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1000 results found for “cathepsin”
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Name :
TIMP2 Human, HisDescription:
Tissue Inhibitor of Metalloprotease 2 Human Recombinant, His Tag
TIMP metallopeptidase inhibitor 2, metalloproteinase inhibitor 2, Tissue inhibitor of metalloproteinases 2, TIMP-2, CSC-21K.
Product # :
ENZ-646Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TIMP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 232 amino acids (27-220) and having a molecular mass of 26.1 kDa.TIMP2 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TIMP2 solution (0.5mg/1ml) 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.
More Info
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Introduction
TIMP2 belongs to the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases, a group of peptidases that take part in degradation of the extracellular matrix. Besides having an inhibitory role against metalloproteinases, the encoded protein has a exclusive part among TIMP family members in its capability to directly suppress the proliferation of endothelial cells. Consequently, the encoded protein is crucial to the conservation of tissue homeostasis by suppressing the production of quiescent tissues as an answer to angiogenic factors, and by inhibiting protease activity in tissues undergoing renovation of the extracellular matrix.
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Synonyms
TIMP metallopeptidase inhibitor 2, metalloproteinase inhibitor 2, Tissue inhibitor of metalloproteinases 2, TIMP-2, CSC-21K.
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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 KDRWGSHM CS CSPVHPQQAF CNADVVIRAK AVSEKEVDSG NDIYGNPIKR IQYEIKQIKM FKGPEKDIEF IYTAPSSAVC GVSLDVGGKK EYLIAGKAEG DGKMHITLCD FIVPWDTLST TQKKSLNHRY QMGCECKITR CPMIPCYISS PDECLWMDWV TEKNINGHQA KFFACIKRSD GSCAWYRGAA PPKQEFLDIE DP
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 :
CAPG HumanDescription:
Capping Protein Gelsolin-Like Human Recombinant
AFCP, CAPG, Macrophage-capping protein, Actin regulatory protein CAP-G, MCP.
Product # :
PRO-759Price :
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Shipped with Ice Packs
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Description
CAPG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 348 amino acids (1-348 a.a.) and having a molecular mass of 38.5 kDa. The CAPG protein is purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein solution (1mg/ml) contains 20mM Tris buffer pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CAPG is part of the gelsolin/villin family of actin-regulatory proteins. CAPG reversibly blocks the barbed ends of F-actin filaments in a Ca2+ and phosphoinositide-regulated method, though it does not separate preformed actin filaments. By capping the barbed ends of actin filaments, CAPG contributes to the control of actin-based motility in non-muscle cells. CAPG is involved in macrophage function. CAPG is involved in regulating cytoplasmic and/or nuclear structures via possible interactions with actin. CAPG binds DNA. CAPG lacks a nuclear export sequence present in structurally related proteins. CAPG is a tumor suppressor protein that plays a role in the tumorigenic progression of certain cancers. Dysregulated expression of CAPG was found in premalignant and malignant oral carcinogenesis.
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Synonyms
AFCP, CAPG, Macrophage-capping protein, Actin regulatory protein CAP-G, MCP.
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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
MYTAIPQSGS PFPGSVQDPG LHVWRVEKLK PVPVAQENQG VFFSGDSYLV LHNGPEEVSH LHLWIGQQSS RDEQGACAVL AVHLNTLLGE RPVQHREVQG NESDLFMSYF PRGLKYQEGG VESAFHKTST GAPAAIKKLY QVKGKKNIRA TERALNWDSF NTGDCFILDL GQNIFAWCGG KSNILERNKA RDLALAIRDS ERQGKAQVEI VTDGEEPAEM IQVLGPKPAL KEGNPEEDLT ADKANAQAAA LYKVSDATGQ MNLTKVADSS PFALELLISD DCFVLDNGLC GKIYIWKGRK ANEKERQAAL QVAEGFISRM QYAPNTQVEI LPQGRESPIF KQFFKDWK.
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 :
CCL24 MouseDescription:
Eotaxin-2 Mouse Recombinant (CCL24)
C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.
Product # :
CHM-368Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CCL24 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of 10.3 kDa. The CCL24 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CCL24 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM Phosphate buffer pH-7.4 and 0.15M sodium chloride.
Purity
Greater than 97.0% as determined by:(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
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Introduction
Eotaxin-2, also called MPIF2 & Ckb6, is a novel CC chemokine produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3 including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Furthermore, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which includes C-terminal truncation, contains 78 amino acids (92 amino acids for the mouse homolog, without C-terminal truncation).
CCL24 functions as a chemotactic chemokine for resting t-lymphocytes, and eosinophils. CCL24 has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. CCL24 is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line and binds to CCR3. -
Synonyms
C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Eotaxin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL24 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 CCL24 Mouse Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
VTIPSSCCTS FISKKIPENR VVSYQLANGS ICPKAGVIFI TKKGHKICTD PKLLWVQRHI QKLDAKKNQP SKGAKAVRTK FAVQRRRGNS TEV.
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Background
What is the molecular weight/Mw of CCL24 MOUSE Protein?
CCL24 MOUSE Protein has a total Mw of 10.3kDa.
What is the source or expression system of CCL24 MOUSE Protein?
Escherichia Coli.
What is the Purity of CCL24 MOUSE Protein?
CCL24 MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL24 MOUSE Protein?
Determined by its ability to chemoattract murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CCL24 MOUSE Protein?
VTIPSSCCTS FISKKIPENR VVSYQLANGS ICPKAGVIFI TKKGHKICTD PKLLWVQRHI QKLDAKKNQP SKGAKAVRTK FAVQRRRGNS TEV.
What applications can CCL24 MOUSE Protein be used in?
CCL24 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL24 MOUSE Protein?
The endotoxin level is minimal, CCL24 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 :
CDH2 HumanDescription:
Cadherin 2 Human Recombinant
Cadherin 2, Cadherin 2, Type 1, N-Cadherin (Neuronal), Neural Cadherin, N-Cadherin, CDw325, NCAD, CDHN, Calcium-Dependent Adhesion Protein, Neuronal, CD325 Antigen, N-Cadherin 1, Cadherin-2, CD325.
Product # :
PRO-2455Price :
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Shipped with Ice Packs
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Description
CDH2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 574 amino acids (160-724a.a.) and having a molecular mass of 62.9kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).CDH2 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CDH2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cadherin-2 isoform 1, also known as CDH2 is a transmembrane, homophilic glycoprotein which belongs to the calcium-dependent cell adhesion molecule family. CDH2 takes part in neurons and later on was discovered to participate in cardiac muscle and in cancer metastasis as well. The CDH2 loss promotes tumorigenesis through releasing membrane-bound β-catenin, and so stimulating Wnt signaling. Furthermore, CDH2 appears to be implicated in tumor development, however this discovery is limited in adrenocortical tumors-ACTs.
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Synonyms
Cadherin 2, Cadherin 2, Type 1, N-Cadherin (Neuronal), Neural Cadherin, N-Cadherin, CDw325, NCAD, CDHN, Calcium-Dependent Adhesion Protein, Neuronal, CD325 Antigen, N-Cadherin 1, Cadherin-2, CD325.
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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
ADPDWVIPPI NLPENSRGPF PQELVRIRSD RDKNLSLRYS VTGPGADQPP TGIFIINPIS GQLSVTKPLD REQIARFHLR AHAVDINGNQ VENPIDIVIN VIDMNDNRPE FLHQVWNGTV PEGSKPGTYV MTVTAIDADD PNALNGMLRY RIVSQAPSTP SPNMFTINNE TGDIITVAAG LDREKVQQYT LIIQATDMEG NPTYGLSNTA TAVITVTDVN DNPPEFTAMT FYGEVPENRV DIIVANLTVT DKDQPHTPAW NAVYRISGGD PTGRFAIQTD PNSNDGLVTV VKPIDFETNR MFVLTVAAEN QVPLAKGIQH PPQSTATVSV TVIDVNENPY FAPNPKIIRQ EEGLHAGTML TTFTAQDPDR YMQQNIRYTK LSDPANWLKI DPVNGQITTI AVLDRESPNV KNNIYNATFL ASDNGIPPMS GTGTLQIYLL DINDNAPQVL PQEAETCETP DPNSINITAL DYDIDPNAGP FAFDLPLSPV TIKRNWTITR LNGDFAQLNL KIKFLEAGIY EVPIIITDSG NPPKSNISIL RVKVCQCDSN GDCTDVDRIV GAGLGTGAHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LACTB E.Coli, His ActiveDescription:
Beta Lactamase E.Coli Recombinant, His Active
Beta-lactamase, Cephalosporinase, ampC, ampA, b4150, JW4111.
Product # :
ENZ-1033Price :
Quantity :
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Shipped with Ice Packs
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Description
LACTB produced in E.Coli is a single, non-glycosylated polypeptide chain containing 379 amino acids (20-377 a.a) and having a molecular mass of 41.8kDa. LACTB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LACTB solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >700 units/mg, in which One unit will hydrolyze 1.0umole of Nitrocefin per minute at pH 7.0 at 37°C.
More Info
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Introduction
Beta-lactamase is a type of enzyme (EC 3.5.2.6) produced by some bacteria that is responsible for their resistance to beta-lactam antibiotics like penicillins, cephalosporins, cephamycins and carbapenems. These antibiotics have a common element in their molecular structure: a four-atom ring known as a beta-lactam. The lactamase enzyme breaks that ring open, deactivating the molecule's antibacterial properties.
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Synonyms
Beta-lactamase, Cephalosporinase, ampC, ampA, b4150, JW4111.
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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 MAPQQINDIV HRTITPLIEQ QKIPGMAVAV IYQGKPYYFT WGYADIAKKQ PVTQQTLFEL GSVSKTFTGV LGGDAIARGE IKLSDPTTKY WPELTAKQWN GITLLHLATY TAGGLPLQVP DEVKSSSDLL RFYQNWQPAW APGTQRLYAN SSIGLFGALA VKPSGLSFEQ AMQTRVFQPL KLNHTWINVP PAEEKNYAWG YREGKAVHVS PGALDAEAYG VKSTIEDMAR WVQSNLKPLD INEKTLQQGI QLAQSRYWQT GDMYQGLGWE MLDWPVNPDS IINGSDNKIA LAARPVKAIT PPTPAVRASW VHKTGATGGF GSYVAFIPEK ELGIVMLANK NYPNPARVDA AWQILNALQ.
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 :
TBCEL HumanDescription:
Tubulin Folding Cofactor E-Like Human Recombinant
Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.
Product # :
PRO-030Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TBCEL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids and having a molecular mass of 50.6kDa. The TBCEL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TBCEL solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
TBCEL, is a factor that is in charge of the microtubule cytoskeleton in determining cell behavior. TBCEL plays a role as a regulator of tubulin stability. While widely expressed in testis, TBCEL is also present in several tissues at a much lower level. TBCEL comprises of seven LRR (leucine-rich) repeats, one LRRCT domain and one ubiquitin-like domain. The gene that translates TBCEL consists of 66,704 bases and maps to human chromosome 11q23.3. Chromosome 11 houses over 1,400 genes and consist of nearly 4% of the human genome. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are associated with defects in genes that map to chromosome 11.
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Synonyms
Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.
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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 MGSMDQPSGR SFMQVLCEKY SPENFPYRRG PGMGVHVPAT PQGSPMKDRL NLPSVLVLNS CGITCAGDEK EIAAFCAHVS ELDLSDNKLE DWHEVSKIVS NVPQLEFLNL SSNPLNLSVL ERTCAGSFSG VRKLVLNNSK ASWETVHMIL QELPDLEELF LCLNDYETVS CPSICCHSLK LLHITDNNLQ DWTEIRKLGV MFPSLDTLVL ANNHLNAIEE PDDSLARLFP NLRSISLHKS GLQSWEDIDK LNSFPKLEEV RLLGIPLLQP YTTEERRKLV IARLPSVSKL NGSVVTDGER EDSERFFIRY YVDVPQEEVP FRYHELITKY GKLEPLAEVD LRPQSSAKVE VHFNDQVEEM SIRLDQTVAE LKKQLKTLVQ LPTSNMLLYY FDHEAPFGPE EMKYSSRALH SFGIRDGDKI YVESKTK.
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 :
ADH6 HumanDescription:
Alcohol Dehydrogenase 6 Human Recombinant
Alcohol dehydrogenase 6, ADH6, ADH-5.
Product # :
ENZ-619Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ADH6 Human Recombinant produced E. coli is a single polypeptide chain containing 399 amino acids (1-375) and having a molecular mass of 42.4kDa.ADH6 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ADH6 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Alcohol dehydrogenase 6 (ADH6) belongs to the alcohol dehydrogenase family. Alcohol dehydrogenase family members metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH6 is expressed in the stomach as well as in the liver, and it contains a glucocorticoid response element upstream of its 5’ UTR, which is a steroid hormone receptor binding site.
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Synonyms
Alcohol dehydrogenase 6, ADH6, ADH-5.
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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 MGSHMSTTGQ VIRCKAAILW KPGAPFSIEE VEVAPPKAKE VRIKVVATGL CGTEMKVLGS KHLDLLYPTI LGHEGAGIVE SIGEGVSTVK PGDKVITLFL PQCGECTSCL NSEGNFCIQF KQSKTQLMSD GTSRFTCKGK SIYHFGNTST FCEYTVIKEI SVAKIDAVAP LEKVCLISCG FSTGFGAAIN TAKVTPGSTC AVFGLGGVGL SVVMGCKAAG AARIIGVDVN KEKFKKAQEL GATECLNPQD LKKPIQEVLF DMTDAGIDFC FEAIGNLDVL AAALASCNES YGVCVVVGVL PASVQLKISG QLFFSGRSLK GSVFGGWKSR QHIPKLVADY MAEKLNLDPL ITHTLNLDKI NEAVELMKTG KCIRCILLL.
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 :
CDC25A HumanDescription:
Cell Division Cycle 25A Human Recombinant
M-phase inducer phosphatase 1, Dual specificity phosphatase Cdc25A, CDC25A, CDC25A2.
Product # :
ENZ-091Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CDC25A Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 560 amino acids (1-524 a.a.) and having a molecular mass of 63.2kDa. The CDC25A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CDC25A solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 20% glycerol, 0.2M NaCl and 1mM EDTA.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
M-phase inducer phosphatase 1 (CDC25A) belongs to the CDC25 family of phosphatases. CDC25A is essential for progression from G1 to the S phase of the cell cycle. CDC25A activates the cyclin-dependent kinase CDC2 by eliminating 2 phosphate groups. CDC25A is specifically degraded in reaction to DNA damage, which inhibits cells with chromosomal abnormalities from progressing in the course of cell division. CDC25A is an oncogene, though its exact function in oncogenesis has not been determined.
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Synonyms
M-phase inducer phosphatase 1, Dual specificity phosphatase Cdc25A, CDC25A, CDC25A2.
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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 KDRWGSMELG PEPPHRRRLL FACSPPPASQ PVVKALFGAS AAGGLSPVTN LTVTMDQLQG LGSDYEQPLE VKNNSNLQRM GSSESTDSGF CLDSPGPLDS KENLENPMRR IHSLPQKLLG CSPALKRSHS DSLDHDIFQL IDPDENKENE AFEFKKPVRP VSRGCLHSHG LQEGKDLFTQ RQNSAPARML SSNERDSSEP GNFIPLFTPQ SPVTATLSDE DDGFVDLLDG ENLKNEEETP SCMASLWTAP LVMRTTNLDN RCKLFDSPSL CSSSTRSVLK RPERSQEESP PGSTKRRKSM SGASPKESTN PEKAHETLHQ SLSLASSPKG TIENILDNDP RDLIGDFSKG YLFHTVAGKH QDLKYISPEI MASVLNGKFA NLIKEFVIID CRYPYEYEGG HIKGAVNLHM EEEVEDFLLK KPIVPTDGKR VIVVFHCEFS SERGPRMCRY VRERDRLGNE YPKLHYPELY VLKGGYKEFF MKCQSYCEPP SYRPMHHEDF KEDLKKFRTK SRTWAGEKSK REMYSRLKKL.
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 :
ACO1 HumanDescription:
Aconitase-1 Human Recombinant
Onitase 1 Soluble, IRP1, IREB1, IREBP, Citrate hydro-lyase, Iron regulatory protein 1, Ferritin repressor protein, Iron-responsive element-binding protein 1, ACONS, Aconitate Hydratase, EC 4.2.1.3, Aconitase.
Product # :
ENZ-056Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ACO1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 912 amino acids (1-889a.a.) and having a molecular mass of 100.8kDa.ACO1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ACO1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
2mM DTT, 100mM NaCl and 10% glycerol.Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
ACO1 has a part in an iron sensor. ACO1 catalyzes the stereo-specific isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid cycle, a non-redox-active process.
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Synonyms
Onitase 1 Soluble, IRP1, IREB1, IREBP, Citrate hydro-lyase, Iron regulatory protein 1, Ferritin repressor protein, Iron-responsive element-binding protein 1, ACONS, Aconitate Hydratase, EC 4.2.1.3, Aconitase.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSNPFAH LAEPLDPVQP GKKFFNLNKL EDSRYGRLPF SIRVLLEAAI RNCDEFLVKK QDIENILHWN VTQHKNIEVP FKPARVILQD FTGVPAVVDF AAMRDAVKKL GGDPEKINPV CPADLVIDHS IQVDFNRRAD SLQKNQDLEF ERNRERFEFL KWGSQAFHNM RIIPPGSGII HQVNLEYLAR VVFDQDGYYY PDSLVGTDSH TTMIDGLGIL GWGVGGIEAE AVMLGQPISM VLPQVIGYRL MGKPHPLVTS TDIVLTITKH LRQVGVVGKF VEFFGPGVAQ LSIADRATIA NMCPEYGATA AFFPVDEVSI TYLVQTGRDE EKLKYIKKYL QAVGMFRDFN DPSQDPDFTQ VVELDLKTVV PCCSGPKRPQ DKVAVSDMKK DFESCLGAKQ GFKGFQVAPE HHNDHKTFIY DNTEFTLAHG SVVIAAITSC TNTSNPSVML GAGLLAKKAV DAGLNVMPYI KTSLSPGSGV VTYYLQESGV MPYLSQLGFD VVGYGCMTCI GNSGPLPEPV VEAITQGDLV AVGVLSGNRN FEGRVHPNTR ANYLASPPLV IAYAIAGTIR IDFEKEPLGV NAKGQQVFLK DIWPTRDEIQ AVERQYVIPG MFKEVYQKIE TVNESWNALA TPSDKLFFWN SKSTYIKSPP FFENLTLDLQ PPKSIVDAYV LLNLGDSVTT DHISPAGNIA RNSPAARYLT NRGLTPREFN SYGSRRGNDA VMARGTFANI RLLNRFLNKQ APQTIHLPSG EILDVFDAAE RYQQAGLPLI VLAGKEYGAG SSRDWAAKGP FLLGIKAVLA ESYERIHRSN LVGMGVIPLE YLPGENADAL GLTGQERYTI IIPENLKPQM KVQVKLDTGK TFQAVMRFDT DVELTYFLNG GILNYMIRKM AK
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 :
Quantity :
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Shipped with Ice Packs
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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 :
C.Albicans PLB1Description:
Candida Albicans Phospholipase B1 Recombinant
Product # :
PRO-2809Price :
Quantity :
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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).
More Info
-
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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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 :
AKR1B1 HumanDescription:
Aldose Reductase Human Recombinant
Aldehyde Reductase, EC 1.1.1.21, ALR2, ALDR1, MGC1804, Aldo-keto reductase family1 member B1, Aldose Reductase, AKR1B1, AR, ADR.
Product # :
ENZ-390Price :
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Description
AKR1B1 Human Recombinant amino produced in E.Coli is a single, non-glycosylated polypeptide chain containing 316 amino acids having a molecular mass of 35.8 kDa.The AKR1B1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The 1mg/ml protein solution contains 20mM Tris-HCl buffer pH 8, 10% glycerol, and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 800pmol/min/ug, and is defined as the amount of enzyme that catalyze the reduction of 1.0 pmole DL-glyceraldehyde in the presence of NADPH per minute at pH7.0 at 37°C.More Info
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Introduction
AKR1B1 is part of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. AKR1B1 catalyzes the reduction several aldehydes, including the aldehyde form of glucose, and thus involved in the development of diabetic complications by catalyzing the reduction of glucose to sorbitol. AKR1B1 catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Transgenic mice over expressing human aldose reductase show that AKR1B1 is a key player in ischemic injury and impairment of functional and metabolic recovery after ischemia. Aldose Reductase is an obligatory mediator of TNF-alpha signaling leading to an increase in the expression of adhesion molecules and increased binding of monocytes to the endothelium. AKR1B1 is a critical regulator of TNF-alpha-induced apoptotic signaling in endothelial cells.
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Synonyms
Aldehyde Reductase, EC 1.1.1.21, ALR2, ALDR1, MGC1804, Aldo-keto reductase family1 member B1, Aldose Reductase, AKR1B1, AR, ADR.
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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
MASRLLLNNG AKMPILGLGT WKSPPGQVTE AVKVAIDVGY RHIDCAHVYQ NENEVGVAIQ EKLREQVVKR EELFIVSKLW CTYHEKGLVK GACQKTLSDL KLDYLDLYLI HWPTGFKPGK EFFPLDESGN VVPSDTNILD TWAAMEELVD EGLVKAIGIS NFNHLQVEMI LNKPGLKYKP AVNQIECHPY LTQEKLIQYC QSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK HNKTTAQVLI RFPMQRNLVV IPKSVTPERI AENFKVFDFE LSSQDMTTLL SYNRNWRVCA LLSCTSHKDY PFHEEF.
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 :
TPSAB1 Human, Sf9Description:
Tryptase Alpha/Beta 1 Human Recombinant, Sf9
Tryptase alpha/beta-1, TPSAB1, TPS1, TPS2, TPSB1, Tryptase I, Tryptase alpha-1.
Product # :
ENZ-1062Price :
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Description
TPSAB1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (31-275 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 251 amino acids and having a molecular mass of 28.2kDa.TPSAB1 shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TPSAB1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) & 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Tryptase alpha/beta-1 (TPSAB1) is a tryptase which is the key neutral protease present in mast cells and is discharged upon the coupled activation-degranulation response of this cell type. TPSAB1 is enzymatically active only as a heparin-stabilized tetramer, and is resistant to all known endogenous proteinase inhibitors. TPSAB1 is implicated as a mediator in the pathogenesis of asthma and other allergic and inflammatory disorders.
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Synonyms
Tryptase alpha/beta-1, TPSAB1, TPS1, TPS2, TPSB1, Tryptase I, Tryptase alpha-1.
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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
IVGGQEAPRS KWPWQVSLRV HGPYWMHFCG GSLIHPQWVL TAAHCVGPDV KDLAALRVQL REQHLYYQDQ LLPVSRIIVH PQFYTAQIGA DIALLELEEP VNVSSHVHTV TLPPASETFP PGMPCWVTGW GDVDNDERLP PPFPLKQVKV PIMENHICDA KYHLGAYTGD DVRIVRDDML CAGNTRRDSC QGDSGGPLVC KVNGTWLQAG VVSWGEGCAQ PNRPGIYTRV TYYLDWIHHY VPKKPHHHHH 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 :
CSTF1 HumanDescription:
Cleavage Stimulation Factor 1 Human Recombinant
Cleavage stimulation factor subunit 1, CF-1 50 kDa subunit, Cleavage stimulation factor 50 kDa subunit, CSTF 50 kDa subunit, CstF-50, CSTF1, CstFp50.
Product # :
PRO-1170Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CSTF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (1-431 a.a) and having a molecular mass of 49.4kDa.CSTF1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CSTF1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2M urea.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Cleavage stimulation factor subunit 1 (CSTF1) is involved in the polyadenylation and 3'end cleavage of pre-mRNAs. The CSTF1 gene encodes one of three subunits which merge to produce cleavage stimulation factor (CSTF). Like the mammalian G protein beta subunits, CSTF1 contains transducin-like repeats. CSTF1 is one of the numerous factors necessary for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. CSTF1 is responsible for the interaction of CSTF with other factors to create a stable complex on the pre-mRNA.
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Synonyms
Cleavage stimulation factor subunit 1, CF-1 50 kDa subunit, Cleavage stimulation factor 50 kDa subunit, CSTF 50 kDa subunit, CstF-50, CSTF1, CstFp50.
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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
MYRTKVGLKD RQQLYKLIIS QLLYDGYISI ANGLINEIKP QSVCAPSEQL LHLIKLGMEN DDTAVQYAIG RSDTVAPGTG IDLEFDADVQ TMSPEASEYE TCYVTSHKGP CRVATYSRDG QLIATGSADA SIKILDTERM LAKSAMPIEV MMNETAQQNM ENHPVIRTLY DHVDEVTCLA FHPTEQILAS GSRDYTLKLF DYSKPSAKRA FKYIQEAEML RSISFHPSGD FILVGTQHPT LRLYDINTFQ CFVSCNPQDQ HTDAICSVNY NSSANMYVTG SKDGCIKLWD GVSNRCITTF EKAHDGAEVC SAIFSKNSKY ILSSGKDSVA KLWEISTGRT LVRYTGAGLS GRQVHRTQAV FNHTEDYVLL PDERTISLCC WDSRTAERRN LLSLGHNNIV RCIVHSPTNP GFMTCSDDFR ARFWYRRSTT DVEHHHHHH.
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 :
CEACAM6 HumanDescription:
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 6 Recombinant Human
Carcinoembryonic antigen-related cell adhesion molecule 6, CEACAM6, CEACAM6, CD66c, CEAL, NCA, Non-specific crossreacting antigen, Normal cross-reacting antigen, CD_antigen: CD66c, NCA.
Product # :
PRO-2331Price :
Quantity :
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Shipped with Ice Packs
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Description
CEACAM6 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 297 amino acids (35-320) and having a molecular mass of 32.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CEACAM6 is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CEACAM6 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 6 (CEACAM6) is a part of the human carcino-embryonic antigen (CEA) family. CEACAM6 belongs to the glycosylphosphatidylinositol-linked immunoglobulin superfamily which is involved in various human cancers. CEACAM6 is linked to the progression of pancreatic cancer.
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Synonyms
Carcinoembryonic antigen-related cell adhesion molecule 6, CEACAM6, CEACAM6, CD66c, CEAL, NCA, Non-specific crossreacting antigen, Normal cross-reacting antigen, CD_antigen: CD66c, NCA.
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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
ADPEFKLTIE STPFNVAEGK EVLLLAHNLP QNRIGYSWYK GERVDGNSLI VGYVIGTQQA TPGPAYSGRE TIYPNASLLI QNVTQNDTGF YTLQVIKSDL VNEEATGQFH VYPELPKPSI SSNNSNPVED KDAVAFTCEP EVQNTTYLWW VNGQSLPVSP RLQLSNGNMT LTLLSVKRND AGSYECEIQN PASANRSDPV TLNVLYGPDV PTISPSKANY RPGENLNLSC HAASNPPAQY SWFINGTFQQ STQELFIPNI TVNNSGSYMC QAHNSATGLN RTTVTMITVS GHHHHHH.
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 :
ACADVL HumanDescription:
Acyl-CoA Dehydrogenase, Very Long Chain Human Recombinant
ACAD6, LCACD, VLCAD.
Product # :
ENZ-250Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ACADVL Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 636 amino acids (41-655 a.a.) and having a molecular mass of 68.5 kda. ACADVL contains 21 amino acid His-Tag at the N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The 0.5mg/ml protein solution contains 20mM Tris-HCl buffer pH-8, 1mM DTT, 1mM EDTA, 10% glycerol and 100mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ACADVL is an inner mitochondrial membrane enzyme that is part of the family of acyl-CoA dehydrogenases. ACADVL protein participates in lipid metabolism and has catalytic activity toward esters of long chain and very long chain fatty acids such as palmitoyl-CoA and stearoyl-CoA, and is involved in the first step of the fatty acid β-oxidation pathway. ACADVL deficiency in reduces myocardial fatty acid beta-oxidation and is related with cardiomyopathy.
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Synonyms
ACAD6, LCACD, VLCAD.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store ACADVL 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 MAGGAAQLAL DKSDSHPSDA LTRKKPAKAE SKSFAVGMFK GQLTTDQVFP YPSVLNEEQT QFLKELVEPV SRFFEEVNDP AKNDALEMVE ETTWQGLKEL GAFGLQVPSE LGGVGLCNTQ YARLVEIVGM HDLGVGITLG AHQSIGFKGI LLFGTKAQKE KYLPKLASGE TVAAFCLTEP SSGSDAASIR TSAVPSPCGK YYTLNGSKLW ISNGGLADIF TVFAKTPVTD PATGAVKEKI TAFVVERGFG GITHGPPEKK MGIKASNTAE VFFDGVRVPS ENVLGEVGSG FKVAMHILNN GRFGMAAALA GTMRGIIAKA VDHATNRTQF GEKIHNFGLI QEKLARMVML QYVTESMAYM VSANMDQGAT DFQIEAAISK IFGSEAAWKV TDECIQIMGG MGFMKEPGVE RVLRDLRIFR IFEGTNDILR LFVALQGCMD KGKELSGLGS ALKNPFGNAG LLLGEAGKQL RRRAGLGSGL SLSGLVHPEL SRSGELAVRA LEQFATVVEA KLIKHKKGIV NEQFLLQRLA DGAIDLYAMV VVLSRASRSL SEGHPTAQHE KMLCDTWCIE AAARIREGMA ALQSDPWQQE LYRNFKSISK ALVERGGVVT SNPLGF.
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 :
LHPP HumanDescription:
Phospholysine Phosphohistidine Inorganic Pyrophosphate Phosphatase Human Recombinant
Phospholysine phosphohistidine inorganic pyrophosphate phosphatase, hLHPP, LHPP, HDHD2B.
Product # :
ENZ-575Price :
Quantity :
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Shipped with Ice Packs
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Description
LHPP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 307 amino acids (1-270) and having a molecular mass of 33.5kDa.LHPP is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LHPP solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP) belongs to the HAD-like hydrolase superfamily. LHPP is an exceptional enzyme which hydrolyzes not only oxygen-phosphorus bonds in inorganic pyrophosphate but also nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate in vitro. LHPP is expressed in the liver, kidney and moderately in the brain.
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Synonyms
Phospholysine phosphohistidine inorganic pyrophosphate phosphatase, hLHPP, LHPP, HDHD2B.
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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
MRGSHHHHHP WYASMTGGQQ MGRDLYDDDD KDRWGSHMAP WGKRLAGVRG VLLDISGVLY DSGAGGGTAI AGSVEAVARL KRSRLKVRFC TNESQKSRAE LVGQLQRLGF DISEQEVTAP APAACQILKE QGLRPYLLIH DGVRSEFDQI DTSNPNCVVI ADAGESFSYQ NMNNAFQVLM ELEKPVLISL GKGRYYKETS GLMLDVGPYM KALEYACGIK AEVVGKPSPE FFKSALQAIG VEAHQAVMIG DDIVGDVGGA QRCGMRALQV RTGKFRPSDE HHPEVKADGY VDNLAEAVDL LLQHADK.
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 :
CDCP1 HumanDescription:
CUB Domain Containing Protein 1 Human Recombinant
CUB Domain Containing Protein 1, Subtractive Immunization M Plus HEp3-Associated 135 KDa Protein, Transmembrane And Associated With Src Kinases, Membrane Glycoprotein Gp140, SIMA135, TRASK, CD318 Antigen, CD318, CUB domain-containing protein 1, Membrane glycoprotein gp140, Subtractive immunization M plus HEp3-associated 135 kDa protein, Transmembrane and associated with src kinases.
Product # :
PRO-2264Price :
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Description
CDCP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 646 amino acids (30-667a.a.) and having a molecular mass of 72.8kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). CDCP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CDCP1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CUB Domain Containing Protein 1, also known as CDCP1 is a transmembrane protein which contains three extracellular CUB domains. CDCP1 is implicated in cell adhesion and cell matrix association. In addition, CDCP1 takes part in the regulation of anchorage versus migration or proliferation versus differentiation through its phosphorylation. CDCP1 is also a novel marker for leukemia diagnosis as well as for immature hematopoietic stem cell subsets. Furthermore, the extracellular region of human CDCP1 shares amino acid identity sequence with the mouse CDCP1.
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Synonyms
CUB Domain Containing Protein 1, Subtractive Immunization M Plus HEp3-Associated 135 KDa Protein, Transmembrane And Associated With Src Kinases, Membrane Glycoprotein Gp140, SIMA135, TRASK, CD318 Antigen, CD318, CUB domain-containing protein 1, Membrane glycoprotein gp140, Subtractive immunization M plus HEp3-associated 135 kDa protein, Transmembrane and associated with src kinases.
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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
FEIALPRESN ITVLIKLGTP TLLAKPCYIV ISKRHITMLS IKSGERIVFT FSCQSPENHF VIEIQKNIDC MSGPCPFGEV QLQPSTSLLP TLNRTFIWDV KAHKSIGLEL QFSIPRLRQI GPGESCPDGV THSISGRIDA TVVRIGTFCS NGTVSRIKMQ EGVKMALHLP WFHPRNVSGF SIANRSSIKR LCIIESVFEG EGSATLMSAN YPEGFPEDEL MTWQFVVPAH LRASVSFLNF NLSNCERKEE RVEYYIPGST TNPEVFKLED KQPGNMAGNF NLSLQGCDQD AQSPGILRLQ FQVLVQHPQN ESNKIYVVDL SNERAMSLTI EPRPVKQSRK FVPGCFVCLE SRTCSSNLTL TSGSKHKISF LCDDLTRLWM NVEKTISCTD HRYCQRKSYS LQVPSDILHL PVELHDFSWK LLVPKDRLSL VLVPAQKLQQ HTHEKPCNTS FSYLVASAIP SQDLYFGSFC PGGSIKQIQV KQNISVTLRT FAPSFQQEAS RQGLTVSFIP YFKEEGVFTV TPDTKSKVYL RTPNWDRGLP SLTSVSWNIS VPRDQVACLT FFKERSGVVC QTGRAFMIIQ EQRTRAEEIF SLDEDVLPKP SFHHHSFWVN ISNCSPTSGK QLDLLFSVTL TPRTVDLTLE 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 :
SIAH1 HumanDescription:
Siah E3 Ubiquitin Protein Ligase 1 Human Recombinant
Siah E3 ubiquitin protein ligase 1, Seven in absentia homolog 1, seven in absentia homolog 1 (Drosophila), E3 ubiquitin-protein ligase SIAH1, HUMSIAH, hSIAH1, Siah-1a, SIAH1A, EC 6.3.2.
Product # :
ENZ-640Price :
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Shipped with Ice Packs
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Description
SIAH1 Human Recombinant produced in E. coli is a single polypeptide chain containing 216 amino acids (90-282) and having a molecular mass of 24.1 kDa.SIAH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SIAH1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 40% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
E3 ubiquitin-protein ligase SIAH1 (SIAH1) belongs to the SIAH (seven in absentia homolog) family. SIAH1 is a tumor suppressor protein, which is expressed in intestinal epithelium and activated during apoptosis. SIAH1 is involved in ubiquitination and proteasome-mediated degradation of specific proteins. SIAH1 is comprised of an N-terminal RING-finger domain (required for proteolysis) and a cystein-rich C-terminal domain (which regulates oligomerization and SIAH binding to target proteins). SIAH1 causes indirect degradation of beta-catenin by way of creation of a complex with Siah-interacting protein (SIP), Skp1 and Ebi.
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Synonyms
Siah E3 ubiquitin protein ligase 1, Seven in absentia homolog 1, seven in absentia homolog 1 (Drosophila), E3 ubiquitin-protein ligase SIAH1, HUMSIAH, hSIAH1, Siah-1a, SIAH1A, EC 6.3.2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSVANSVLF PCKYASSGCE ITLPHTEKAD HEELCEFRPY SCPCPGASCK WQGSLDAVMP HLMHQHKSIT TLQGEDIVFL ATDINLPGAV DWVMMQSCFG FHFMLVLEKQ EKYDGHQQFF AIVQLIGTRK QAENFAYRLE LNGHRRRLTW EATPRSIHEG IATAIMNSDC LVFDTSIAQL FAENGNLGIN VTISMC.
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 :
CHP HumanDescription:
Calcium Binding Protein P22 Human Recombinant
CHP, CHP Human, Calcium-binding protein p22, Calcium-binding protein CHP, Calcineurin homologous protein, Calcineurin B homolog, SLC9A1BP.
Product # :
PRO-847Price :
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Shipping Method :
Shipped with Ice Packs
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Description
CHP Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (1-195 a.a.) and having a molecular mass of 24.7 kDa. The CHP is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CHP Human solution containing 20mM Tris-HCl pH-7.5 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Calcium-binding protein P22 is a phosphoprotein that binds to the sodium-hydrogen exchangers (NHEs). CHP is an essential cofactor which maintains the physiological activity of NHE family members. CHP has protein sequence resemblance to calcineurin B and it is also identified to be an endogenous inhibitor of calcineurin activity.CHP is necessary for constitutive membrane traffic. CHP Inhibits GTPase-stimulated Na(+)/H(+) exchange. CHP inhibits calcineurin phosphatase activity. Required for activity of SLC9A1/NHE1.
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Synonyms
CHP, CHP Human, Calcium-binding protein p22, Calcium-binding protein CHP, Calcineurin homologous protein, Calcineurin B homolog, SLC9A1BP.
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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 MMGSRASTLL RDEELEEIKK ETGFSHSQIT RLYSRFTSLD KGENGTLSRE DFQRIPELAI NPLGDRIINA FFPEGEDQVN FRGFMRTLAH FRPIEDNEKS KDVNGPEPLN SRSNKLHFAF RLYDLDKDEK ISRDELLQVL RMMVGVNISD EQLGSIADRT IQEADQDGDS AISFTEFVKV LEKVDVEQKM SIRFLH.
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 :
DECR2 HumanDescription:
2,4-Dienoyl CoA Reductase 2 Human Recombinant
Peroxisomal 2,4-dienoyl-CoA reductase, pDCR, 2,4-dienoyl-CoA reductase 2, DECR2, PDCR, SDR17C1.
Product # :
ENZ-211Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DECR2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-292) and having a molecular mass of 33.2kDa.DECR2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DECR2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Peroxisomal 2,4-dienoyl-CoA reductase (DECR2) is an supporting enzyme of beta-oxidation. DECR2 partakes in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. DECR2 catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.
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Synonyms
Peroxisomal 2,4-dienoyl-CoA reductase, pDCR, 2,4-dienoyl-CoA reductase 2, DECR2, PDCR, SDR17C1.
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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 MGSMAQPPPD VEGDDCLPAY RHLFCPDLLR DKVAFITGGG SGIGFRIAEI FMRHGCHTVI ASRSLPRVLT AARKLAGATG RRCLPLSMDV RAPPAVMAAV DQALKEFGRI DILINCAAGN FLCPAGALSF NAFKTVMDID TSGTFNVSRV LYEKFFRDHG GVIVNITATL GNRGQALQVH AGSAKAAVDA MTRHLAVEWG PQNIRVNSLA PGPISGTEGL RRLGGPQASL STKVTASPLQ RLGNKTEIAH SVLYLASPLA SYVTGAVLVA DGGAWLTFPN GVKGLPDFAS FSAKL.
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 :
LPL Human, HEKDescription:
Lipoprotein Lipase Human Recombinant, HEK
Lipoprotein lipase, LPL, LIPD, HDLCQ11.
Product # :
ENZ-087Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Recombinant Human LPL produced in HEK293 cell line has a molecular mass of 51.8kDa containing 461 amino acid residues of the human LPL (Ala28-Gly475, variant Asn > Ser318) and fused to a 13 a.a. Flag-tag at N-terminus.
Source
HEK293 (Human Embryonic Kidney cell line).
Formulation
LPL was filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl, pH 7.5.
More Info
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Introduction
LPL is a lipoprotein lipase, which is expressed in the heart, muscle, and adipose tissue. LPL acts as a homodimer, and has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake. Type I hyperlipoproteinemia is a result of severe mutations which cause LPL deficiency, whereas less extreme mutations in LPL are linked to many disorders of lipoprotein metabolism. Lipoprotein lipase (LPL) is a fundamental enzyme in plasma triglyceride hydrolysis and is secreted by macrophages in the subendothelial space. LPL also promotes the development of atherosclerosis through facilitation of monocyte adhesion to endothelial cells, stimulation of tumor necrosis factor alpha (TNF) secretion and induction of vascular smooth muscle cell proliferation.
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Synonyms
Lipoprotein lipase, LPL, LIPD, HDLCQ11.
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Physical Appearance
Filtered white lyophilized 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 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
HVDYKDDDDK PAGADQRRDF IDIESKFALR TPEDTAEDTC HLIPGVAESV ATCHFNHSSK TFMVIHGWTV TGMYESWVPK ADQRRDF IDIESKFALR TPEDTAEDTC HLIPGVAESV ATCHFNHSSK TFMVIHGWTV TGMYESWVPK LVAALYKREP DSNVIVVDWL SRAQEHYPVS AGYTKLVGQD VARFINWMEE EFNYPLDNVH LLGYSLGAHA AGIAGSLTNK KVNRITGLDP AGPNFEYAEA PSRLSPDDAD FVDVLHTFTR GSPGRSIGIQ KPVGHVDIYP NGGTFQPGCN IGEAIRVIAE RGLGDVDQLV KCSHERSIHL FIDSLLNEEN PSKAYRCSSK EAFEKGLCLS CRKNRCNNLG YEISKVRAKR SSKMYLKTRS QMPYKVFHYQ VKIHFSGTES ETHTNQAFEI SLYGTVAESE NIPFTLPEVS TNKTYSFLIY TEVDIGELLM LKLKWKSDSY FSWSDWWSSP GFAIQKIRVK AGETQKKVIF CSREKVSHLQ KGKAPAVFVK CHDKSLNKKS G.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MAP1LC3B MouseDescription:
Microtubule-Associated Protein 1 Light Chain 3 Beta Mouse Recombinant
Microtubule-Associated Protein 1 Light Chain 3 beta, ATG8F, Autophagy-related ubiquitin-like modifier LC3 B, MAP1 light chain 3-like protein 2, MAP1A/MAP1B LC3 B, LC3B, MAP1A/1BLC3, MAP1ALC3.
Product # :
PRO-2482Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MAP1LC3B Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 144 amino acids (1-120 a.a.) and having a molecular mass of 16.7kDa. MAP1LC3B is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MAP1LC3B protein solution (0.25mg/ml) containing 20mM MES(pH6.0), 0.1M NaCl, 1mM DTT and 30% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
MAP1LC3B is a member of the MAP1 LC3 family. MAP1LC3B is a subunit of neuronal microtubule-associated MAP1A and MAP1B proteins, that are involved in microtubule assembly and important for neurogenesis. In addition, MAP1LC3B takes part in formation of autophagosomal vacuoles and is expressed mainly in heart, testis, brain and skeletal muscle.
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Synonyms
Microtubule-Associated Protein 1 Light Chain 3 beta, ATG8F, Autophagy-related ubiquitin-like modifier LC3 B, MAP1 light chain 3-like protein 2, MAP1A/MAP1B LC3 B, LC3B, MAP1A/1BLC3, MAP1ALC3.
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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 MGSHMPSEKT FKQRRSFEQR VEDVRLIREQ HPTKIPVIIE RYKGEKQLPV LDKTKFLVPD HVNMSELIKI IRRRLQLNAN QAFFLLVNGH SMVSVSTPIS EVYESERDED GFLYMVYASQ ETFG.
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 :
PTPRN HumanDescription:
Protein Tyrosine Phosphatase Receptor Type N Human Recombinant
Receptor-type tyrosine-protein phosphatase-like N, R-PTP-N, Islet cell antigen 512, ICA 512, Islet cell autoantigen 3, PTP IA-2, PTPRN, ICA3, ICA512.
Product # :
ENZ-1162Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Protein Tyrosine Phosphatase Receptor Type N produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 46kDa. PTPRN is expressed with a 6xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
PTPRN is supplied in 50mM Sodium phosphate (pH 8.0) and 20% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Protein Tyrosine Phosphatase Receptor Type N (PTPRN) is a catalytically inactive protein and a major target of autoimmune response in diabetes mellitus. The long C-terminal intracellular tail covers the majority of autoantibody epitopes. PTPRN is expressed in neural, neuroendocrine and pancreatic islet cells.
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Synonyms
Receptor-type tyrosine-protein phosphatase-like N, R-PTP-N, Islet cell antigen 512, ICA 512, Islet cell autoantigen 3, PTP IA-2, PTPRN, ICA3, ICA512.
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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.
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.