyrosine and orthophosphate, and also orthophosphoric monoesters to alcohol and orthophosphate. ACP1 is present in adipocytes, thus playing a specific role in the regulation of adipose tissue. High levels of the ACP1 negatively regulate cell proliferation and growth of leiomyomas during dephosphorylation of the PDGF receptor. High significant differences in birth weight-placental weight relationships were observed among acid phosphatase locus 1 phenotypes.
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Synonyms
HAAP, MGC3499, MGC111030, ACP1, Low molecular weight phosphotyrosine protein phosphatase, LMW-PTPase, LMW-PTP, Low molecular weight cytosolic acid phosphatase, Red cell acid phosphatase 1, Adipocyte acid phosphatase.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAEQATKSVL FVCLGNICRS PIAEAVFRKL VTDQNISENW VIDSGAVSDW NVGRSPDPRA VSCLRNHGIHTAHKARQITK EDFATFDYIL CMDESNLRDL NRKSNQVKTC KAKIELLGSY DPQKQLIIED PYYGNDSDFE TVYQQCVRCC RAFLEKAH.
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Unit Definition
One unit is defined as the amount of enzyme that will hydrolyze 1nmole of p-nitrophenyl phosphate per minute at 37°C in MES pH5.0 using 10mM of substrate.
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Specific Activity
> 15,000 Units per 1mg protein.
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.