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1000 results found for “uteroglobin”
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Name :
CIAO1 HumanDescription:
Cytosolic Iron-Sulfur Protein Assembly 1 Human Recombinant
CIA1, WDR39, Probable cytosolic iron-sulfur protein assembly protein CIAO1, WD repeat-containing protein 39, CIAO1.
Product # :
PRO-1396Price :
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Description
CIAO1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 362 amino acids (1-339a.a) and having a molecular mass of 40kDa. CIAO1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CIAO1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CIAO1 is a vital component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. CIAO1 protein is required for the maturation of extra mitochondrial Fe/S proteins and seems to specifically modulate the trans-activation activity of WT1. CIAO1 participates in chromosome segregation as a part of the mitotic spindle-associated MMXD complex.
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Synonyms
CIA1, WDR39, Probable cytosolic iron-sulfur protein assembly protein CIAO1, WD repeat-containing protein 39, CIAO1.
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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 MGSMKDSLVL LGRVPAHPDS RCWFLAWNPA GTLLASCGGD RRIRIWGTEG DSWICKSVLS EGHQRTVRKV AWSPCGNYLA SASFDATTCI WKKNQDDFEC VTTLEGHENE VKSVAWAPSG NLLATCSRDK SVWVWEVDEE DEYECVSVLN SHTQDVKHVV WHPSQELLAS ASYDDTVKLY REEEDDWVCC ATLEGHESTV WSLAFDPSGQ RLASCSDDRT VRIWRQYLPG NEQGVACSGS DPSWKCICTL SGFHSRTIYD IAWCQLTGAL ATACGDDAIR VFQEDPNSDP QQPTFSLTAH LHQAHSQDVN CVAWNPKEPG LLASCSDDGE VAFWKYQRPE GL.
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 :
VAMP8 HumanDescription:
Endobrevin Human Recombinant
VAMP8, VAMP-8, Endobrevin, Vesicle-Associated Membrane Protein 8, EDB.
Product # :
PRO-660Price :
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Description
VAMP8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 96 amino acids (1-76 a.a.) and having a molecular mass of 10.9 kDa. The VAMP8 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatography techniques.
Source
Escherichia Coli.
Formulation
The VAMP8 protein solution (0.25mg/ml) contains 20mM Tris pH-8, 0.1mM PMSF, 0.2M NaCl and 50% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
VAMP8 also called endobrevin, is the main component of a SNARE complex involved in the docking and fusion of synaptic vesicles with the presynaptic membrane. VAMP8 protein is involved in the regulatation of enzyme secretion in pancreatic acinar cells and plays a part in the abscission of the midbody during cell division, which leads to completely separate daughter cells. VAMP8 is essential for dense-granule secretion in platelets. VAMP8 is related with the perinuclear vesicular structures of the early endocytic compartment. VAMP8 interacts particularly with the soluble NSF-attachment protein (alpha-SNAP), through an VAMP8-containing SNARE complex.
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Synonyms
VAMP8, VAMP-8, Endobrevin, Vesicle-Associated Membrane Protein 8, EDB.
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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 prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEEASEGGGN DRVRNLQSEV EGVKNIMTQN VERILARGEN LEHLRNKTED LEATSEHFKT TSQKVARKFW WKNVKM.
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 :
VTA1 HumanDescription:
Vps20-Associated 1 Homolog Human Recombinant
Vacuolar protein sorting-associated protein VTA1 homolog, DRG-1, LYST-interacting protein 5, LIP5, SKD1-binding protein 1, SBP1, VTA1, C6orf55, DRG1My012, HSPC228.
Product # :
PRO-1044Price :
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Description
VTA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-307 a.a.) and having a molecular mass of 36.5kDa.VTA1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
VTA1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 200mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Vps20-associated 1 homolog (VTA1) is a member of the VTA1 family. The VTA1 protein is involved in the endosomal multivesicular bodies (MVB) pathway. Furthermore, VTA1 is interacts with CHMP1B, CHMP2A, CHMP5, VPS4B, KIAA0174 (IST1) and possibly CHMP3. VTA1 is believed to be a cofactor of VPS4A/B, which catalyzes membrane-associated ESCRT-III assemblies. In addition, VTA1 is involved in the sorting and down-regulation of EGFR and also in HIV-1 budding.
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Synonyms
Vacuolar protein sorting-associated protein VTA1 homolog, DRG-1, LYST-interacting protein 5, LIP5, SKD1-binding protein 1, SBP1, VTA1, C6orf55, DRG1My012, HSPC228.
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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 MGSHMAALAP LPPLPAQFKS IQHHLRTAQE HDKRDPVVAY YCRLYAMQTG MKIDSKTPEC RKFLSKLMDQ LEALKKQLGD NEAITQEIVG CAHLENYALK MFLYADNEDR AGRFHKNMIK SFYTASLLID VITVFGELTD ENVKHRKYAR WKATYIHNCL KNGETPQAGP VGIEEDNDIE ENEDAGAASL PTQPTQPSSS STYDPSNMPS GNYTGIQIPP GAHAPANTPA EVPHSTGVAS NTIQPTPQTI PAIDPALFNT ISQGDVRLTP EDFARAQKYC KYAGSALQYE DVSTAVQNLQ KALKLLTTGR E.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
YWHAB HumanDescription:
Tyr-3/Trp- 5 Monooxygenase Activation Protein Beta Human Recombinant
14-3-3 protein beta/alpha, Protein kinase C inhibitor protein 1, Protein 1054, YWHAB, HS1, GW128, KCIP-1, Tyr-3/Trp- 5 Monooxygenase Activation Protein Beta, 14-3-3 Beta.
Product # :
PKA-348Price :
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Description
YWHAB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 246 amino acids (1-246) and having a molecular mass of 28kDa. YWHAB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The YWHAB protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM EDTA & 50mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
YWHAB belongs to the 14-3-3 family of proteins which are in charge for signal transduction by binding to phosphoserine-containing proteins. YWHAB is found in both plants and mammals. YWHAB protein interacts with RAF1 and CDC25 phosphatases,thus linking mitogenic signaling and the cell cycle machinery. YWHAB is an adapter protein involved in the regulation of a large spectrum of both general and specialized signaling pathway. YWHAB binds to a large number of proteins by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.
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Synonyms
14-3-3 protein beta/alpha, Protein kinase C inhibitor protein 1, Protein 1054, YWHAB, HS1, GW128, KCIP-1, Tyr-3/Trp- 5 Monooxygenase Activation Protein Beta, 14-3-3 Beta.
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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
MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL ELLDKYLIPN ATQPESKVFY LKMKGDYFRY LSEVASGDNK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD
AGEGEN.
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 :
RND1 HumanDescription:
Rho Family GTPase 1 Human Recombinant
Rho family GTPase 1, GTP-binding protein, ras homolog gene family, member S, ARHS, RHOS, rho-related GTP-binding protein Rho6, RHO6, Rnd1, FLJ42294.
Product # :
PRO-893Price :
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Description
RND1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-200) and having a molecular mass of 24.5 kDa.The RND1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The RND1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 30% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
RND1 is a Rho-related GTPases that form a separate branch of the Rho family, since they are different in charge, size, and biochemical properties. RND1 is found in the activated GTP-bound form and performs as a negative regulator of actin assembly and of cell adhesion. RND1 assists in regulation of the organization of the actin cytoskeleton as a reaction to extracellular growth factors.
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Synonyms
Rho family GTPase 1, GTP-binding protein, ras homolog gene family, member S, ARHS, RHOS, rho-related GTP-binding protein Rho6, RHO6, Rnd1, FLJ42294.
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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 MKERRAPQPV VARCKLVLVG DVQCGKTAML QVLAKDCYPE TYVPTVFENY TACLETEEQR VELSLWDTSG SPYYDNVRPL CYSDSDAVLL CFDISRPETV DSALKKWRTE ILDYCPSTRV LLIGCKTDLR TDLSTLMELS HQKQAPISYE QGCAIAKQLG AEIYLEGSAF TSEKSIHSIF RTASMLCLNK PSPLPQKSPV
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 :
KRT20 HumanDescription:
Cytokeratin 20 Human Recombinant
Keratin type I cytoskeletal 20, Cytokeratin-20, CK-20, Keratin-20, K20, Protein IT, KRT20, CD20, CK20, KRT21, MGC35423.
Product # :
PRO-351Price :
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Shipped at Room temp
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Description
Cytokeratin 20 Human Recombinant produced in E.Coli is a single,non-glycosylated polypeptide chain having a molecular mass of 48,553 Dalton. The KRT20 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/1ml) was lyophilized after from a sterile solution containing 30mM Tris-HCL pH-8, 9.5M urea, 2mM DDT, 2mM EDTA and 10mM methylammonium chloride.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
KRT20 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. This cytokeratin is a major cellular protein of mature enterocytes and goblet cells and is specifically expressed in the gastric and intestinal mucosa. The type I cytokeratin genes are clustered in a region of chromosome 17q12-q21.
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Synonyms
Keratin type I cytoskeletal 20, Cytokeratin-20, CK-20, Keratin-20, K20, Protein IT, KRT20, CD20, CK20, KRT21, MGC35423.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized KRT20 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution KRT20 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 KRT20 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Reconstitution to filaments
Performed by mixing equimolar amounts of cytokeratins of type I and type II at concentrations of approx. 0.5 mg/ml, both dissolved in 9.5 M urea buffer (see above). Protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4 M urea and then to low salt condition (50 mM NaCI, 2 mM dithiothreitol, 10 mM Tris-HCI, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco's PBS).
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 :
METTL21A HumanDescription:
Methyltransferase Like 21A Human Recombinant
Protein N-lysine methyltransferase METTL21A, HSPA lysine methyltransferase, HSPA-KMT, Hepatocellular carcinoma-associated antigen 557b, Methyltransferase-like protein 21A, METTL21A, FAM119A, HCA557B, Methyltransferase Like 21A.
Product # :
ENZ-718Price :
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Description
METTL21A Human Recombinant produced in E. coli is a single polypeptide chain containing 149 amino acids (93-218) and having a molecular mass of 17 kDa.METTL21A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The METTL21A solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 30% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
METTL21A, which is a part of the methyltransferase superfamily, is a Protein-lysine methyltransferase that in vitro methylates HSPA1, HSPA5 and HSPA8.
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Synonyms
Protein N-lysine methyltransferase METTL21A, HSPA lysine methyltransferase, HSPA-KMT, Hepatocellular carcinoma-associated antigen 557b, Methyltransferase-like protein 21A, METTL21A, FAM119A, HCA557B, Methyltransferase Like 21A.
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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 MGSTDRKVAL EFLKSNVQAN LPPHIQTKTV VKELTWGQNL GSFSPGEFDL ILGADIIYLE ETFTDLLQTL EHLCSNHSVI LLACRIRYER DNNFLAMLER QFTVRKVHYD PEKDVHIYEA QKRNQKEDL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
BLVRB MouseDescription:
Biliverdin Reductase B Mouse Recombinant
Flavin reductase (NADPH), FR, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, NADPH-dependent diaphorase, NADPH-flavin reductase, FLR.
Product # :
ENZ-1074Price :
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Description
BLVRB Mouse Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (1-206 a.a) and having a molecular mass of 24.6kDa.BLVRB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BLVRB protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0) containing 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
BLVRB (EC 1.3.1.24) catalyzes electron transfer from reduced pyridine nucleotides to flavins as well as methylene blue, pyrroloquinoline quinone, riboflavin, or methemoglobin. BLVRB is involved in protecting cells from oxidative damage or in regulating iron metabolism. BLVRB converts biliverdin to bilirubin in the liver, converting a double-bond between the second and third pyrrole ring into a single-bond. BLVRB plays a role as in human erythrocytic heme catabolic pathway and most mammalian species. Biliverdin reductase is abundantly expressed in kidney, spleen, liver and brain as well as at lower levels in the thymus and minimal levels being detected in testis.
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Synonyms
Flavin reductase (NADPH), FR, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, NADPH-dependent diaphorase, NADPH-flavin reductase, FLR.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMTVKKIA IFGATGRTGL TTLAQAVQAG YEVTVLVRDS SRLPSEGPQP AHVVVGDVRQ AADVDKTVAG QEAVIVLLGT GNDLSPTTVM SEGTRNIVTA MKAHGVDKVV ACTSAFLLWD PTKVPPRLQD VTDDHIRMHK ILQESGLKYV AVMPPHIGDQ PLTGAYTVTL DGRGPSRVIS KHDLGHFMLR CLTTNEYDGH TTYPSHQYD.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CA10 HumanDescription:
Carbonic Anhydrase X Human Recombinant
Carbonic anhydrase-related protein 10, Carbonic anhydrase-related protein X, CA-RP X, CARP X, carbonic anhydrase X, Cerebral protein 15, hucep-15, epididymis secretory sperm binding protein, UNQ533/PRO1076.
Product # :
ENZ-1189Price :
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Description
CA10 Human Recombinant is a single, glycosylated polypeptide chain containing 317 amino acids (22-328a.a) and having a molecular mass of 36.3kDa (calculated). CA10 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
CA10 protein solution (0.5mg/ml) is filtered in Phosphate-Buffered Saline pH 7.4 and 10% (w/v) glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 150 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1pmole of pnitrophenyl acetate to p-nitrophenol per minute at pH8.0 at 37℃.
Citations
More Info
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Synonyms
Carbonic anhydrase-related protein 10, Carbonic anhydrase-related protein X, CA-RP X, CARP X, carbonic anhydrase X, Cerebral protein 15, hucep-15, epididymis secretory sperm binding protein, UNQ533/PRO1076.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
DGSMQQNSPK IHEGWWAYKE VVQGSFVPVP SFWGLVNSAW NLCSVGKRQS PVNIETSHMI FDPFLTPLRI NTGGRKVSGT MYNTGRHVSL RLDKEHLVNI SGGPMTYSHR LEEIRLHFGS EDSQGSEHLL NGQAFSGEVQ LIHYNHELYT NVTEAAKSPN GLVVVSIFIK VSDSSNPFLN RMLNRDTITR ITYKNDAYLL QGLNIEELYP ETSSFITYDG SMTIPPCYET ASWIIMNKPV YITRMQMHSL RLLSQNQPSQ IFLSMSDNFR PVQPLNNRCI RTNINFSLQG KDCPNNRAQK LQYRVNEWLL KHHHHHH
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Background
Carbonic anhydrases (CAs) are a family of enzymes that play a crucial role in regulating pH balance and carbon dioxide transport in various tissues and organs. Carbonic anhydrase X (CA10) is a less-studied member of this family, and this research aims to explore its structure, function, and implications in metabolism and disease. Understanding the molecular mechanisms and regulatory roles of CA10 can provide valuable insights into its potential as a therapeutic target for various disorders.
Structure and Expression of Carbonic Anhydrase X:
CA10, also known as mitochondrial carbonic anhydrase, is a membrane-associated protein predominantly found in the mitochondria of various tissues, including the liver, kidney, and brain. It possesses the characteristic zinc-binding catalytic domain found in other CAs. However, CA10 has distinct features, including a unique N-terminal mitochondrial targeting sequence, suggesting its specific role within mitochondria.
Role of Carbonic Anhydrase X in Metabolism:
CA10 is involved in the regulation of pH and bicarbonate concentrations within the mitochondrial matrix, impacting mitochondrial metabolism. It catalyzes the reversible hydration of carbon dioxide to bicarbonate, facilitating the exchange of carbon dioxide between the mitochondria and the cytoplasm. This process is vital for maintaining acid-base homeostasis and efficient energy production through oxidative phosphorylation.
Implications of Carbonic Anhydrase X in Disease:
Emerging evidence suggests that CA10 may be implicated in various pathological conditions. Alterations in CA10 expression or activity have been associated with metabolic disorders, including obesity and diabetes. Furthermore, dysregulation of mitochondrial function and pH homeostasis, in which CA10 plays a role, have been linked to neurodegenerative diseases, cancer, and cardiovascular disorders. Elucidating the precise contributions of CA10 in these pathologies is an area of active investigation.
Therapeutic Potential of Carbonic Anhydrase X:
The unique properties and expression patterns of CA10 make it an intriguing target for therapeutic interventions. Modulating CA10 activity or expression could have implications in metabolic disorders, where the manipulation of mitochondrial function and pH regulation could offer therapeutic benefits. Developing selective inhibitors or activators of CA10 could be explored to regulate its enzymatic activity and modulate mitochondrial metabolism.
Challenges and Future Directions:
Although CA10 shows promise as a therapeutic target, several challenges remain. The elucidation of the precise regulatory mechanisms and signaling pathways involving CA10 within mitochondria is necessary for a comprehensive understanding of its function. Additionally, the development of specific modulators that selectively target CA10 without affecting other CAs or disrupting physiological processes is a critical consideration.
Conclusion:
The study of CA10 protein provides valuable insights into its distinct role in mitochondrial metabolism and disease pathogenesis. Understanding the molecular mechanisms and functional implications of CA10 opens avenues for the development of targeted therapies for metabolic disorders, neurodegenerative diseases, cancer, and cardiovascular disorders. Further research on CA10, its interactions, and its modulation in pathological conditions will contribute to the development of novel therapeutic interventions to improve patient outcomes.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
FLT1 HumanDescription:
Vascular Endothelial Growth Factor Receptor-1 Human Recombinant
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
Product # :
PKA-240Price :
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Shipped at Room temp
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Description
Soluble FLT1 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide containing 687 amino acids and having a molecular mass of 96 kDa. The soluble receptor protein contains only the first 6 extracellular domains, which contain all the information necessary for binding of VEGF.The FLT1 is purified by proprietary chromatographic techniques.
Source
Insect Cells.
Formulation
FLT1 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.
Purity
Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity of FLT1 was determined by its ability to inhibit the VEGF (165)-induced proliferation of HUVECs.
Citations
More Info
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Introduction
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.
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Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized FLT-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLT1 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 FLT1 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
SKLK DPELSLKGTQ HIMQAGQTLH LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK KEITIRGEHC NKKAVFSRIS KFKSTRNDCT TQSNVKH
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 :
POR Human, ActiveDescription:
P450 Oxidoreductase Human Recombinant, Active
P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.
Product # :
ENZ-1176Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
POR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 686 amino acids (1-680a.a.) and having a molecular mass of 77.9kDa. POR is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
POR protein solution (0.25mg/ml) contains Phosphate buffer saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 4,000 pmol/min/mg. Defined by the amount of enzyme that reduction of 1 pmole cytochrome-C by NADPH/min. at pH-8 25C.
Citations
More Info
-
Introduction
P450 Oxidoreductase, also known as POR is a flavoprotein which contributes electrons to all microsomal P450 enzymes. POR is localized to the endoplasmic reticulum, where it is also capable of transfering electrons to heme oxygenase as well as cytochrome b5. POR is structurally related to two separate flavoprotein families; first one is ferredoxin nucleotide reductase and the second flavodoxin.
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Synonyms
P450 (Cytochrome) Oxidoreductase, EC 1.6.2.4, CYPOR, P450R, CPR, NADPH-Dependent Cytochrome P450 Reductase, NADPH--Cytochrome P450 Reductase, NADPH--cytochrome P450 reductase.
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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.
-
Amino Acid Sequence
MINMGDSHVD TSSTVSEAVA EEVSLFSMTD MILFSLIVGL LTYWFLFRKK KEEVPEFTKI QTLTSSVRES SFVEKMKKTG RNIIVFYGSQ TGTAEEFANR LSKDAHRYGM RGMSADPEEY DLADLSSLPE IDNALVVFCM ATYGEGDPTD NAQDFYDWLQ ETDVDLSGVK FAVFGLGNKT YEHFNAMGKY VDKRLEQLGA QRIFELGLGD DDGNLEEDFI TWREQFWLAV CEHFGVEATG EESSIRQYEL VVHTDIDAAK VYMGEMGRLK SYENQKPPFD AKNPFLAAVT TNRKLNQGTE RHLMHLELDI SDSKIRYESG DHVAVYPAND SALVNQLGKI LGADLDVVMS LNNLDEESNK KHPFPCPTSY RTALTYYLDI TNPPRTNVLY ELAQYASEPS EQELLRKMAS SSGEGKELYL SWVVEARRHI LAILQDCPSL RPPIDHLCEL LPRLQARYYS IASSSKVHPN SVHICAVVVE YETKAGRINK GVATNWLRAK EPVGENGGRA LVPMFVRKSQ FRLPFKATTP VIMVGPGTGV APFIGFIQER AWLRQQGKEV GETLLYYGCR RSDEDYLYRE ELAQFHRDGA LTQLNVAFSR EQSHKVYVQH LLKQDREHLW KLIEGGAHIY VCGDARNMAR DVQNTFYDIV AELGAMEHAQ AVDYIKKLMT KGRYSLDVWS 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.
- View Data Sheet
Name :
HIF1A Human (85 a.a.)Description:
Hypoxia-Inducible Factor-1 Alpha (85 a.a.) Human Recombinant
Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.
Product # :
PRO-258Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HIF1A Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 105 amino acids (1-85 a.a.) and having a molecular mass of 11.8 kDa. The HIF1A is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HIF1A Human (0.25mg/ml) solution containing 20mM Tris buffer(pH 8.0), 20% glycerol, 1mM DTT, 0.2M NaCl and 1mM EDTA.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
HIF1A has a role as a master transcriptional monitor of the adaptive response to hypoxia. Under hypoxic conditions HIF1A activates the transcription of over 40 genes, including, erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, and genes whose protein products increase oxygen release or facilitate metabolic adaptation to hypoxia. HIF1A functions as an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease.
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Synonyms
Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEGAGGANDK KKISSERRKE KSRDAARSRR SKESEVFYEL AHQLPLPHNV SSHLDKASVM RLTISYLRVR KLLDAGDLDI EDDMK.
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 :
ESR2 HumanDescription:
Estrogen Receptor 2 Human Recombinant
Estrogen Receptor Beta.
Product # :
PRO-2838Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The ESR2 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The ESR2 His-Tagged Fusion Protein, produced in E. coli, is a 10kDa protein containing 101 amino acid residues of the ESR2 Human, 216-316 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Synonyms
Estrogen Receptor Beta.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized ESR2 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Amino Acid Sequence
CGSR RERCGYRLVR RQRSADEQLH CAGKAKRSGGHAPRVRELLL DALSPEQLVL TLLEAEPPHV LISRPSAPFTEASMMMSLTKLADKELVHMI SWAKKI.
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Background
Estrogen Receptor 2 also known as ESR2 takes part in mediating the biological effects of estrogen, influencing various physiological and pathological processes. ESR2 is found in different tissues including the brain, reproductive organs, bones, cardiovascular system, and immune cells and has distinct functions. ESR2 is involved in various biological processes by responding to estrogen which is an important hormone in regulating reproductive and metabolic functions.
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 :
Protein-A/G, HisDescription:
Protein A/G Recombinant, His Tag
Product # :
PRO-1927Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Protein-A/G Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with a 6×His tag at C-terminus. Protein-A/G is comprised of 5 IgG-binding regions of protein A (E-D-A-B-C) and 3 of protein G (C1-C2-C3) containing 513 amino acids in total and having a molecular mass of 56.9kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein A/G to guarantee the maximum specific IgG binding.
Source
Escherichia Coli.
Formulation
Protein-A/G was lyophilized without any additives.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
-
Introduction
The recombinant Protein A/G is a genetically engineered protein comprised of 8 IgG-binding domains EDABC-C1C2C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1, C2 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Protein-A/G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Protein-A/G in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
-
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 GSGSGTYKLI LNGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTKAVDAETA EKAFKQYAND NGVDGVWTYD DATKTFTVTE KLAAALEHHH HHH.
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 :
ESM1 Human, SF9Description:
Endothelial Cell-Specific Molecule 1 Human Recombinant, Sf9
Endothelial Cell Specific Molecule 1, Endothelial Cell-Specific Molecule 1, ESM-1, Endocan.
Product # :
PRO-2588Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ESM1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 174 amino acids (20-184a.a.) and having a molecular mass of 19.2kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). ESM1 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ESM1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
ESM1, also knows as, Endothelial cell-specific molecule 1 is a protein encoded by a gene called ESM1 in humans. ESM1 is a secreted protein that is highly expressed in human kidney and lung tissues (in the endothelial cells). There are suggestions regarding the protein’s involvement in endothelium-dependent pathological diseases, due to his regulation that is performed by cytokines.
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Synonyms
Endothelial Cell Specific Molecule 1, Endothelial Cell-Specific Molecule 1, ESM-1, Endocan.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADLWSNNYAV DCPQHCDSSE CKSSPRCKRT VLDDCGCCRV CAAGRGETCY RTVSGMDGMK CGPGLRCQPS NGEDPFGEEF GICKDCPYGT FGMDCRETCN CQSGICDRGT GKCLKFPFFQ YSVTKSSNRF VSLTEHDMAS GDGNIVREEV VKENAAGSPV MRKWLNPRHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
KCTD5 HumanDescription:
Potassium Channel Tetramerisation Domain Containing 5 Human Recombinant
BTB/POZ domain-containing protein KCTD5, KCTD5.
Product # :
PRO-1276Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KCTD5 Human Recombinant produced in E. coli is a single polypeptide chain containing 257 amino acids (1-234) and having a molecular mass of 28.5 kDa. KCTD5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The KCTD5 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
BTB/POZ domain-containing protein KCTD5 (KCTD5), is a 234 amino acid protein which localizes mainly in the cytoplasm however translocates to the nucleus on interaction with REP proteins. The expression of KCTD5 is up regulated post-transcriptionally in peripheral blood lymphocytes stimulated via the T-cell receptor. KCTD5 interacts particularly with cullin3, attaches ubiquitinated proteins, and created oligomers through its BTB domain.
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Synonyms
BTB/POZ domain-containing protein KCTD5, KCTD5.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAENHCE LLSPARGGIG AGLGGGLCRR CSAGLGALAQ RPGSVSKWVR LNVGGTYFLT TRQTLCRDPK SFLYRLCQAD PDLDSDKDET GAYLIDRDPT YFGPVLNYLR HGKLVINKDL AEEGVLEEAE FYNITSLIKL VKDKIRERDS KTSQVPVKHV YRVLQCQEEE LTQMVSTMSD GWKFEQLVSI GSSYNYGNED QAEFLCVVSK ELHNTPYGTA SEPSEKAKIL QERGSRM
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 :
YWHAB Human, HisDescription:
Tyr-3/Trp-5 Monooxygenase Activation Protein, Beta, Human Recombinant, His Tag
14-3-3 protein beta/alpha, Protein kinase C inhibitor protein 1, Protein 1054, YWHAB, HS1, GW128, KCIP-1, Tyr-3/Trp- 5 Monooxygenase Activation Protein Beta, 14-3-3 Beta.
Product # :
PKA-096Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
YWHAB Human Recombinant produced in E. coli is a single polypeptide chain containing 270 amino acids (1-246) and having a molecular mass of 30.6kDa. YWHAB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The YWHAB solution (1mg/1ml) contains phosphate buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
YWHAB belongs to the 14-3-3 family of proteins which are in charge for signal transduction by binding to phosphoserine-containing proteins. YWHAB is found in both plants and mammals. YWHAB protein interacts with RAF1 and CDC25 phosphatases,thus linking mitogenic signaling and the cell cycle machinery. YWHAB is an adapter protein involved in the regulation of a large spectrum of both general and specialized signaling pathway. YWHAB binds to a large number of proteins by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.
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Synonyms
14-3-3 protein beta/alpha, Protein kinase C inhibitor protein 1, Protein 1054, YWHAB, HS1, GW128, KCIP-1, Tyr-3/Trp- 5 Monooxygenase Activation Protein Beta, 14-3-3 Beta.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMTMDKS ELVQKAKLAE QAERYDDMAA AMKAVTEQGH ELSNEERNLL SVAYKNVVGA RRSSWRVISS IEQKTERNEK KQQMGKEYRE KIEAELQDIC NDVLELLDKY LIPNATQPES KVFYLKMKGD YFRYLSEVAS GDNKQTTVSN SQQAYQEAFE ISKKEMQPTH PIRLGLALNF SVFYYEILNS PEKACSLAKT AFDEAIAELD TLNEESYKDS TLIMQLLRDN LTLWTSENQG DEGDAGEGEN.
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 :
EPO MouseDescription:
Erythropoietin Mouse Recombinant
Erythropoietin, erythropoietin isoform 1 precursor, Epo.
Product # :
CYT-1171Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
- Citations
Description
EPO Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 176 amino acids (27-192 aa) and having a molecular mass of 19.8kDa.EPO is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EPO Mouse protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.
sds-page
Citations
More Info
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Introduction
Erythropoietin or EPO is a hormone (glycoprotein), part of the type I cytokine group of proteins. EPO is found mainly in the kidney tissue, produced from fibroblast-like cortical interstitial cells near the proximal tubules. EPO is also present in the blood, where it acts as red cell production regulator, by the promotion of differentiation of erythroid and thereby starts hemoglobin synthesis. Furthermore, EPO has neuroprotective activity towards brain injuries & anti-apoptotic activity in different tissues.
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Synonyms
Erythropoietin, erythropoietin isoform 1 precursor, Epo.
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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
ADPMAPPRLI CDSRVLERYI LEAKEAENVT MGCAEGPRLS ENITVPDTKV NFYAWKRMEV EEQAIEVWQG LSLLSEAILQ AQALLANSSQ PPETLQLHID KAISGLRSLT SLLRVLGAQK ELMSPPDTTP PAPLRTLTVD TFCKLFRVYA NFLRGKLKLY TGEVCRRGDR HHHHHH.
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Background
What is the molecular weight/Mw of EPO Protein?
EPO Protein has a total Mw of 19.8kDa.
What is the source or expression system of EPO Protein?
Sf9, Baculovirus cells.
What is the Purity of EPO Protein?
EPO Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EPO Protein?
Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.
What is the amino acid sequence of EPO Protein?
ADPMAPPRLI CDSRVLERYI LEAKEAENVT MGCAEGPRLS ENITVPDTKV NFYAWKRMEV EEQAIEVWQG LSLLSEAILQ AQALLANSSQ PPETLQLHID KAISGLRSLT SLLRVLGAQK ELMSPPDTTP PAPLRTLTVD TFCKLFRVYA NFLRGKLKLY TGEVCRRGDR HHHHHH.
What applications can EPO Protein be used in?
EPO Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EPO Protein?
The endotoxin level is minimal, EPO 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.
- View Data Sheet
Name :
BIN2 HumanDescription:
Bridging Integrator 2 Human Recombinant
Bridging Integrator 2, Breast Cancer-Associated Protein 1, Breast Cancer Associated Protein BRAP1, BRAP-1, BRAP1, BIN2.
Product # :
PRO-2485Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
BIN2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (1-597 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 606 amino acids and having a molecular mass of 66.1kDa.BIN2 shows multiple bands between 70-100kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
BIN2 protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 20% glycerol, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
BIN2, also known as Bridging Integrator 2, is a cytoplasmic protein. BIN2 comprises one BAR domain and Interacts with BIN1. BIN2 is highly expressed in some hematopoietic tissues, including peripheral blood, colon, thymus and placenta. BIN2 stimulates cell motility and migration, most likely through its interaction with the cell membrane and with podosome proteins which mediate interaction with the cytoskeleton and likewise modulates membrane curvature & mediates membrane tubulation.
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Synonyms
Bridging Integrator 2, Breast Cancer-Associated Protein 1, Breast Cancer Associated Protein BRAP1, BRAP-1, BRAP1, BIN2.
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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
ADPMRGMPGA RTSSSGASEN HRARGQGGGP QGVGRMAEGK AGGAAGLFAK QVQKKFSRAQ EKVLQKLGKA VETKDERFEQ SASNFYQQQA EGHKLYKDLK NFLSAVKVMH ESSKRVSETL QEIYSSEWDG HEELKAIVWN NDLLWEDYEE KLADQAVRTM EIYVAQFSEI KERIAKRGRK LVDYDSARHH LEAVQNAKKK DEAKTAKAEE EFNKAQTVFE DLNQELLEEL PILYNSRIGC YVTIFQNISN LRDVFYREMS KLNHNLYEVM SKLEKQHSNK VFVVKGLSSS SRRSLVISPP VRTATVSSPL TSPTSPSTLS LKSESESVSA TEDLAPDAAQ GEDNSEIKEL LEEEEIEKEG SEASSSEEDE PLPACNGPAQ AQPSPTTERA KSQEEVLPSS TTPSPGGALS PSGQPSSSAT EVVLRTRTAS EGSEQPKKRA SIQRTSAPPS RPPPPRATAS PRPSSGNIPS SPTASGGGSP TSPRASLGTG TASPRTSLEV SPNPEPPEKP VRTPEAKENE NIHNQNPEEL CTSPTLMTSQ VASEPGEAKK MEDKEKDNKL ISANSSEGQD QLQVSMVPEN NNLTAPEPQE EVSTSENPQL 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.
- View Data Sheet
Name :
WIF1 HumanDescription:
WNT Inhibitory Factor 1 Human Recombinant
WIF1, WIF-1, Wnt inhibitory factor 1.
Product # :
PRO-684Price :
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Shipped with Ice Packs
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Description
WIF1 Human is a single, glycosylated polypeptide chain containing 360 amino acids (29-379 a.a.) and having a molecular mass of 39.5 kDaWIF1 is fused to 6 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The WIF1 protein solution contains 1X PBS pH 7.4, 20% glycerol, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
WIF1 binds to wnt proteins and inhibits their activities. WIF1 plays a role in mesoderm segmentation. WNT proteins are extracellular signaling molecules that take part in the control of embryonic development & cancer. WIF1 protein contains a WNT inhibitory factor (WIF) domain and 5 epidermal growth factor (EGF)-like domains. WIF1 takes part in mesoderm segmentation. WIF1 protein is found to be present in fish, amphibia and mammals. WIF1 is a recurrent target in human salivary gland oncogenesis. Downregulation of WIF1 takes part in the development and progression of pleomorphic adenomas. WIF1 is a tumor suppressor, specifically in nonfunctioning pituitary tumors.
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Synonyms
WIF1, WIF-1, Wnt inhibitory factor 1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADLGPPQEES LYLWIDAHQA RVLIGFEEDI LIVSEGKMAP FTHDFRKAQQ RMPAIPVNIH SMNFTWQAAG QAEYFYEFLS LRSLDKGIMA DPTVNVPLLG TVPHKASVVQ VGFPCLGKQD GVAAFEVDVI VMNSEGNTIL QTPQNAIFFK TCQQAECPGG CRNGGFCNER RICECPDGFH GPHCEKALCT PRCMNGGLCV TPGFCICPPG FYGVNCDKAN CSTTCFNGGT CFYPGKCICP PGLEGEQCEI SKCPQPCRNG GKCIGKSKCK CSKGYQGDLC SKPVCEPGCG AHGTCHEPNK CQCQEGWHGR HCNKRYEASL IHALRPAGAQ LRQHTPSLKK AEERRDPPES NYIWHHHHHH
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 :
TK1 HumanDescription:
Thymidine Kinase 1 Human Recombinant
Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.
Product # :
PKA-036Price :
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Shipped with Ice Packs
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Description
TK1 Human Recombinant produced in E. coli is a single polypeptide chain containing 258 amino acids (1-234) and having a molecular mass of 28.0 kDa.TK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TK1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Thymidine Kinase 1 (TK1) is a phosphotransferase (a kinase): 2'-deoxythymidine kinase, ATP-thymidine 5'-phosphotransferase. TK1 is present in 2 forms in mammalian cells, TK1 and TK2. Thymidine kinases hold a main function in the synthesis of DNA and thus in cell division, as they are part of the distinctive reaction chain to introduce deoxythymidine (present in the body fluids as a result of degradation of DNA from food and from dead cells) into the DNA. Thymidine kinase is necessary for the action of many antiviral drugs. Thymidine kinase is used to select hybridoma cell lines in production of monoclonal antibodies.
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Synonyms
Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.
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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 MGSHMSCINL PTVLPGSPSK TRGQIQVILG PMFSGKSTEL MRRVRRFQIA QYKCLVIKYA KDTRYSSSFC THDRNTMEAL PACLLRDVAQ EALGVAVIGI DEGQFFPDIV EFCEAMANAG KTVIVAALDG TFQRKPFGAI LNLVPLAESV VKLTAVCMEC FREAAYTKRL GTEKEVEVIG GADKYHSVCR LCYFKKASGQ PAGPDNKENC PVPGKPGEAV AARKLFAPQQ ILQCSPAN.
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 :
YWHAG AntibodyDescription:
YWHAG Mouse Anti Human
14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3 monooxygenase/tryptophan 5-monooxygenase activation protein gamma polypeptide.
Product # :
ANT-539Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
- Western Blot, ICC/IF
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
Western Blot, ICC/IF
Citations
More Info
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Introduction
The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms that have been identified in mammals. The 14-3-3gamma, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.
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Synonyms
14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3 monooxygenase/tryptophan 5-monooxygenase activation protein gamma polypeptide.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human YWHAG mAb, clone PAT4B9AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human YWHAG protein 1-247 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and k light chain.
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Clone
PAT4B9AT.
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Applications
The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
YWHAG antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
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 :
ABO HumanDescription:
ABO Blood Group Human Recombinant
Histo-blood group ABO system transferase, Fucosylglycoprotein 3-alpha-galactosyltransferase, Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-galactosyltransferase, Histo-blood group A transferase, A transferase, Histo-blood group B transferase, B transferase, NAGAT, ABO, GTB, A3GALNT, A3GALT1.
Product # :
ENZ-167Price :
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Shipped with Ice Packs
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Description
ABO Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (54-354 a.a) and having a molecular mass of 37.4kDa.ABO is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ABO protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 200mM NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
NAGAT (ABO) is a member of the glycosyltransferase 6 family. The ABO protein is the basis of the ABO blood group system and related to the first discovered blood group system, ABO. The allele that is present in an individual determines the blood group. The histo-blood group ABO is comprised of 3 carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity which converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals are deficient of such activity.
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Synonyms
Histo-blood group ABO system transferase, Fucosylglycoprotein 3-alpha-galactosyltransferase, Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-galactosyltransferase, Histo-blood group A transferase, A transferase, Histo-blood group B transferase, B transferase, NAGAT, ABO, GTB, A3GALNT, A3GALT1.
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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 MAVREPDHLQ RVSLPRMVYP QPKVLTPCRK DVLVVTPWLA PIVWEGTFNI DILNEQFRLQ NTTIGLTVFA IKKYVAFLKL FLETAEKHFM VGHRVHYYVF TDQPAAVPRV TLGTGRQLSV LEVRAYKRWQ DVSMRRMEMI SDFCERRFLS EVDYLVCVDV DMEFRDHVGV EILTPLFGTL HPGFYGSSRE AFTYERRPQS QAYIPKDEGD FYYLGGFFGG SVQEVQRLTR ACHQAMMVDQ ANGIEAVWHD ESHLNKYLLR HKPTKVLSPE YLWDQQLLGW PAVLRKLRFT AVPKNHQAVR NP.
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 :
S100A8 Human, HisDescription:
S100 Calcium Binding Protein A8 Human Recombinant, His Tag
Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.
Product # :
PRO-150Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Recombinant Human S100A8 produced in E.coli has a molecular mass of 12.08kDa containing 103 amino acid residues of the human S100A8 and fused to a 10 a.a. His tag at N-terminus.
Source
Escherichia Coli.
Formulation
S100A8 was filtered (0.4µm) and lyophilized in 0.5mg/ml in 20mM Tris and 100mM NaCl, pH 7.5.
Citations
More Info
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Introduction
S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.
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Synonyms
Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.
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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
MKHHHHHHAS MLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI NTDGAVNFQEMLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI NTDGAVNFQE FLILVIKMGV AAHKKSHEES HKE.
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.