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1000 results found for “cystatin”
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Name :
CTSZ HumanDescription:
Cathepsin-Z Human Recombinant
Cathepsin Z preproprotein, Cathepsin Z, CTSX, Cathepsin P, Cathepsin X, CTSZ, Cathepsin-Z.
Product # :
ENZ-748Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CTSZ Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 265 amino acids (62-303) and having a molecular mass of 29.5kDa.CTSZ is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CTSZ solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and member of the peptidase C1 family. CTSZ, which has been also known as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and, similar to other members of this family, takes part in tumorigenesis.
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Synonyms
Cathepsin Z preproprotein, Cathepsin Z, CTSX, Cathepsin P, Cathepsin X, CTSZ, Cathepsin-Z.
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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 MGSLPKSWDW RNVDGVNYAS ITRNQHIPQY CGSCWAHAST SAMADRINIK RKGAWPSTLL SVQNVIDCGN AGSCEGGNDL SVWDYAHQHG IPDETCNNYQ AKDQECDKFN QCGTCNEFKE CHAIRNYTLW RVGDYGSLSG REKMMAEIYA NGPISCGIMA TERLANYTGG IYAEYQDTTY INHVVSVAGW GISDGTEYWI VRNSWGEPWG ERGWLRIVTS TYKDGKGARY NLAIEEHCTF GDPIV.
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 :
KRT14 Human, HisDescription:
Cytokeratin 14 Human Recombinant, His Tag
Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.
Product # :
PRO-941Price :
Quantity :
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Shipped with Ice Packs
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Description
KRT14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 492 amino acids (1-472 a.a.) and having a molecular mass of 53.8kDa.KRT14 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KRT14 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cytokeratin 14 is a member of the keratin family, the most diverse group of intermediate filaments. Cytokeratin 14 is a type I keratin, is usually found as a heterotetramer with two keratin 5 molecules, a type II keratin. Together they form the cytoskeleton of epithelial cells. Mutations in the genes for these keratins are associated with epidermolysis bullosa simplex. At least one pseudogene has been identified at 17p12-p11.
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Synonyms
Keratin, type I cytoskeletal 14, Cytokeratin-14, CK-14, Keratin-14, K14, KRT14, NFJ, CK14, EBS3, EBS4.
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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 MTTCSRQFTS SSSMKGSCGI GGGIGGGSSR ISSVLAGGSC RAPSTYGGGL SVSSSRFSSG GAYGLGGGYG GGFSSSSSSF GSGFGGGYGG GLGTGLGGGF GGGFAGGDGL LVGSEKVTMQ NLNDRLASYL DKVRALEEAN ADLEVKIRDW YQRQRPAEIK
DYSPYFKTIE DLRNKILTAT VDNANVLLQI DNARLAADDF RTKYETELNL RMSVEADING LRRVLDELTL ARADLEMQIE SLKEELAYLK KNHEEEMNAL RGQVGGDVNV EMDAAPGVDL SRILNEMRDQ YEKMAEKNRK DAEEWFFTKT EELNREVATN SELVQSGKSE ISELRRTMQN
LEIELQSQLS MKASLENSLE ETKGRYCMQL AQIQEMIGSV EEQLAQLRCE MEQQNQEYKI LLDVKTRLEQ EIATYRRLLE GEDAHLSSSQ FSSGSQSSRD VTSSSRQIRT KVMDVHDGKV VSTHEQVLRT KN.
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 :
CSNK2A1 HumanDescription:
Casein Kinase 2 alpha 1 Human Recombinant
Casein kinase II subunit alpha, EC 2.7.11.1, CK II, CK2A1, CKII alpha, CSNK2A1, PKCK2, CSK21.
Product # :
PKA-208Price :
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Shipped with Ice Packs
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Description
Casein Kinase 2 alpha 1 Human Recombinant is a non-glycosylated polypeptide having a molecular mass of 45.1 kDa. Casein Kinase 2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CSNK2A1 is supplied in 25mM Tris-HCl, 500mM NaCl, 1mM DTT, 500μm PMSF, 50% glycerol, pH 8.5.
Purity
Greater than 99% as determined by SDS-PAGE.
More Info
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Introduction
The Casein kinase 2 (EC2.7.11.1) is a serine/threonine-selective protein kinasethat is a tetramer of two alpha subunits and two beta subunits. The alpha subunits have the catalytic kinase domain. Casein kinase 2 has been implicated in cell cyclecontrol, DNA repair, regulation of the circadian rhythmand other cellular processes. Casein kinase 2 activity has been reported to be activated following Wnt signaling pathwayactivation. A Pertussis toxin-sensitive G proteinand Disheveled appear to be an intermediary between Wnt-mediated activation of the Frizzled receptor and activation of casein kinase 2.
Mice that lack casein kinase 2 alpha prime have a defect in the morphology of developing sperm. -
Synonyms
Casein kinase II subunit alpha, EC 2.7.11.1, CK II, CK2A1, CKII alpha, CSNK2A1, PKCK2, CSK21.
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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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Unit Definition
No protease activity detectable, specific activity > 1.320 U/mg (1U = 1µmol/min at 37 degree C) using the synthetic peptide RRRDDDSDDD.
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 :
SPA-Cys HisDescription:
Staphylococcal Protein-A Cys Recombinant, His Tag
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
Product # :
PRO-1923Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SPA-Cys His Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain with 6×His-tag and a Cys on C-terminus. SPA-Cys His is comprised of 5 IgG-binding domains E-D-A-B-C aligned in series containing 307 amino acids and having a molecular mass of 34.8kDa containing little or no carbohydrate. Cell wall binding region, cell membrane binding region and albumin binding region were removed to ensure the highest specific IgG binding.
Source
Escherichia Coli.
Formulation
SPA protein was lyophilized with no additives.
Purity
Greater than 96.0% as determined by: (a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.
More Info
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Introduction
Protein A is a cell wall component produced by several strains of Staphylococcus aureus. The recombinant Protein A is genetically engineered protein and holds 5 IgG-binding regions of protein A. Recombinant Protein A functions basically the same as native Protein A and is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to human IgG1, IgG2 and IgG4, mouse IgG2a, IgG2b and IgG3 and rat IgG2c. Protein A also binds to total IgG from rabbit, pig, dog, cat, and guinea pig.
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Synonyms
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SPA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SPA 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 SPA in sterile 18MΩ-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE HHHHHHC
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 :
CTSA MouseDescription:
Cathepsin-A Mouse Recombinant
Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.
Product # :
ENZ-945Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CTSA produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 459 amino acids (24-474 a.a.) and having a molecular mass of 52.4kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CTSA is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9 Insect cells.
Formulation
CTSA protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cathepsin-A (CTSA) is a protective protein which is crucial for both the activity of beta-galactosidase and neuraminidase, CTSA associates with these enzymes and exerts a protective function required for their stability and activity. The CTSA protein is also a carboxypeptidase and can deamidate tachykinins. CTSA is a component of the lysosomal multienzyme complex along with beta-galactosidase and sialidase Neu1. CTSA is a multicatalytic enzyme with deamidase and esterase in addition to carboxypeptidase activities.
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Synonyms
Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.
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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
APDQDEIDCL PGLAKQPSFR QYSGYLRASD SKHFHYWFVE SQNDPKNSPV VLWLNGGPGC SSLDGLLTEH GPFLIQPDGV TLEYNPYAWN LIANVLYIES PAGVGFSYSD DKMYVTNDTE VAENNYEALK DFFRLFPEYK DNKLFLTGES YAGIYIPTLA VLVMQDPSMN LQGLAVGNGL ASYEQNDNSL VYFAYYHGLL GNRLWTSLQT HCCAQNKCNF YDNKDPECVN NLLEVSRIVG KSGLNIYNLY APCAGGVPGR HRYEDTLVVQ DFGNIFTRLP LKRRFPEALM RSGDKVRLDP PCTNTTAPSN YLNNPYVRKA LHIPESLPRW DMCNFLVNLQ YRRLYQSMNS QYLKLLSSQK YQILLYNGDV DMACNFMGDE WFVDSLNQKM EVQRRPWLVD YGESGEQVAG FVKECSHITF LTIKGAGHMV PTDKPRAAFT MFSRFLNKEP YVEHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
KRT19 Human, HisDescription:
Cytokeratin 19 Human Recombinant , His Tag
Keratin type I cytoskeletal 19, Cytokeratin-19, CK-19, Keratin-19, K19, KRT19, CK19, K1CS, MGC15366.
Product # :
PRO-1347Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KRT19 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 423 amino acids (1-400) and having a molecular mass of 46.5kDa.KRT19 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The KRT19 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
CTK-19 is a member of the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins consist of acidic proteins which are arranged in pairs of heterotypic keratin chains. Unlike its related family members, this smallest known acidic cytokeratin is not paired with a basic cytokeratin in epithelial cells. It is specifically expressed in the periderm, the transiently superficial layer that envelopes the developing epidermis. The type I cytokeratins are clustered in a region of chromosome 17q12-q21.
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Synonyms
Keratin type I cytoskeletal 19, Cytokeratin-19, CK-19, Keratin-19, K19, KRT19, CK19, K1CS, MGC15366.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMTSYSYR QSSATSSFGG LGGGSVRFGP GVAFRAPSIH GGSGGRGVSV SSARFVSSSS SGAYGGGYGG VLTASDGLLA GNEKLTMQNL NDRLASYLDK VRALEAANGE LEVKIRDWYQ KQGPGPSRDY SHYYTTIQDL RDKILGATIE NSRIVLQIDN ARLAADDFRT KFETEQALRM SVEADINGLR RVLDELTLAR TDLEMQIEGL KEELAYLKKN HEEEISTLRG QVGGQVSVEV DSAPGTDLAK ILSDMRSQYE VMAEQNRKDA EAWFTSRTEE LNREVAGHTE QLQMSRSEVT DLRRTLQGLE IELQSQLSMK AALEDTLAET EARFGAQLAH IQALISGIEA QLGDVRADSE RQNQEYQRLM DIKSRLEQEI ATYRSLLEGQ EDHYNNLSAS KVL.
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 :
KRT8 Human, HisDescription:
Cytokeratin 8 Human Recombinant, His Tag
Keratin type II cytoskeletal 8, Cytokeratin-8, CK-8, Keratin-8, K8, KRT8, CYK8, KO, CK8, K2C8, CARD2.
Product # :
PRO-1567Price :
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Shipped with Ice Packs
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Description
KRT8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 506 amino acids (1-483 a.a) and having a molecular mass of 56kDa. KRT8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KRT8 protein solution (1mg/ml) containing 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
Cytokeratin 8 (KRT8) belongs to the type II keratin family clustered on the long arm of chromosome 12. Type I and type II keratins heteropolymerize to form intermediate-sized filaments in the cytoplasm of epithelial cells. KRT8 typically dimerizes with keratin 18 to form an intermediate filament in simple single-layered epithelial cells. KRT8 has a role in retaining cellular structural integrity and also functions in signal transduction and cellular differentiation. KRT8 gene mutations cause cryptogenic cirrhosis.
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Synonyms
Keratin type II cytoskeletal 8, Cytokeratin-8, CK-8, Keratin-8, K8, KRT8, CYK8, KO, CK8, K2C8, CARD2.
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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 MGSMSIRVTQ KSYKVSTSGP RAFSSRSYTS GPGSRISSSS FSRVGSSNFR GGLGGGYGGA SGMGGITAVT VNQSLLSPLV LEVDPNIQAV RTQEKEQIKT LNNKFASFID KVRFLEQQNK MLETKWSLLQ QQKTARSNMD NMFESYINNL RRQLETLGQE KLKLEAELGN MQGLVEDFKN KYEDEINKRT EMENEFVLIK KDVDEAYMNK VELESRLEGL TDEINFLRQL YEEEIRELQS QISDTSVVLS MDNSRSLDMD SIIAEVKAQY EDIANRSRAE AESMYQIKYE ELQSLAGKHG DDLRRTKTEI SEMNRNISRL QAEIEGLKGQ RASLEAAIAD AEQRGELAIK DANAKLSELE AALQRAKQDM ARQLREYQEL MNVKLALDIE IATYRKLLEG EESRLESGMQ NMSIHTKTTS GYAGGLSSAY GGLTSPGLSY SLGSSFGSGA GSSSFSRTSS SRAVVVKKIE TRDGKLVSES SDVLPK.
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 :
CSNK1A1 HumanDescription:
Casein Kinase 1 alpha 1 Human Recombinant
Casein kinase I isoform alpha, CKI-alpha, CK1, CSNK1A1, HLCDGP1, PRO2975.
Product # :
PKA-056Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CSNK1A1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-337) and having a molecular mass of 41kDa. CSNK1A1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CSNK1A1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Caseine Kinase 1 alpha belongs is a member of the protein kinase superfamily, CK1 Ser/Thr protein kinase family, Casein kinase I subfamily. The CK1 isoforms - alpha, beta, gamma, delta, epsilon and their splice variants are involved in diverse cellular processes including membrane trafficking, circadian rhythm, cell cycle progression, chromosome segregation, apoptosis and cellular differentiation. Possibly CSNK1A1 can phosphorylate a large number of proteins and is involved in Wnt signaling where it phosphorylates CTNNB1 on Ser45. CSNK1A1 also interacts with the Axin complex.
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Synonyms
Casein kinase I isoform alpha, CKI-alpha, CK1, CSNK1A1, HLCDGP1, PRO2975.
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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 MASSSGSKAE FIVGGKYKLV RKIGSGSFGD IYLAINITNG EEVAVKLESQ KARHPQLLYE SKLYKILQGG VGIPHIRWYG QEKDYNVLVM DLLGPSLEDL FNFCSRRFTM KTVLMLADQM ISRIEYVHTK NFIHRDIKPD NFLMGIGRHC NKLFLIDFGL AKKYRDNRTR QHIPYREDKN LTGTARYASI NAHLGIEQSR RDDMESLGYV LMYFNRTSLP WQGLKAATKK QKYEKISEKK MSTPVEVLCK GFPAEFAMYL NYCRGLRFEE APDYMYLRQL FRILFRTLNH QYDYTFDWTM LKQKAAQQAA SSSGQGQQAQ TPTGKQTDKT KSNMKGF.
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 :
CCN1 (275-381)Description:
Cysteine-Rich Angiogenic Inducer 61 (275-381 a.a.) Human Recombinant
CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.
Product # :
CYT-1235Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The CYR61Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The CYR61His-Tagged Fusion Protein, produced in E. coli, is a 17kDa protein containing 107 amino acid residues of the CYR61Human, 275-381 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized CYR61at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
Cysteine-Rich Angiogenic Inducer 61 also known as CYR61 is a growth factor-inducible, immediate-early gene which has many activities in various cancers. CYR61 is a part of to the CCN family a group of secreted extracellular matrix-associated proteins which regulate diverse biological processes including cell adhesion, proliferation, migration, survival and angiogenesis. CYR61 plays a significant role in development, tissue repair, wound healing, and various pathological conditions such as cancer and fibrosis. CYR61 is encoded by a growth factor-inducible immediate-early gene. CYR61 promotes the adhesion of endothelial cells by interaction with integrin and enhances growth factor-induced DNA synthesis in the same cell type.
What is the molecular weight/Mw of CCN1 Protein?
CCN1 Protein has a total Mw of 17kDa.
What is the source or expression system of CCN1 Protein?
Escherichia Coli.
What is the Purity of CCN1 Protein?
CCN1 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CCN1 Protein?
The biological functionality of CCN1 Protein will be determined in the future.
What is the amino acid sequence of CCN1 Protein?
CCN1 Protein is composed from 107 amino acids.
What applications can CCN1 Protein be used in?
CCN1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCN1 Protein?
The endotoxin level is minimal, CCN1 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 :
Cys-Protein-LDescription:
Cys-Protein L Recombinant
Product # :
PRO-1933Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at N-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 366 amino acids in total and having a molecular mass of 40.6kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein-L was lyophilized without any additives.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein-L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-L 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 Protein-L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
CKEETPETPE TDSEEEVTIK ANLIFANGST QTAEFKGTFE KATSEAYAYA DTLKKDNGEY TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT FEEATAEAYR YADALKKDNG EYTVDVADKG YTLNIKFAGK EKTPEEPKEE VTIKANLIYA DGKTQTAEFK GTFEEATAEA YRYADLLAKE NGKYTVDVAD KGYTLNIKFA GKEKTPEEPK EEVTIKANLI YADGKTQTAE FKGTFAEATA EAYRYADLLA KENGKYTADL EDGGYTINIR FAGKKVDEKP EEKEQVTIKE NIYFEDGTVQ TATFKGTFAE ATAEAYRYAD LLSKEHGKYT ADLEDGGYTI NIRFAG.
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 :
CHST10 HumanDescription:
Carbohydrate Sulfotransferase 10 Human Recombinant
Carbohydrate Sulfotransferase 10, HNK1ST, HNK-1 Sulfotransferase,HuHNK-1ST, HNK-1ST, EC 2.8.2.-, EC 2.8.2, CHST10.
Product # :
ENZ-894Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CHST10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (28-356 a.a) and having a molecular mass of 41.2kDa.CHST10 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CHST10 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Carbohydrate Sulfotransferase 10, also known as CHST10 is a member of the sulfotransferase 2 family. CHST10 was first recognized as a sulfotransferase which acts on the human natural killer-1 (HNK-1) glycan. Furthermore, CHST10 is a carbohydrate involved in neurodevelopment as well as synaptic plasticity.
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Synonyms
Carbohydrate Sulfotransferase 10, HNK1ST, HNK-1 Sulfotransferase,HuHNK-1ST, HNK-1ST, EC 2.8.2.-, EC 2.8.2, CHST10.
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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 MTFKDPDVYS AKQEFLFLTT MPEVRKLPEE KHIPEELKPT GKELPDSQLV QPLVYMERLE LIRNVCRDDA LKNLSHTPVS KFVLDRIFVC DKHKILFCQT PKVGNTQWKK VLIVLNGAFS SIEEIPENVV HDHEKNGLPR LSSFSDAEIQ KRLKTYFKFF IVRDPFERLI SAFKDKFVHN PRFEPWYRHE IAPGIIRKYR RNRTETRGIQ FEDFVRYLGD PNHRWLDLQF GDHIIHWVTY VELCAPCEIM YSVIGHHETL EDDAPYILKE AGIDHLVSYP TIPPGITVYN RTKVEHYFLG ISKRDIRRLY ARFEGDFKLF GYQKPDFLLN.
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 :
CTSS HumanDescription:
Cathepsin-S Human Recombinant
Cathepsin S, MGC3886, CTSS, Cathepsin-S.
Product # :
ENZ-686Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CTSS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (17-331) and having a molecular mass of 38.1kDa. CTSS is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CTSS solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Cathepsin S (CTSS) belongs to the peptidase C1 family. CTSS is a lysosomal cysteine proteinase that participates in the degradation of antigenic proteins to peptides for presentation on MHC class II molecules. CTSS functions as an elastase over a broad pH range in alveolar macrophages.
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Synonyms
Cathepsin S, MGC3886, CTSS, Cathepsin-S.
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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 MQLHKDPTLD HHWHLWKKTY GKQYKEKNEE AVRRLIWEKN LKFVMLHNLE HSMGMHSYDL GMNHLGDMTS EEVMSLMSSL RVPSQWQRNI TYKSNPNWIL PDSVDWREKG CVTEVKYQGS CGACWAFSAV GALEAQLKLK TGKLVSLSAQ NLVDCSTEKY GNKGCNGGFM TTAFQYIIDN KGIDSDASYP YKAMDQKCQY DSKYRAATCS KYTELPYGRE DVLKEAVANK GPVSVGVDAR HPSFFLYRSG VYYEPSCTQN VNHGVLVVGY GDLNGKEYWL VKNSWGHNFG EEGYIRMARN KGNHCGIASF PSYPEI.
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 :
CAMP HumanDescription:
Cathelicidin Antimicrobial Peptide Human Recombinant
CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.
Product # :
PRO-1405Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CAMP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (34-173 a.a.) and having a molecular mass of 18.4kDa.CAMP is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
CAMP protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
CAMP belongs to the antimicrobial peptide family, contains highly conserved N-terminal signal peptide, a cathelin domain and a structurally variable cationic antimicrobial peptide that produced by extracellular proteolysis from the C-terminus. CAMP has numerous functions besides the antimicrobial activity such as: cell chemotaxis, immune mediator induction and inflammatory response regulation.
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Synonyms
CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.
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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 MGSQVLSYKE AVLRAIDGIN QRSSDANLYR LLDLDPRPTM DGDPDTPKPV SFTVKETVCP RTTQQSPEDC DFKKDGLVKR CMGTVTLNQA RGSFDISCDK DNKRFALLGD FFRKSKEKIG KEFKRIVQRI KDFLRNLVPR TES.
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 :
Myostatin HumanDescription:
Myostatin Human Recombinant
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
Product # :
CYT-418Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Myostatin Human Recombinant produced in E.Coli is a homodimer, non-glycosylated polypeptide chain containing 2 x 109 amino acids and having a total molecular mass of 24814 Dalton. The GDF-8 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the inhibition of the proliferation of MPC-11 cells is < 20ng/ml, corresponding to a Specific Activity of 50,000units/mg.More Info
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Introduction
GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.
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Synonyms
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Myostatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Myostatin 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 Myostatin in sterile 20mM HCl at 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Asp-Phe-Gly-Leu-Asp.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.55 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Myostatin as a Reference Standard.
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 :
PI16 HumanDescription:
Peptidase Inhibitor 16 Human Recombinant
Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.
Product # :
ENZ-113Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Peptidase Inhibitor 16 Human Recombinant is produced in HEK293 cells and fused with a C-terminal Flag Tag (11 amino acids). The PI16 Flag Tagged Fusion Protein is 45.7kDa protein containing a total of 426 amino acid residues and purified by proprietary chromatographic techniques.
Source
HEK293 (Human Embryonic Kidney cell line).
Formulation
PI16 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Peptidase Inhibitor 16 (PI16) which a member of the CRISP family, is a putative serine protease inhibitor. PI16 interacts with PSP94/MSMB. PI16 is expressed in the prostate, testis, ovary and intestine. It also concentrates in prostate cancer patient's sera. PI16 may serve as a marker following prostatectomy for prostate cancer.
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Synonyms
Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized PI16 Human recombinant 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 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
LTDEEKRLMV ELHNLYRAQV SPPASDMLHM RWDEELAAFA KAYARQCVWG HNKERGRRGE NLFAITDEGM DVPLAMEEWH HEREHYNLSA ATCSPGQMCG HYTQVVWAKT ERIGCGSHFC EKLQGVEETN IELLVCNYEP PGNVKGKRPY QEGTPCSQCP SGYHCKNSLC EPIGSPEDAQ DLPYLVTEAP SFRATEASDS RKMGTPSSLA TGIPAFLVTE VSGSLATKAL PAVETQAPTS LATKDPPSMA TEAPPCVTTE VPSILAAHSL PSLDEEPVTF PKSTHVPIPK SADKVTDKTK VPSRSPENSL DPKMSLTGAR ELLPHAQEEA EAEAELPPSS EVLASVFPAQ DKPGELQATL DHTGHTSSKS LPNFPNTSAT ANATGGRALA LQSSLPGAEG PDKPSVVSGL NSGPGAAADYKDDDDK.
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 :
CXCL4 Variant 1 HumanDescription:
Platelet Factor-4 Variant 1 Human Recombinant
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
Product # :
CHM-243Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CXCL4 Variant-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa. The CXCL4 Variant-1 is fused to 6xHis tag at N-Terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized without additives.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets . Its major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemocinfamily. Human PF4 is used for the proof of induced thrombocytopenia. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.
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Synonyms
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Human CXCL4 although stable at 25°C 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CXCL4 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
MHHHHHHEAE EDGDLQCLCV KTTSQVRPRH ITSLEVIKAG PHCPTAQLIA TLKNGRKICL DLQALLYKKI IKEHLES.
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 :
Cys-Protein-A/G/LDescription:
Cys-Protein A/G/L Recombinant
Product # :
PRO-1935Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Protein-A/G/L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at N-terminus. Protein- A/G/L is comprised of 5 IgG-binding regions of Protein A (E-D-A-B-C), 2 of protein G (C1-C3) and 5 of Protein L (B1-B2-B3-B4-B5) containing 806 amino acids in total and having a molecular mass of 89.3kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein- A/G/L to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein- A/G/L was lyophilized without any additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein-A/G/L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G/L 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 Protein-A/G/L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
CNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE GSGSGTYKLI LNGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTKAVDAETA EKAFKQYAND NGVDGVWTYD DATKTFTVTE EPRARPGSGS GKEETPETPE TDSEEEVTIK ANLIFANGST QTAEFKGTFE KATSEAYAYA DTLKKDNGEY TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT FEEATAEAYR YADALKKDNG EYTVDVADKG YTLNIKFAGK EKTPEEPKEE VTIKANLIYA DGKTQTAEFK GTFEEATAEA YRYADLLAKE NGKYTVDVAD KGYTLNIKFA GKEKTPEEPK EEVTIKANLI YADGKTQTAE FKGTFAEATA EAYRYADLLA KENGKYTADL EDGGYTINIR FAGKKVDEKP EEKEQVTIKE NIYFEDGTVQ TATFKGTFAE ATAEAYRYAD LLSKEHGKYT ADLEDGGYTI NIRFAG.
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 :
CSK HumanDescription:
C-Src Tyrosine Kinase Human Recombinant
Tyrosine-protein kinase CSK, C-Src kinase, Protein-tyrosine kinase CYL, CSK, C-Src Tyrosine Kinase.
Product # :
PKA-062Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CSK Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 473 amino acids (1-450) and having a molecular mass of 53.1 kDa.The CSK is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CSK protein (0.5mg/ml) is containing Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
C-Src Tyrosine Kinase, also known as CSK, regulates cell growth, migration, differentiation, and immune response. CSK Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases. CSK is a protein coding gene which suppresses signaling by several surface receptors. Among CSK's related pathways are PI-3K cascade and Signaling by FGFR.
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Synonyms
Tyrosine-protein kinase CSK, C-Src kinase, Protein-tyrosine kinase CYL, CSK, C-Src Tyrosine Kinase.
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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 MGSMSAIQAA WPSGTECIAK YNFHGTAEQD LPFCKGDVLT IVAVTKDPNW YKAKNKVGRE GIIPANYVQK REGVKAGTKL SLMPWFHGKI TREQAERLLY PPETGLFLVR ESTNYPGDYT LCVSCDGKVE HYRIMYHASK LSIDEEVYFE NLMQLVEHYT SDADGLCTRL IKPKVMEGTV AAQDEFYRSG WALNMKELKL LQTIGKGEFG DVMLGDYRGN KVAVKCIKND ATAQAFLAEA SVMTQLRHSN LVQLLGVIVE EKGGLYIVTE YMAKGSLVDY LRSRGRSVLG GDCLLKFSLD VCEAMEYLEG NNFVHRDLAA RNVLVSEDNV AKVSDFGLTK EASSTQDTGK LPVKWTAPEA LREKKFSTKS DVWSFGILLW EIYSFGRVPY PRIPLKDVVP RVEKGYKMDA PDGCPPAVYE VMKNCWHLDA AMRPSFLQLR EQLEHIKTHE LHL.
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 :
OSM Human, 195 a.aDescription:
Oncostatin-M Human Recombinant (195 a.a.)
OSM, MGC20461, Oncostatin M.
Product # :
CYT-735Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Oncostatin-M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids and having a molecular mass of 22kDa. The OSM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing 1xPBS pH-7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependent stimulation of the proliferation of human TF-1 cells is < 0.2ng/ml, corresponding to a specific activity of > 5.0x106 units/mg.More Info
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Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
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Synonyms
OSM, MGC20461, Oncostatin M.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Oncostatin M although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin 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 Oncostatin M 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
AAIGSCSKEY RVLLGQLQKQ TDLMQDTSRL LDPYIRIQGL DVPKLREHCR ERPGAFPSEE TLRGLGRRGF LQTLNATLGC VLHRLADLEQ RLPKAQDLER SGLNIEDLEK LQMARPNILG LRNNIYCMAQ LLDNSDTAEP TKAGRGASQP PTPTPASDAF QRKLEGCRFL HGYHRFMHSV GRVFSKWGES PNRSR.
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 :
CRISP2 HumanDescription:
Cysteine-Rich Secretory Protein 2 Human Recombinant
Cysteine-Rich Secretory Protein 2, Cancer/Testis Antigen 36, TPX1, Testis Specific Protein 1 (Probe H4-1 P3-1), Testis-Specific Protein TPX-1, CRISP-2, GAPDL5, TSP1, CT36, Glyceraldehyde-3-Phosphate Dehydrogenase-Like 5, CRISP2.
Product # :
PRO-2030Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CRISP2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (22-243) containing 232 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 26.32kDa.
Source
Escherichia Coli.
Formulation
CRISP2 filtered (0.4µm) solution at a concentration of 0.3mg/ml in 50mM acetate buffer, pH 4, 5mM DTT and 20%glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cysteine-Rich Secretory Protein 2 (CRISP2) regulates some ion channels activity and thereby regulates calcium fluxes during sperm capacitation. Amongst its related pathways are p53 signaling. Diseases related with CRISP2 include epididymitis and orchitis.
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Synonyms
Cysteine-Rich Secretory Protein 2, Cancer/Testis Antigen 36, TPX1, Testis Specific Protein 1 (Probe H4-1 P3-1), Testis-Specific Protein TPX-1, CRISP-2, GAPDL5, TSP1, CT36, Glyceraldehyde-3-Phosphate Dehydrogenase-Like 5, CRISP2.
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Physical Appearance
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
MKHHHHHHASKDPAFTALLT TQLQVQREIV NKHNELRKAV SPPASNMLKM EWSREVTTNA QRWANKCTLQ HSDPEDRKTS TRCGENLYMS SDPTSWSSAI QSWYDEILDF VYGVGPKSPN AVVGHYTQLV WYSTYQVGCG IAYCPNQDSL KYYYVCQYCP AGNNMNRKNT PYQQGTPCAG CPDDCDKGLC TNSCQYQDLL SNCDSLKNTA GCEHELLKEK CKATCLCENK IY.
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 :
CTSL MouseDescription:
Cathepsin-L Mouse Recombinant
Cathepsin L1, Cathepsin L, Major excreted protein, MEP, p39 cysteine proteinase.
Product # :
ENZ-944Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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Description
CTSL Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 325 amino acids (18-334a.a.) and having a molecular mass of 36.8kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CTSL is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CTSL protein solution (0.25mg/ml) containing 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
Cathepsin-L also known as CTSL is a member of the peptidase C1 family. CTSL, is a dimer composed of disulfide-linked heavy and light chains, both formed from a single protein precursor. Furthermore, CTSL is a lysosomal cysteine proteinase which takes a main part in intracellular protein catabolism. CTSL substrates include collagen and elastin, as well as alpha-1 protease inhibitor, which is the most important controlling element of neutrophil elastase activity. CTSL has been implicated in a number of pathologic processes, including myofibril necrosis in myopathies and in myocardial ischemia, and in the renal tubular response to proteinuria. Multiple alternatively spliced transcript variants have been found for CTSL.
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Synonyms
Cathepsin L1, Cathepsin L, Major excreted protein, MEP, p39 cysteine proteinase.
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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
TPKFDQTFSA EWHQWKSTHR RLYGTNEEEW RRAIWEKNMR MIQLHNGEYS NGQHGFSMEM NAFGDMTNEE FRQVVNGYRH QKHKKGRLFQ EPLMLKIPKS VDWREKGCVT PVKNQGQCGS CWAFSASGCL EGQMFLKTGK LISLSEQNLV DCSHAQGNQG CNGGLMDFAF QYIKENGGLD SEESYPYEAK DGSCKYRAEF AVANDTGFVD IPQQEKALMK AVATVGPISV AMDASHPSLQ FYSSGIYYEP NCSSKNLDHG VLLVGYGYEG TDSNKNKYWL VKNSWGSEWG MEGYIKIAKD RDNHCGLATA ASYPVVNLEH HHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CDO1 HumanDescription:
Cysteine Dioxygenase Human Recombinant
Cysteine dioxygenase type 1, Cysteine dioxygenase type I, CDO-I, CDO, CDO1.
Product # :
ENZ-449Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CDO1 Human Recombinant fused with a 37 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids (1-170 a.a.) and having a molecular mass of 23.9kDa.The CDO1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CDO1 solution contains 20mM Tris buffer(pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CDO1 (Cysteine dioxygenase) is a mammalian non-heme iron enzyme that initiates a number of significant metabolic pathways associated with pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. CDO1 catalyzes the conversion of L-cysteine to cysteine sulfinic acid (cysteine sulfinate) by incorporation of dioxygen. CDO1 is a vital regulator of cellular cysteine concentrations and has an essential role in maintaining the hepatic concentration of intracellular free cysteine within a proper narrow range. CDO1 is able to alter intracellular cysteine levels and glutathione levels. CDO1 is highly expressed in the liver and placenta. On the other hand CDO1 has a low expression in heart, brain and pancreas. CDO1 can also be detected in hepatoblastoma HepG2 cells.
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Synonyms
Cysteine dioxygenase type 1, Cysteine dioxygenase type I, CDO-I, CDO, CDO1.
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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 KDRWGSHMEQ TEVLKPRTLA DLIRILHQLF AGDEVNVEEV QAIMEAYESD PTEWAMYAKF DQYRYTRNLV DQGNGKFNLM ILCWGEGHGS SIHDHTNSHC FLKMLQGNLK ETLFAWPDKK SNEMVKKSER VLRENQCAYI NDSVGLHRVE NISHTEPAVS LHLYSPPFDT CHAFDQR.
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 :
CSNK2B HumanDescription:
Casein Kinase 2 beta Human Recombinant
PKCK2 Beta, PKCK2B, CK2N, CSK2B, MGC138222, MGC138224, G5A, Phosvitin, Casein Kinase 2 beta, Casein Kinase 2B, Casein Kinase 2 beta, Casein kinase 2 beta polypeptide, Casein kinase II subunit beta, CK II beta, CK2B, CSNK 2B, CSNK2B, G5A
Product # :
PKA-129Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CSNK2B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 215 amino acids (1-215 a.a) and having a molecular mass of 24.9 kDa.CSNK2B is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CSNK2B protein solution (1mg/ml) in 0.2M NaCl, 20mM Tris-HCl buffer (pH 8.0), 1mM EDTA, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Casein Kinase 2 beta (CSNK2B) is a ubiquitous Ser/Thr kinase expressed in all eukaryotes. CSNK2Bis atetramer comprised of 2 catalytic kinase domains, alpha subunits and 2 identical regulatory beta subunits.CSNK2Btakes part incell cycle control, DNA repair,regulation of the circadian rhythm and other cellularprocesses. The beta subunit itself confers stability to the CK2 alpha subunitand is involved in activity and substrate specificity but does not have kinase activity.
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Synonyms
PKCK2 Beta, PKCK2B, CK2N, CSK2B, MGC138222, MGC138224, G5A, Phosvitin, Casein Kinase 2 beta, Casein Kinase 2B, Casein Kinase 2 beta, Casein kinase 2 beta polypeptide, Casein kinase II subunit beta, CK II beta, CK2B, CSNK 2B, CSNK2B, G5A
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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
MSSSEEVSWI SWFCGLRGNE FFCEVDEDYI QDKFNLTGLN EQVPHYRQAL DMILDLEPDE ELEDNPNQSD LIEQAAEMLY GLIHARYILT NRGIAQMLEK YQQGDFGYCP RVYCENQPML PIGLSDIPGE AMVKLYCPKC MDVYTPKSSR HHHTDGAYFG TGFPHMLFMV HPEYRPKRPA NQFVPRLYGF KIHPMAYQLQ LQAASNFKSP VKTIR
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 :
CTSZ Mouse, ActiveDescription:
Cathepsin-Z, Active Mouse Recombinant
Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.
Product # :
ENZ-1108Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CTSZ Mouse Recombinant produced in Baculovirus is a single, glycosylated, polypeptide chain containing 292 amino acids (23-306 aa) and having a molecular mass of 32.8kDa.CTSZ is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The CTSZ solution (0.5 mg/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. One unit will convert 1 pmole of Mca-PLGL-Dpa-AR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25°C.
More Info
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Introduction
Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and a member of the peptidase C1 family. CTSZ, which is known also as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and as other members of this family, takes part in tumorigenesis.
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Synonyms
Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.
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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
ARARLYFRSG QTCYHPIRGD QLALLGRRTY PRPHEYLSPA DLPKNWDWRN VNGVNYASVT
RNQHIPQYCG SCWAHGSTSA MADRINIKRK GAWPSILLSV QNVIDCGNAG SCEGGNDLPV
WEYAHKHGIP DETCNNYQAK DQDCDKFNQC GTCTEFKECH TIQNYTLWRV GDYGSLSGRE
KMMAEIYANG PISCGIMATE MMSNYTGGIY AEHQDQAVIN HIISVAGWGV SNDGIEYWIV
RNSWGEPWGE KGWMRIVTST YKGGTGDSYN LAIESACTFG DPIVLEHHHH HH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.