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1000 results found for “Beta Lactamase”
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Name :
ATP1B1 Human, Sf9Description:
ATPase Transporting Beta 1 Human Recombinant, Sf9
Sodium/potassium-transporting ATPase subunit beta-1, ATPase, Na+/K+ transporting, beta 1 polypeptide, ATP1B, ATPBS, Sodium/potassium-dependent ATPase subunit beta-1, ATP1B1, ATPaseTransporting Beta 1.
Product # :
PRO-2385Price :
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Description
ATP1B1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 250 amino acids (63-303 a.a.) and having a molecular mass of 29kDa (Molecular size on SDS-PAGE will appear at approximately 28-40 kDa).ATP1B1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ATP1B1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ATPase Transporting Beta 1 (ATP1B1) is a part of the family of Na+/K+ and H+/K+ ATPases beta chain proteins, and the subfamily of Na+/K+ -ATPases. Na+/K+ -ATPase is an essential membrane protein accountable for establishing and maintaining the electrochemical gradients of Na and K ions over the plasma membrane. These gradients are vital for osmoregulation, for sodium-coupled transport of a range of organic and inorganic molecules, and for electrical excitability of muscle and nerve. ATP1B1is combined of 2 subunits, a large catalytic subunit (alpha) and a smaller glycoprotein subunit (beta). The beta subunit regulates the number of sodium pumps transported to the plasma membrane through assembly of alpha/beta heterodimers. ATP1B1 is a beta 1 subunit.
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Synonyms
Sodium/potassium-transporting ATPase subunit beta-1, ATPase, Na+/K+ transporting, beta 1 polypeptide, ATP1B, ATPBS, Sodium/potassium-dependent ATPase subunit beta-1, ATP1B1, ATPaseTransporting Beta 1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPEFKPTYQ DRVAPPGLTQ IPQIQKTEIS FRPNDPKSYE AYVLNIVRFL EKYKDSAQRD DMIFEDCGDV PSEPKERGDF NHERGERKVC RFKLEWLGNC SGLNDETYGY KEGKPCIIIK LNRVLGFKPK PPKNESLETY PVMKYNPNVL PVQCTGKRDE DKDKVGNVEY FGLGNSPGFP LQYYPYYGKL LQPKYLQPLL AVQFTNLTMD TEIRIECKAY GENIGYSEKD RFQGRFDVKI EVKSHHHHHH.
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 :
EBI3 HumanDescription:
Epstein Barr Virus Induced 3 Human Recombinant
Interleukin-27 subunit beta, IL-27 subunit beta, IL-27B, Epstein-Barr virus-induced gene 3 protein, EBV-induced gene 3 protein, EBI3, IL27B.
Product # :
CYT-367Price :
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Shipped at Room temp
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Description
EBI3 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 209 amino acids fragment (21-229) having a molecular weight of 23.3kDa. The EBI3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EBI3 Human Recombinant was lyophilized from a solution containing 10mM Acetic Acid and 0.5% Mannitol.
Purity
Greater than 90% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Assay data for Human recombinant EBI3 is based upon qualitative binding to anti-EBI3 antibody.Citations
More Info
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Introduction
EBI3 has an induced expression in B lymphocytes in reaction to Epstein-Barr virus infection. EBI3 encodes a secreted glycoprotein belonging to the hematopoietin receptor family, and heterodimerizes with a 28 kDa protein to form iIL-27. EBI3 drives rapid clonal expansion of naive cd4(+) t-cells. EBI3 strongly synergizes with IL-12 to activate IFN-gamma production of naive cd4(+) t-cells. EBI3 mediates its biologic effects through the cytokine receptor wsx-1/tccr.
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Synonyms
Interleukin-27 subunit beta, IL-27 subunit beta, IL-27B, Epstein-Barr virus-induced gene 3 protein, EBV-induced gene 3 protein, EBI3, IL27B.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EBI3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EBI3 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized EBI3 in sterile 10mM Acetic acid not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
RKGPPAALTLPRVQCRASRYPIAVDCSWTLPPAPNSTSPVSF
IATYRLGMAARGHSWPCLQQTPTSTSCTITDVQLFSMAPYVL
NVTAVHPWGSSSSFVPFITEHIIKPDPPEGVRLSPLAERQLQ
VQWEPPGSWPFPEIFSLKYWIRYKRQGAARFHRVGPIEATSF
ILRAVRPRARYYVQVAAQDLTDYGELSDWSLPATATMSLGK. -
Background
Title: Epstein-Barr Virus Induced 3 Human Recombinant: Unveiling its Role in Epstein-Barr Virus-Associated Diseases
Abstract:
Epstein-Barr Virus Induced 3 (EBI3) is a crucial cytokine involved in the immune response against Epstein-Barr virus (EBV) and various other pathogens. This research paper provides an extensive analysis of human recombinant EBI3, focusing on its production, characterization, and potential applications in understanding EBV-associated diseases. The paper highlights the significance of EBI3 in modulating immune responses and explores its role in the pathogenesis of EBV-related malignancies. Furthermore, it discusses ongoing research and clinical trials investigating the therapeutic potential of recombinant EBI3 in immune disorders and cancer. The information presented in this paper aims to enhance our understanding of human recombinant EBI3 and its utility as a research tool and a potential immunotherapeutic agent.Introduction:
Epstein-Barr Virus Induced 3 (EBI3) is a cytokine that plays a critical role in the immune response against EBV. Human recombinant EBI3, produced through genetic engineering techniques, provides a valuable tool for studying its immunomodulatory properties and exploring its potential therapeutic applications.Production and Characterization:
Recombinant EBI3 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant EBI3.Role in EBV-Associated Diseases:
EBI3 is involved in the regulation of immune responses during EBV infection. It acts as a subunit of the heterodimeric cytokine interleukin-27 (IL-27), which plays a crucial role in anti-viral immunity. Recombinant EBI3 serves as a valuable tool for investigating the mechanisms underlying EBI3-mediated immune regulation and its potential implications in EBV-associated diseases, including infectious mononucleosis, nasopharyngeal carcinoma, and EBV-related lymphomas.Therapeutic Implications:
Dysregulation of the immune response is implicated in various immune disorders and cancers. Recombinant EBI3 holds promise as a potential immunotherapeutic agent due to its immunomodulatory properties. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant EBI3 in conditions such as autoimmune diseases, viral infections, and cancer.Conclusion:
Human recombinant EBI3 represents a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in understanding EBV-associated diseases contribute to our understanding of immune regulation and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant EBI3 offer promising avenues for improving outcomes in immune disorders and EBV-related malignancies.What is the molecular weight/Mw of EBI3 Protein?
EBI3 Protein has a total Mw of 23.3kDa.
What is the source or expression system of EBI3 Protein?
Escherichia Coli.
What is the Purity of EBI3 Protein?
EBI3 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of EBI3 Protein?
Assay data for Human recombinant EBI3 is based upon qualitative binding to anti-EBI3 antibody.
What is the amino acid sequence of EBI3 Protein?
RKGPPAALTLPRVQCRASRYPIAVDCSWTLPPAPNSTSPVSF
IATYRLGMAARGHSWPCLQQTPTSTSCTITDVQLFSMAPYVL
NVTAVHPWGSSSSFVPFITEHIIKPDPPEGVRLSPLAERQLQ
VQWEPPGSWPFPEIFSLKYWIRYKRQGAARFHRVGPIEATSF
ILRAVRPRARYYVQVAAQDLTDYGELSDWSLPATATMSLGK.
What applications can EBI3 Protein be used in?
EBI3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EBI3 Protein?
The endotoxin level is minimal, EBI3 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Y.Enterocolitica (O:9) YopMDescription:
Yersinia Enterocolitica (O:9) YopM Recombinant
Product # :
PRO-2273Price :
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Description
Recombinant Yersinia Enterocolitica (O:9) YopM produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 42,703 Dalton. Y.Enterocolitica (O:9) YopM is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Y.Enterocolitica (O:9) YopM is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Yersinia enterocolitica is a Gram-negative bacillus-shaped bacterium, which is a member of the Enterobacteriaceae family. Y.Enterocolitica is motile at temperatures between 22-29°C, however becomes non-motile at normal human body temperature. Y. Enterocolitica infection causes the yersiniosis disease, which is an animal-borne disease occurring in humans, as well as in a various groups of animals such as cattle, deer, pigs, and birds. Yersinia enterocolitica is a heterogeneous group of strains, which are conventionally classified by bio-typing into six bio-groups on the basis of phenotypic characteristics, and by serotyping into more than 57 “O” serogroups, on the basis of their O (lipopolysaccharide or LPS) surface antigen. Five of the six biogroups (1B and 2–5) are considered as pathogens. Nevertheless, only a few of these serogroups have been linked with disease in either humans or animals. Strains which belong to serogroups O:3 (biogroup 4), O:5,27 (biogroups 2 and 3), O:8 (biogroup 1B), and O:9 (biogroup 2) are most frequently isolated worldwide from human samples. Still, the main Y. enterocolitica serogroup in many European countries is serogroup O:3 followed by O:9, whereas the serogroup O:8 is mostly detected in the United States.
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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. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG- and IgM- and IgA-type human antibodies.2. Immunodot test with positive/negative sera panels.
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 :
PSMB4 HumanDescription:
Proteasome Subunit Beta Type 4 Human Recombinant
Proteasome (prosome, macropain) subunit beta type 4, PROS26, HN3, Macropain beta chain, Multicatalytic endopeptidase complex beta chain, Proteasome chain 3, 26 kDa prosomal protein, HsN3, PROS-26, hsBPROS26, EC 3.4.25.1.
Product # :
ENZ-197Price :
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Description
PSMB4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (46-264 a.a.) and having a molecular mass of 26.6kDa.PSMB4 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PSMB4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 30% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
PSMB4 is a member of the peptidase T1B family. The 20S Proteasome chamber holds structural alpha subunits and predominantly catalytic beta subunits. The two external rings in the proteasome contain seven alpha subunits each and the two internal rings contain of seven beta subunits each. PSMB4 is a beta subunit of the 20S Proteasome that is spread all over the eukaryotic cells in large quantities and cleaves peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway.
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Synonyms
Proteasome (prosome, macropain) subunit beta type 4, PROS26, HN3, Macropain beta chain, Multicatalytic endopeptidase complex beta chain, Proteasome chain 3, 26 kDa prosomal protein, HsN3, PROS-26, hsBPROS26, EC 3.4.25.1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTQNPMVTGT SVLGVKFEGG VVIAADMLGS YGSLARFRNI SRIMRVNNST MLGASGDYAD FQYLKQVLGQ MVIDEELLGD GHSYSPRAIH SWLTRAMYSR RSKMNPLWNT MVIGGYADGE SFLGYVDMLG VAYEAPSLAT GYGAYLAQPL LREVLEKQPV LSQTEARDLV ERCMRVLYYR DARSYNRFQI ATVTEKGVEI EGPLSTETNW DIAHMISGFE
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
P4HB Human, ActiveDescription:
Prolyl 4-Hydroxylase Beta Human Recombinant, Active
P4Hbeta, PDI, PDIA1, PHD, PO4DB, PO4HB, ERBA2L.
Product # :
ENZ-991Price :
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Description
P4HB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 521 amino acids (18-508 a.a.) and having a molecular mass of 57.5kDa. The P4HB is fused to a 21 amino acid His Tag and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The P4HB 1mg/ml protein solution contains 20mM Tris-HCl pH-8, and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity > 100 A650/cm/min/mg. Enzymatic activity was confirmed by measuring the aggregation of insulin in the presence of DTT.Citations
More Info
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Introduction
P4HB is a multifunctional and highly abundant enzyme that is part of the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, P4HB has a role in hydroxylation of prolyl residues in preprocollagen. P4HB is a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds.
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Synonyms
P4Hbeta, PDI, PDIA1, PHD, PO4DB, PO4HB, ERBA2L.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDAPEEEDHV LVLRKSNFAE ALAAHKYLLV EFYAPWCGHC KALAPEYAKA AGKLKAEGSE IRLAKVDATE ESDLAQQYGV RGYPTIKFFR NGDTASPKEY TAGREADDIV NWLKKRTGPA ATTLPDGAAA ESLVESSEVA VIGFFKDVES DSAKQFLQAA EAIDDIPFGI TSNSDVFSKY QLDKDGVVLF KKFDEGRNNF EGEVTKENLL DFIKHNQLPL VIEFTEQTAP KIFGGEIKTH ILLFLPKSVS DYDGKLSNFK TAAESFKGKI LFIFIDSDHT DNQRILEFFG LKKEECPAVR LITLEEEMTK YKPESEELTA ERITEFCHRF LEGKIKPHLM SQELPEDWDK QPVKVLVGKN FEDVAFDEKK NVFVEFYAPW CGHCKQLAPI WDKLGETYKD HENIVIAKMD STANEVEAVK VHSFPTLKFF PASADRTVID YNGERTLDGF KKFLESGGQD GAGDDDDLED LEEAEEPDME EDDDQKAVKD EL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MMAB HumanDescription:
Methylmalonic Aciduria Type B Human Recombinant
CBIB, Cob(I)alamin adenosyltransferase, EC 2.5.1.17.
Product # :
ENZ-248Price :
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Description
MMAB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 239 amino acids (33-250 a.a.) and having a molecular mass of 26.3 kDa. The MMAB is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MMAB 1mg/ml protein solution contains 20mM Tris pH-7.5 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
MMAB protein catalyzes the last step in the conversion of vitamin B(12) into adenosylcobalamin (AdoCbl), a vitamin B12 containing coenzyme for methylmalonyl-CoA mutase(MCM). Decreased MMAB activity leads to the inherited disorder vitamin B12 dependent methylmalonic aciduria linked to the cblB complementation group.
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Synonyms
CBIB, Cob(I)alamin adenosyltransferase, EC 2.5.1.17.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
MMAB Human 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 MQSRGPQGVE DGDRPQPSSK TPRIPKIYTK TGDKGFSSTF TGERRPKDDQ VFEAVGTTDE LSSAIGFALE LVTEKGHTFA EELQKIQCTL QDVGSALATP CSSAREAHLK YTTFKAGPIL ELEQWIDKYT SQLPPLTAFI LPSGGKISSA LHFCRAVCRR AERRVVPLVQ MGETDANVAK FLNRLSDYLF TLARYAAMKE GNQEKIYKKN DPSAESEGL.
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 :
BPHL HumanDescription:
Biphenyl Hydrolase-Like Human Recombinant
Biphenyl Hydrolase-Like (serine hydrolase), Bph-rp, Breast Epithelial Mucin-Associated Antigen, MCNAA, VACVASE, MGC41865, MGC125930.
Product # :
ENZ-055Price :
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Description
BPHL produced in E.Coli is a single, non-glycosylated polypeptide chain containing 275 amino acids (38-291a.a.) and having a molecular mass of 31.1kDa.BPHL is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BPHL protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
1mM DTT, 50mM NaCl and 10% glycerol.Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
BPHL is a Serine hydrolase that is a part of the AB hydrolase superfamily which catalyzes the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs. BPHL is expressed large quantities in liver and kidney and in minor quantities in heart, intestine and skeletal muscle. BPHL takes part in detoxification processes and is a specific alpha-amino acid ester hydrolase which favors small, hydrophobic, and aromatic side chains and does not have a strict necessity for the leaving group except for favoring a primary alcohol.
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Synonyms
Biphenyl Hydrolase-Like (serine hydrolase), Bph-rp, Breast Epithelial Mucin-Associated Antigen, MCNAA, VACVASE, MGC41865, MGC125930.
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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.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSVTSAKVAV NGVQLHYQQT GEGDHAVLLL PGMLGSGETD FGPQLKNLNK KLFTVVAWDP RGYGHSRPPD RDFPADFFER DAKDAVDLMK ALKFKKVSLL GWSDGGITAL IAAAKYPSYI HKMVIWGANA YVTDEDSMIY EGIRDVSKWS ERTRKPLEAL YGYDYFARTC EKWVDGIRQF KHLPDGNICR HLLPRVQCPA LIVHGEKDPL VPRFHADFIH KHVKGSRLHL MPEGKHNLHL RFADEFNKLA EDFLQ
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 :
PSMB6 HumanDescription:
Proteasome Subunit Beta Type 6 Human Recombinant
Proteasome subunit beta type-6, Macropain delta chain, Multicatalytic endopeptidase complex delta chain, Proteasome delta chain, Proteasome subunit Y, PSMB6, LMPY, Y, DELTA.
Product # :
ENZ-223Price :
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Description
PSMB6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 226 amino acids (35-239) and having a molecular mass of 24.2kDa.PSMB6 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PSMB6 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 1mM DTT and 0.15M NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
PSMB6 belongs to the proteasome B-type family (T1B family) which is a 20S core beta subunit in the proteasome. The PSMB6 is not present in the immunoproteasome and is replaced by PSMB9. 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.
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Synonyms
Proteasome subunit beta type-6, Macropain delta chain, Multicatalytic endopeptidase complex delta chain, Proteasome delta chain, Proteasome subunit Y, PSMB6, LMPY, Y, DELTA.
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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 MTTIMAVQFD GGVVLGADSR TTTGSYIANR VTDKLTPIHD RIFCCRSGSA ADTQAVADAV TYQLGFHSIE LNEPPLVHTA ASLFKEMCYR YREDLMAGII IAGWDPQEGG QVYSVPMGGM MVRQSFAIGG SGSSYIYGYV DATYREGMTK EECLQFTANA LALAMERDGS SGGVIRLAAI AESGVERQVL LGDQIPKFAV ATLPPA.
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 :
IFNAR1 MouseDescription:
Interferon Alpha And Beta Receptor Mouse Recombinant
IFN-R-1, IFN-alpha/beta receptor 1, Type I interferon receptor 1, Ifar, Ifnar, Infar CD118 and Ifnar1.
Product # :
CYT-994Price :
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Shipped with Ice Packs
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Description
IFNAR1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 411 amino acids (27-429a.a) and having a molecular mass of 46.8kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IFNAR1 is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IFNAR1 protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
SDS-PAGE
Citations
More Info
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Introduction
Interferon Alpha And Beta Receptor, also known IFNAR1, belongs to the class II cytokine receptor family. IFNAR1 protein forms one of the two chains of a receptor for interferons alpha as well as beta. IFNAR1 binds and activates the receptor which stimulates Janus protein kinases, which in turn phosphorylate some proteins, including STAT1 & STAT2. Furthermore, IFNAR1 also functions as an antiviral factor.
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Synonyms
IFN-R-1, IFN-alpha/beta receptor 1, Type I interferon receptor 1, Ifar, Ifnar, Infar CD118 and Ifnar1.
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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
ENLKPPENID VYIIDDNYTL KWSSHGESMG SVTFSAEYRT KDEAKWLKVP ECQHTTTTKC EFSLLDTNVY IKTQFRVRAE EGNSTSSWNE VDPFIPFYTA HMSPPEVRLE AEDKAILVHI SPPGQDGNMW ALEKPSFSYT IRIWQKSSSD KKTINSTYYV EKIPELLPET TYCLEVKAIH PSLKKHSNYS TVQCISTTVA NKMPVPGNLQ VDAQGKSYVL KWDYIASADV LFRAQWLPGY SKSSSGSRSD KWKPIPTCAN VQTTHCVFSQ DTVYTGTFFL HVQASEGNHT SFWSEEKFID SQKHILPPPP VITVTAMSDT LLVYVNCQDS TCDGLNYEII FWENTSNTKI SMEKDGPEFT LKNLQPLTVY CVQARVLFRA LLNKTSNFSE KLCEKTRPGS FSTLEHHHHH H
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Background
What is the molecular weight/Mw of IFNAR1 MOUSE Protein?
IFNAR1 MOUSE Protein has a total Mw of 46.8kDa.
What is the source or expression system of IFNAR1 MOUSE Protein?
Sf9, Baculovirus cells.
What is the Purity of IFNAR1 MOUSE Protein?
IFNAR1 MOUSE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNAR1 MOUSE Protein?
The biological functionality of IFNAR1 MOUSE Protein will be determined in the future.
What is the amino acid sequence of IFNAR1 MOUSE Protein?
ENLKPPENID VYIIDDNYTL KWSSHGESMG SVTFSAEYRT KDEAKWLKVP ECQHTTTTKC EFSLLDTNVY IKTQFRVRAE EGNSTSSWNE VDPFIPFYTA HMSPPEVRLE AEDKAILVHI SPPGQDGNMW ALEKPSFSYT IRIWQKSSSD KKTINSTYYV EKIPELLPET TYCLEVKAIH PSLKKHSNYS TVQCISTTVA NKMPVPGNLQ VDAQGKSYVL KWDYIASADV LFRAQWLPGY SKSSSGSRSD KWKPIPTCAN VQTTHCVFSQ DTVYTGTFFL HVQASEGNHT SFWSEEKFID SQKHILPPPP VITVTAMSDT LLVYVNCQDS TCDGLNYEII FWENTSNTKI SMEKDGPEFT LKNLQPLTVY CVQARVLFRA LLNKTSNFSE KLCEKTRPGS FSTLEHHHHH H
What applications can IFNAR1 MOUSE Protein be used in?
IFNAR1 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNAR1 MOUSE Protein?
The endotoxin level is minimal, IFNAR1 MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
C4BPB HumanDescription:
Complement Component 4 Binding Protein, Beta Human Recombinant
C4b-binding protein beta chain, C4BPB, C4BP.
Product # :
PRO-1174Price :
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Description
C4BPB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (18-252 a.a) and having a molecular mass of 29kDa.C4BPB is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
C4BPB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol and 0.15M NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Complement Component 4 Binding Protein, Beta (C4BPB) belongs to a superfamily of proteins composed primarily of tandemly arrayed short consensus repeats of approximately 60 amino acids. C4BPB has a regulatory role in the coagulation system also, mediated via the beta-chain binding of protein S, a vitamin K-dependent protein which functions as a cofactor of activated protein C. A single, unique beta-chain of the C4BPB assembles with 7 identical alpha-chains into the principal isoform of C4BPB, which is a multimeric protein that controls activation of the complement cascade via the classical pathway. C4BPB binds as a cofactor to C3b/C4b inactivator (C3bINA), which subsequently hydrolyzes the complement fragment C4b. In addition, C4BPB accelerates the degradation of the C4bC2a complex (C3 convertase) by detaching the complement fragment C2a. Furthermore, C4BPB interacts with anticoagulant protein S and with serum amyloid P component.
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Synonyms
C4b-binding protein beta chain, C4BPB, C4BP.
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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 MGSHMSDAEH CPELPPVDNS IFVAKEVEGQ ILGTYVCIKG YHLVGKKTLF CNASKEWDNT TTECRLGHCP DPVLVNGEFS SSGPVNVSDK ITFMCNDHYI LKGSNRSQCL EDHTWAPPFP ICKSRDCDPP GNPVHGYFEG NNFTLGSTIS YYCEDRYYLV GVQEQQCVDG EWSSALPVCK LIQEAPKPEC EKALLAFQES KNLCEAMENF MQQLKESGMT MEELKYSLEL KKAELKAKLL.
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 :
INHBC HumanDescription:
Inhibin-Beta C Chain Human Recombinant
Inhibin Beta C, Actv Beta-C Chain, IHBC, Inhibin Beta C Chain.
Product # :
HOR-010Price :
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Description
INHBC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 139 amino acids (237-352) and having a molecular mass of 14.9kDa.INHBC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The INHBC solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
INHBC, the beta C chain of inhibin, belongs to the TGF-beta superfamily. INHBC formulates heterodimers with beta A and beta B subunits. Other members of the TGF-beta superfamily are Actv's and Inhibins, hormones with contradictory roles which take part in pituitary, hypothalamic, and gonadal hormone secretion, as well as differentiation and growth of numerous cell types.
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Synonyms
Inhibin Beta C, Actv Beta-C Chain, IHBC, Inhibin Beta C Chain.
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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 MGSGIDCQGG SRMCCRQEFF VDFREIGWHD WIIQPEGYAM NFCIGQCPLH IAGMPGIAAS FHTAVLNLLK ANTAAGTTGG GSCCVPTARR PLSLLYYDRD SNIVKTDIPD MVVEACGCS
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 :
PROK Tritirachium albumDescription:
Tritirachium album Proteinase-K Recombinant
Proteinase K (EC:3.4.21.64), Endopeptidase K, Tritirachium alkaline proteinase, PROK.
Product # :
ENZ-1015Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Tritirachium album Proteinase-K expressed in yeast containing 285 amino acids having a Mw of 29.3 kDa is purified by standard chromatography techniques.
Source
Yeast
Formulation
The Proteinase-K was lyophilized without any additives.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
36 Units/mg.
One unit is defined as the amount of enzyme that will hydrolyze urea-denatured hemoglobin to produce color equivalent to 1.0 mol tyrosine per min at 37°C, pH 7.5 (color by Folin-Ciocalteu reagent).Citations
More Info
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Introduction
The Proteinase K enzyme is a member of the Peptidase family S8. Proteinase K is a broad-spectrum serine protease. Proteinase K is capable of digesting hair (keratin), henceforth, the name "Proteinase K". Proteinase K is activated by calcium, the enzyme digests proteins especially after hydrophobic amino acids (aliphatic, aromatic and other hydrophobic amino acids). Proteinase K is frequently utilized in molecular biology to digest protein and remove contamination from preparations of nucleic acid. Addition of Proteinase K to nucleic acid preparations rapidly inactivates nucleases which may otherwise degrade the DNA or RNA during purification. Proteinase K is greatly fitting to this application as the enzyme is active in the presence of chemicals which denature proteins, such as SDS and urea, chelating agents such as EDTA, sulfhydryl reagents, as well as trypsin or chymotrypsin inhibitors. Proteinase K is utilized for the destruction of proteins in cell lysates (tissue, cell culture cells) and for the release of nucleic acids, given that it quite effectively inactivates DNases and RNases.
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Synonyms
Proteinase K (EC:3.4.21.64), Endopeptidase K, Tritirachium alkaline proteinase, PROK.
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Physical Appearance
Sterile Filtered lyophilized powder.
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Stability
Recombinant Proteinase-K although stable at room temperature, should be stored between 2-8°C. Do not freeze!
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Solubility
It is recommended to reconstitute the lyophilized Proteinase-K in 20mM Tris-HCl (pH 7.4~8.0), 1mM CaCl2, 50% glycerol not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Note
Bulk Proteinase-K recombinant is available 1,000 grams price is $100 per gram
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 :
C.Albicans PLB1Description:
Candida Albicans Phospholipase B1 Recombinant
Product # :
PRO-2809Price :
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Description
Recombinant Candida Albicans Phospholipase B1 (24-526 a.a) produced in E. coli having a Mw of 52kDa. C.Albicans PLB1 is fused to a 6xHis tag at its C terminal is and purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
Phosphate buffer and 25mM K2CO3.
Purity
Protein is >90% pure as determined by 10% PAGE (coomassie staining).
Citations
More Info
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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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Background
Potential as a Therapeutic Target:
Understanding the role of PLB1 in fungal pathogenesis opens avenues for developing novel antifungal strategies. Inhibiting PLB1 activity could potentially render C. albicans less virulent and susceptible to host immune defenses. Recombinant Candida Albicans Phospholipase B1 studies play a critical role in identifying and characterizing potential inhibitors that could form the basis for antifungal drug development.
Challenges and Future Directions:
While the potential of Recombinant Candida Albicans Phospholipase B1 in antifungal research is promising, challenges persist. Fine-tuning its applications, deciphering its role in different infection scenarios, and optimizing strategies for therapeutic use are critical considerations for translational success. Additionally, understanding the interplay between PLB1 and other virulence factors in C. albicans pathogenesis remains an active area of investigation.
Recombinant Candida Albicans Phospholipase B1 emerges as a key player in the intricate dance between the fungus and its human host. Its structural insights, enzymatic activities, and implications in host-pathogen interactions position it as a central focus in the exploration of C. albicans virulence. As researchers continue to unravel the molecular intricacies of PLB1, they not only deepen our understanding of fungal pathogenesis but also pave the way for transformative advancements in antifungal drug development, shaping the future of precision medicine in the realm of fungal infections.
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 :
ITGB1 HumanDescription:
Integrin Beta 1 Human Recombinant
Integrin beta-1, Fibronectin receptor subunit beta, Glycoprotein IIa, GPIIA, VLA-4 subunit beta, CD29, ITGB1, FNRB, MDF2, MSK12, Integrin beta 1, CD29, VLAB.
Product # :
PRO-1817Price :
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Description
ITGB1 Human Recombinant produced in E. coli is a single polypeptide chain containing 462 amino acids (21-461) and having a molecular mass of 51.2 kDa.ITGB1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ITGB1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Integrins are heterodimeric proteins consist of alpha and beta subunits. There are more than 18 alpha and 8 beta subunits discovered in mammals. Integrin family members are membrane receptors that participates in cell adhesion and recognition in a variety of processes including embryogenesis, hemostasis, tissue repair, immune response and metastatic diffusion of tumor cells. ITGB1 encodes a beta subunit.
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Synonyms
Integrin beta-1, Fibronectin receptor subunit beta, Glycoprotein IIa, GPIIA, VLA-4 subunit beta, CD29, ITGB1, FNRB, MDF2, MSK12, Integrin beta 1, CD29, VLAB.
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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 MQTDENRCLK ANAKSCGECI QAGPNCGWCT NSTFLQEGMP TSARCDDLEA LKKKGCPPDD IENPRGSKDI KKNKNVTNRS KGTAEKLKPE DITQIQPQQL VLRLRSGEPQ TFTLKFKRAE DYPIDLYYLM DLSYSMKDDL ENVKSLGTDL MNEMRRITSD
FRIGFGSFVE KTVMPYISTT PAKLRNPCTS EQNCTSPFSY KNVLSLTNKG EVFNELVGKQ RISGNLDSPE GGFDAIMQVA VCGSLIGWRN VTRLLVFSTD AGFHFAGDGK LGGIVLPNDG QCHLENNMYT MSHYYDYPSI AHLVQKLSEN NIQTIFAVTE EFQPVYKELK NLIPKSAVGT LSANSSNVIQ LIIDAYNSLS SEVILENGKL SEGVTISYKS YCKNGVNGTG ENGRKCSNIS IGDEVQFEIS ITSNKCPKKD SDSFKIRPLG FTEEVEVILQ YI.
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 :
ENO3 HumanDescription:
Enolase-3 Human Recombinant
Enolase 3 (beta, muscle), Muscle-specific enolase, Skeletal muscle enolase, MSE, 2-phospho-D-glycerate hydrolyase, beta-enolase, GSD13, EC 4.2.1.11, EC 4.2.1.
Product # :
ENZ-183Price :
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Description
ENO3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 454 amino acids (1-434) and having a molecular mass of 49.0 kDa.ENO3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ENO3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ENO3 is one of three enolase isoenzymes in mammals. The homodimer ENO3 is located in skeletal muscle cells of adults and has a part in converting phosphoglyceric acid to phosphenolpyruvic acid in the glycolytic pathway. Mutations in ENO3 gene is linked to metabolic myopathies which is caused by low stability of the enzyme.
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Synonyms
Enolase 3 (beta, muscle), Muscle-specific enolase, Skeletal muscle enolase, MSE, 2-phospho-D-glycerate hydrolyase, beta-enolase, GSD13, EC 4.2.1.11, EC 4.2.1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKGRYLGK GVLKAVENIN STLGPALLQK KLSVADQEKV DKFMIELDGT ENKSKFGANA ILGVSLAVCK AGAAEKGVPL YRHIADLAGN PDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFKE AMRIGAEVYH HLKGVIKAKY GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV VIGMDVAASE FYRNGKYDLD FKSPDDPARH ITGEKLGELY KSFIKNYPVV SIEDPFDQDD WATWTSFLSG VNIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV TESIQACKLA QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK AIFAGRKFRN PKAK.
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Unit Definition
One unit will convert 1.0 umole of 2-phosphoglycerate to phospho(enol)pyruvate per minute at pH7.5 at 25°C.
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Specific Activity
> 1.5 units/ml.
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 :
CBFB HUmanDescription:
Core Binding Factor Beta Human Recombinant
PEBP2B, polyomavirus enhancer binding protein b, PEA2, CBF-beta.
Product # :
PRO-534Price :
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Description
CBFB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-202 a.a.) and having a molecular mass of 23.6 kDa. The CBFB is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
0.5mg/ml solution containing 20mM MES pH-6, 0.1mM PMSF & 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CBFB beta subunit is a heterodimeric core-binding transcription factor that is part of the PEBP2/CBF transcription factor family which controls a host of genes particulary to hematopoiesis and osteogenesis. CBFB is a non-DNA binding regulatory subunit which increases DNA binding by alpha subunit.
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Synonyms
PEBP2B, polyomavirus enhancer binding protein b, PEA2, CBF-beta.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
CBFB Human although stable at 4C for 1 week, should be stored below -18C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPRVVPDQRS KFENEEFFRK LSRECEIKYT GFRDRPHEER QARFQNACRD GRSEIAFVAT GTNLSLQFFP
ASWQGEQRQT PSREYVDLER EAGKVYLKAP MILNGVCVIW KGWIDLQRLD GMGCLEFDEE RAQQEDALAQ QAFEEARRRT REFEDRDRSH
REEMEVRVSQ LLAVTGKKTT RP.
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 :
LGMN MouseDescription:
Legumain Mouse Recombinant
Legumain, Asparaginyl endopeptidase, Protease, cysteine 1.
Product # :
ENZ-933Price :
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Description
LGMN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 426 amino acids (18-435a.a.) and having a molecular mass of 48.6kDa. LGMN is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
LGMN protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
Citations
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Introduction
Legumain, also known as LGMN is a lysosomal cysteine protease which is found in all mouse tissues, however it was mainly abundant in the kidney as well as placenta. LGMN plays an essential role in the endosomal/lysosomal degradation system as the Legumain deficiency causes the accumulation of pro cathepsins B, H & L, another group of lysosomal cysteine proteases. Furthermore, over expression of LGMN in tumors is important for invasion/metastasis.
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Synonyms
Legumain, Asparaginyl endopeptidase, Protease, cysteine 1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
VPVGVDDPED GGKHWVVIVA GSNGWYNYRH QADACHAYQI IHRNGIPDEQ IIVMMYDDIA NSEENPTPGV VINRPNGTDV YKGVLKDYTG EDVTPENFLA VLRGDAEAVK GKGSGKVLKS GPRDHVFIYF TDHGATGILV FPNDDLHVKD LNKTIRYMYE HKMYQKMVFY IEACESGSMM NHLPDDINVY ATTAANPKES SYACYYDEER GTYLGDWYSV NWMEDSDVED LTKETLHKQY HLVKSHTNTS HVMQYGNKSI STMKVMQFQG MKHRASSPIS LPPVTHLDLT PSPDVPLTIL KRKLLRTNDV KESQNLIGQI QQFLDARHVI EKSVHKIVSL LAGFGETAER HLSERTMLTA HDCYQEAVTH FRTHCFNWHS VTYEHALRYL YVLANLCEAP YPIDRIEMAM DKVCLSHYLE HHHHHH.
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 :
BLVRB MouseDescription:
Biliverdin Reductase B Mouse Recombinant
Flavin reductase (NADPH), FR, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, NADPH-dependent diaphorase, NADPH-flavin reductase, FLR.
Product # :
ENZ-1074Price :
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Description
BLVRB Mouse Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (1-206 a.a) and having a molecular mass of 24.6kDa.BLVRB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BLVRB protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0) containing 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
BLVRB (EC 1.3.1.24) catalyzes electron transfer from reduced pyridine nucleotides to flavins as well as methylene blue, pyrroloquinoline quinone, riboflavin, or methemoglobin. BLVRB is involved in protecting cells from oxidative damage or in regulating iron metabolism. BLVRB converts biliverdin to bilirubin in the liver, converting a double-bond between the second and third pyrrole ring into a single-bond. BLVRB plays a role as in human erythrocytic heme catabolic pathway and most mammalian species. Biliverdin reductase is abundantly expressed in kidney, spleen, liver and brain as well as at lower levels in the thymus and minimal levels being detected in testis.
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Synonyms
Flavin reductase (NADPH), FR, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, NADPH-dependent diaphorase, NADPH-flavin reductase, FLR.
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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 MGSMTVKKIA IFGATGRTGL TTLAQAVQAG YEVTVLVRDS SRLPSEGPQP AHVVVGDVRQ AADVDKTVAG QEAVIVLLGT GNDLSPTTVM SEGTRNIVTA MKAHGVDKVV ACTSAFLLWD PTKVPPRLQD VTDDHIRMHK ILQESGLKYV AVMPPHIGDQ PLTGAYTVTL DGRGPSRVIS KHDLGHFMLR CLTTNEYDGH TTYPSHQYD.
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 :
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 :
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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
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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.
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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.
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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 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.
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Name :
CMBL HumanDescription:
Carboxymethylenebutenolidase Human Recombinant
Carboxymethylenebutenolidase homolog, CMBL, JS-1.
Product # :
ENZ-634Price :
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Description
CMBL Human Recombinant produced in E. coli is a single polypeptide chain containing 269 amino acids (1-245) and having a molecular mass of 30.6kDa.CMBL is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CMBL solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Carboxymethylenebutenolidase homolog (CMBL) is a cysteine hydrolase of the dienelactone hydrolase family which is highly expressed in the liver cytosol. CMBL is the human homolog of Pseudomonas dienelactone hydrolase, which is a protein that participates in the bacterial halocatechol degradation pathway. CMBL which preferentially cleaves cyclic esters activates medoxomil-ester prodrugs in which the medoxomil moiety is coupled with an oxygen atom. CMBL is inhibited by PCMB (p-chloromercuribenzoate) and is encoded by a gene which maps to human chromosome 5p15.2. CMBL can also activate beta-lactam antibiotics faropenem medoxomil and lenampicillin. CMBL is widely expressed, with the highest levels in the liver, followed by the kidney, small intestine and the colon.
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Synonyms
Carboxymethylenebutenolidase homolog, CMBL, JS-1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMANEAY PCPCDIGHRL EYGGLGREVQ VEHIKAYVTK SPVDAGKAVI VIQDIFGWQL PNTRYIADMI SGNGYTTIVP DFFVGQEPWD PSGDWSIFPE WLKTRNAQKI DREISAILKY LKQQCHAQKI GIVGFCWGGT AVHHLMMKYS EFRAGVSVYG IVKDSEDIYN LKNPTLFIFA ENDVVIPLKD VSLLTQKLKE HCKVEYQIKT FSGQTHGFVH RKREDCSPAD KPYIDEARRN LIEWLNKYM.
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 :
GADD45B HumanDescription:
Growth Arrest and DNA-Damage-Inducible Beta Human Recombinant
MYD118, GADD45BETA, GADD45B, Growth arrest and DNA-damage-inducible protein GADD45 beta, Myeloid differentiation primary response protein MyD118, Negative growth regulatory protein MyD118, DKFZp566B133.
Product # :
PRO-563Price :
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Description
GADD45B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 160 amino acids and having a molecular mass of 17.8 kDa.
Source
Escherichia Coli.
Formulation
The GADD45B protein solution contains 20mM Tris-HCl pH-7.5 and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GADD45B is part of the nuclear proteins to interact with various proteins whose transcript levels are raised after stressful growth arrest conditions and treatment with DNA-damaging agents. GADD45B reacts to environmental stresses by mediating activation of the p38/JNK pathway which is mediated through their protein binding and activating MTK1/MEKK4 kinase, which is an upstream activator of both p38 and JNK MAPKs. GADD45B is involved in the regulation of growth and apoptosis. GADD45b takes part during chondrocyte terminal differentiation and mediates MMP-13 gene expression. GADD45 in B cells is induced by CD40 via a mechanism that involves NF-kappa B and that induction suppresses Fas-mediated killing. GADD45b is down-regulated in most cases of hepatocellular carcinoma (HCC), and is a molecular marker in the diagnosis of HCC and as a possible therapeutic target.
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Synonyms
MYD118, GADD45BETA, GADD45B, Growth arrest and DNA-damage-inducible protein GADD45 beta, Myeloid differentiation primary response protein MyD118, Negative growth regulatory protein MyD118, DKFZp566B133.
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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
MTLEELVACD NAAQKMQTVT AAVEELLVAA QRQDRLTVGV YESAKLMNVD PDSVVLCLLA IDEEEEDDIA LQIHFTLIQS FCCDNDINIV
RVSGMQRLAQ LLGEPAETQG TTEARDLHCL LVTNPHTDAW KSHGLVEVAS YCEESRGNNQ WVPYISLQER.
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 :
ACAA2 HumanDescription:
Acetyl-COA Acyltransferase 2 Human Recombinant
DSAEC, 3-ketoacyl-CoA thiolase, mitochondrial, Acetyl-CoA acyltransferase, Beta-ketothiolase.
Product # :
ENZ-697Price :
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Shipped with Ice Packs
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Description
ACAA2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 404 amino acids (17-397) and having a molecular mass of 42.6kDa.ACAA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ACAA2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Acetyl-COA Acyltransferase 2, (ACAA2) is a member of the thiolase family. ACAA2 catalyzes the final step of the mitochondrial fatty acid beta-oxidation spiral. Not like most mitochondrial matrix proteins, ACAA2 contains a non-cleavable amino-terminal targeting signal.
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Synonyms
DSAEC, 3-ketoacyl-CoA thiolase, mitochondrial, Acetyl-CoA acyltransferase, Beta-ketothiolase.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSFGAYGGL LKDFTATDLS EFAAKAALSA GKVSPETVDS VIMGNVLQSS SDAIYLARHV GLRVGIPKET PALTINRLCG SGFQSIVNGC QEICVKEAEV VLCGGTESMS QAPYCVRNVR FGTKLGSDIK LEDSLWVSLT DQHVQLPMAM TAENLAVKHK ISREECDKYA LQSQQRWKAA NDAGYFNDEM APIEVKTKKG KQTMQVDEHA RPQTTLEQLQ KLPPVFKKDG TVTAGNASGV ADGAGAVIIA SEDAVKKHNF TPLARIVGYF VSGCDPSIMG IGPVPAISGA LKKAGLSLKD MDLVEVNEAF APQYLAVERS LDLDISKTNV NGGAIALGHP LGGSGSRITA HLVHELRRRG GKYAVGSACI GGGQGIAVII QSTA.
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 :
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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
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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.
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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.
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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
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 :
HADHB HumanDescription:
2-Enoyl-Coenzyme A (CoA) Hydratase, Beta Human Recombinant
Hydroxyacyl-CoA Dehydrogenase/3-Ketoacyl-CoA Thiolase/Enoyl-CoA Hydratase (Trifunctional Protein) Beta Subunit, Hydroxyacyl-Coenzyme A Dehydrogenase/3-Ketoacyl-Coenzyme A Thiolase/Enoyl-Coenzyme A Hydratase (Trifunctional Protein) Beta Subunit, TP-BETA, 3-Ketoacyl-Coenzyme A (CoA) Thiolase Of Mitochondrial Trifunctional Protein Beta Subunit, 2-Enoyl-Coenzyme A (CoA) Hydratase Beta Subunit, Trifunctional Enzyme Subunit Beta Mitochondrial, Mitochondrial Trifunctional Protein, Acetyl-CoA Acyltransferase, Beta-Ketothiolase, Beta Subunit, EC 2.3.1.16, EC 2.3.1, MSTP029, ECHB, MTPB.
Product # :
ENZ-845Price :
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Shipped with Ice Packs
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Description
HADHB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 464 amino acids (34-474 a.a) and having a molecular mass of 49.9kDa. HADHB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HADHB protein solution (0. 5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
2-Enoyl-Coenzyme A (CoA) Hydratase, Beta (HADHB) is the beta subunit of the mitochondrial trifunctional protein, that catalyzes the last 3 phases of mitochondrial beta-oxidation of long chain fatty acids. HADHB binds RNA and reduces the stability of various mRNAs. Mutations in HADHB cause trifunctional protein deficiency.
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Synonyms
Hydroxyacyl-CoA Dehydrogenase/3-Ketoacyl-CoA Thiolase/Enoyl-CoA Hydratase (Trifunctional Protein) Beta Subunit, Hydroxyacyl-Coenzyme A Dehydrogenase/3-Ketoacyl-Coenzyme A Thiolase/Enoyl-Coenzyme A Hydratase (Trifunctional Protein) Beta Subunit, TP-BETA, 3-Ketoacyl-Coenzyme A (CoA) Thiolase Of Mitochondrial Trifunctional Protein Beta Subunit, 2-Enoyl-Coenzyme A (CoA) Hydratase Beta Subunit, Trifunctional Enzyme Subunit Beta Mitochondrial, Mitochondrial Trifunctional Protein, Acetyl-CoA Acyltransferase, Beta-Ketothiolase, Beta Subunit, EC 2.3.1.16, EC 2.3.1, MSTP029, ECHB, MTPB.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSAAPAVQT KTKKTLAKPN IRNVVVVDGV RTPFLLSGTS YKDLMPHDLA RAALTGLLHR TSVPKEVVDY IIFGTVIQEV KTSNVAREAA LGAGFSDKTP AHTVTMACIS ANQAMTTGVG LIASGQCDVI VAGGVELMSD VPIRHSRKMR KLMLDLNKAK SMGQRLSLIS KFRFNFLAPE LPAVSEFSTS ETMGHSADRL AAAFAVSRLE QDEYALRSHS LAKKAQDEGL LSDVVPFKVP GKDTVTKDNG IRPSSLEQMA KLKPAFIKPY GTVTAANSSF LTDGASAMLI MAEEKALAMG YKPKAYLRDF MYVSQDPKDQ LLLGPTYATP KVLEKAGLTM NDIDAFEFHE AFSGQILANF KAMDSDWFAE NYMGRKTKVG LPPLEKFNNW GGSLSLGHPF GATGCRLVMA AANRLRKEGG QYGLVAACAA GGQGHAMIVE AYPK.
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.