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1000 results found for “Cyclin”
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Name :
C-JUN Human (241 a.a.)Description:
Jun Proto-Oncogene (1-241 a.a.) Human Recombinant
Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.
Product # :
PKA-001Price :
Quantity :
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Shipped with Ice Packs
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Description
C-JUN Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 261 amino acids (1-241 a.a.) and having a molecular mass of 27.3kDa. The C-JUN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The C-JUN solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
C-JUN is a gene which, in combination with c-Fos, forms the AP-1early response transcription factor. C-JUN is activated by the JNKpathway. C-JUN is the putative transforming gene of avian sarcoma virus 17. C-JUN is a protein which is highly similar to the viral protein, and which interacts directly with specific target DNA sequences to regulate gene expression. The C-JUN gene is intronless and is mapped to 1p32-p31, a chromosomal region involved in both translocations and deletions in human malignancies.
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Synonyms
Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.
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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 MTAKMETTFY DDALNASFLP SESGPYGYSN PKILKQSMTL NLADPVGSLK PHLRAKNSDL LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE LHSQNTLPSV TSAAQPVNGA GMVAPAVASV AGGSGSGGFS ASLHSEPPVY ANLSNFNPGA LSSGGGAPSY GAAGLAFPAQ PQQQQQPPHH LPQQMPVQHP RLQALKEEPQ TVPEMPGETP P.
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 :
CNTF HumanDescription:
Ciliary-Neurotrophic Factor Human Recombinant
HCNTF, CNTF, Ciliary Neurotrophic Factor.
Product # :
CYT-272Price :
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Shipped at Room temp
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Description
Ciliary Neurotrophic Factor Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and having a molecular mass of 22706 Dalton. The CNTF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 5mM sodium Phosphate buffer pH=7.5 and 5mM sodium chloride.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.More Info
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Introduction
CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. -
Synonyms
HCNTF, CNTF, Ciliary Neurotrophic Factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Ciliary Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CNTF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized HCNTF 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
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Phe-Thr-Glu.
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Background
Exploring the Potential of Human Recombinant Ciliary-Neurotrophic Factor: Implications and Applications
Abstract:
Ciliary-Neurotrophic Factor (CNTF) holds remarkable promise in neurobiology and therapeutic development due to its neuroprotective and regenerative properties. This paper delves into the significance of Human Recombinant CNTF, its production methodologies, and its potential applications in treating neurodegenerative disorders. The review sheds light on the therapeutic potential of CNTF and its role in advancing neuroregeneration research.
Introduction:
CNTF, a neurotrophic cytokine, is known for its pivotal role in neuronal survival and growth. The availability of Human Recombinant CNTF allows researchers to investigate its therapeutic potential and explore avenues for developing novel treatments for neurodegenerative diseases. CNTF's ability to support neuronal health and promote regeneration makes it a promising candidate for medical interventions.
Mechanisms of Action:
CNTF interacts with specific receptor complexes, activating various downstream signaling pathways, including Janus kinase (JAK) and Signal Transducer and Activator of Transcription (STAT) pathways. These pathways contribute to cell survival, differentiation, and axonal growth, forming the foundation for CNTF's neuroprotective effects.
Production Methods:
Human Recombinant CNTF is produced by introducing the CNTF gene into suitable expression systems, often employing bacterial or mammalian cells. Ensuring proper post-translational modifications is essential for maintaining the protein's biological activity and therapeutic potential.
Therapeutic Applications:
CNTF's neuroprotective and regenerative effects offer potential therapeutic applications in neurodegenerative disorders, such as amyotrophic lateral sclerosis (ALS), retinal degeneration, and Parkinson's disease. It holds promise for preserving and restoring neuronal function, thereby improving the quality of life for affected individuals.
Challenges and Future Directions:
While Human Recombinant CNTF shows great potential, challenges include precise dosing, delivery methods, and potential side effects. Further research is needed to optimize CNTF-based therapies and assess their long-term safety and efficacy in clinical settings.
Conclusion:
Human Recombinant Ciliary-Neurotrophic Factor emerges as a critical tool in advancing our understanding of neuroprotection and neuroregeneration. Its potential in treating neurodegenerative disorders highlights the ongoing quest for innovative therapeutic approaches that harness the body's inherent ability to heal and regenerate.
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 22kDa.
What is the source or expression system of CNTF Protein?
Escherichia Coli.
What is the Purity of CNTF Protein?
CNTF Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTF Protein?
The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.
What is the amino acid sequence of CNTF Protein?
CNTF Protein is composed from 199 amino acids.
What applications can CNTF Protein be used in?
CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTF Protein?
The endotoxin level is minimal, CNTF Protein was purified using conventional chromatography techniques.
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Protein content
CNTF quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.28 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 CNTF Recombinant 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 :
KLK11 Human, Sf9Description:
Kallikrein-11, 4 Human Recombinant, Sf9
Kallikrein-11 isoform 1, KLK11, PRSS20, TLSP.
Product # :
ENZ-1089Price :
Quantity :
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Shipped with Ice Packs
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Description
KLK11 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 241 amino acids (19-250a.a.) and having a molecular mass of 26.7 kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).KLK11 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
KLK11 protein solution ( 0.5mg/m ) contains 50mM Tris-HCl (pH 7.5), 0.1M NaCl, 2mM CaCl2 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins are involved in carcinogenesis. Kallikrein-11 (KLK11) which is a multifunctional protease is 1 of the 15 kallikrein subfamily members found in a cluster on chromosome 19. KLK11 cleaves synthetic peptides after arginine but not lysine residues.
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Synonyms
Kallikrein-11 isoform 1, KLK11, PRSS20, TLSP.
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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
ADLETRIIKG FECKPHSQPW QAALFEKTRL LCGATLIAPR WLLTAAHCLK PRYIVHLGQH NLQKEEGCEQ TRTATESFPH PGFNNSLPNK DHRNDIMLVK MASPVSITWA VRPLTLSSRC VTAGTSCLIS GWGSTSSPQL RLPHTLRCAN ITIIEHQKCE NAYPGNITDT MVCASVQEGG KDSCQGDSGG PLVCNQSLQG IISWGQDPCA ITRKPGVYTK VCKYVDWIQE TMKNNHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MAPT Human 383a.a.Description:
Microtubule-Associated Protein Tau 383 a.a. Human Recombinant
Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.
Product # :
PRO-012Price :
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Shipped with Ice Packs
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Description
MAPT Human Recombinant (Isoform 3) fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 403 amino acids (1-383 a.a.) and having a molecular mass of 42.1kDa (Molecular size on SDS-PAGE will appear higher). The MAPT is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAPT solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
MAPT is a neuronal microtubule associated protein localized mostly on axons.
MAPT promotes tubulin polymerisation and stabilizes microtubules, however it also serves to connect certain signalling pathways to the cytoskeleton. MAPT, in its hyperphosphorylated form, is the main part of paired helical filaments (PHF) and neurofibrillary lesions in Alzheimer''s disease (AD) brain. -
Synonyms
Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.
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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 MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKAEEAGI GDTPSLEDEA AGHVTQARMV SKSKDGTGSD DKKAKGADGK TKIATPRGAA PPGQKGQANA TRIPAKTPPA PKTPPSSGEP PKSGDRSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSS AKSRLQTAPV PMPDLKNVKS KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE VKSEKLDFKD RVQSKIGSLD NITHVPGGGN KKIETHKLTF RENAKAKTDH GAEIVYKSPV VSGDTSPRHL SNVSSTGSID MVDSPQLATL ADEVSASLAK QGL.
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 :
CXCL9 Human, HisDescription:
MIG Human Recombinant (CXCL9), His Tag
C-X-C motif chemokine 9, CMK, crg-10, Humig, MIG, SCYB9, Gamma-interferon-induced monokine, Monokine induced by interferon-gamma, HuMIG, Small-inducible cytokine B9, CXCL9.
Product # :
CHM-016Price :
Quantity :
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Shipped with Ice Packs
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Description
MIG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (23-125 a.a.) and having a molecular mass of 14kDa.MIG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIG protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 30% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
MIG (CXCL9) is a small cytokine which is part of the CXC chemokine family. MIG, which is also recognized as monokine is induced by gamma interferon. MIG is related to 2 other CXC chemokines named CXCL10 and CXCL11, whose genes are located next to the gene for CXCL9 on human chromosome 4. CXCL9, CXCL10 and CXCL11 obtain their chemotactic functions by interacting with the chemokine receptor CXCR3.
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Synonyms
C-X-C motif chemokine 9, CMK, crg-10, Humig, MIG, SCYB9, Gamma-interferon-induced monokine, Monokine induced by interferon-gamma, HuMIG, Small-inducible cytokine B9, CXCL9.
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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 MGSTPVVRKG RCSCISTNQG TIHLQSLKDL KQFAPSPSCE KIEIIATLKN GVQTCLNPDS ADVKELIKKW EKQVSQKKKQ KNGKKHQKKK VLKVRKSQRS RQKKTT.
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Background
What is the molecular weight/Mw of CXCL9 HUMAN, HIS Protein?
CXCL9 HUMAN, HIS Protein has a total Mw of 14kDa.
What is the source or expression system of CXCL9 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL9 HUMAN, HIS Protein?
CXCL9 HUMAN, HIS Protein is > 85% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL9 HUMAN, HIS Protein?
The biological functionality of CXCL9 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL9 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSTPVVRKG RCSCISTNQG TIHLQSLKDL KQFAPSPSCE KIEIIATLKN GVQTCLNPDS ADVKELIKKW EKQVSQKKKQ KNGKKHQKKK VLKVRKSQRS RQKKTT.
What applications can CXCL9 HUMAN, HIS Protein be used in?
CXCL9 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL9 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL9 HUMAN, HIS 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 :
DGCR6 HumanDescription:
DiGeorge Syndrome Critical Region Gene 6 Human Recombinant
DiGeorge syndrome critical region gene 6, Protein DGCR6, DGCR6.
Product # :
PRO-1372Price :
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Shipped with Ice Packs
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Description
DGCR6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (1-220 a.a) and having a molecular mass of 27kDa. DGCR6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
DGCR6 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
DiGeorge syndrome critical region gene 6 (DGCR6) shares homology with the Drosophila melanogaster gonadal protein, that participates in gonadal and germ cell development, and also with the gamma-1 subunit of human laminin. DGCR6 is involved in DiGeorge syndrome pathology and in schizophrenia.
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Synonyms
DiGeorge syndrome critical region gene 6, Protein DGCR6, DGCR6.
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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 MGSMERYAGA LEEVADGARQ QERHYQLLSA LQSLVKELPS SFQQRLSYTT LSDLALALLD GTVFEIVQGL LEIQHLTEKS LYNQRLRLQN EHRVLRQALR QKHQEAQQAC RPHNLPVLQA AQQRELEAVE HRIREEQRAM DQKIVLELDR KVADQQSTLE KAGVAGFYVT TNPQELMLQM NLLELIRKLQ QRGCWAGKAA LGLGGPWQLP AAQCDQKGSP VPP.
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 :
ARL14 HumanDescription:
ADP-Ribosylation Factor-Like 14 Human Recombinant
ADP-ribosylation factor-like protein 14, ADP-ribosylation factor 7, ARL14, ARF7, FLJ22595.
Product # :
PRO-936Price :
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Description
ARL14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-192 a.a.) and having a molecular mass of 23.8kDa (Molecular weight on SDS-PAGE will appear higher).ARL14 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARL14 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 40% glycerol, 200mM NaCl and 1mM EDTA.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ADP-ribosylation factor-like 14 (ARL14) is a developmentally regulated member of the ADP-ribosylation factor/ARF-like protein (ARF/ARL) family of Ras-related GTPases. ARL14 is GTPase which recruits MYO1E to MHC class II-containing vesicles via the effector protein C11orf46/ARF7EP and thus controls the movement of these vesicles along the actin cytoskeleton in dendritic cells. MHC-II transport was controlled by the GTPase ARL14/ARF7, which recruits the motor myosin 1E via an effector protein ARF7EP.
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Synonyms
ADP-ribosylation factor-like protein 14, ADP-ribosylation factor 7, ARL14, ARF7, FLJ22595.
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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 MGSLGSKNPQ TKQAQVLLLG LDSAGKSTLL YKLKLAKDIT TIPTIGFNVE MIELERNLSL TVWDVGGQEK MRTVWGCYCE NTDGLVYVVD STDKQRLEES QRQFEHILKN EHIKNVPVVL LANKQDMPGA LTAEDITRMF KVKKLCSDRN WYVQPCCALT GEGLAQGFRK LTGFVKSHMK SRGDTLAFFK QN.
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 :
SMARCA4 HumanDescription:
SMARCA4 Human Recombinant
SWI/SNF Related, Matrix Associated, Actin Dependent Regulator Of Chromatin, Subfamily A, Member 4, Mitotic Growth And Transcription Activator, ATP-Dependent Helicase SMARCA4, BRG1, Global Transcription Activator Homologous Sequence Sucrose Nonfermenting-Like 4, BRG1-Associated Factor 190A, Protein Brahma Homolog 1, BRM/SWI2-Related Gene 1, Homeotic Gene Regulator, Brahma Protein-Like 1 Nuclear Protein GRB1, Protein BRG-1, SNF2-Like 4, SNF2-Beta, BAF190A, SNF2L4, MRD16, RTPS2, SWI/SNF-Related Matrix-Associated Actin-Dependent Regulator Of Chromatin Subfamily A Member 4, Transcription Activator BRG1, EC 3.6.4.-, EC 3.6.1, BAF190, SNF2LB, HSNF2b, SNF2B, SNF2, SWI2, Transcription activator BRG1.
Product # :
PRO-2071Price :
Quantity :
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Shipped with Ice Packs
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Description
SMARCA4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (362-549aa) and having a molecular mass of 25kDa. SMARCA4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SMARCA4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
SMARCA4 belongs to the SWI/SNF family of proteins and is similar to the brahma protein of Drosophila. Proteins in this family have helicase and ATPase activities and are considered to regulate transcription ofcertain genes by altering the chromatin structure around those genes. SMARCA4 is part of the large ATP-dependent chromatin remodeling complex SNF/SWI, which is essential for transcriptional activation of genesnormally repressed by chromatin. In addition, SMARCA4 is able to bind BRCA1, as well as regulating the expression ofthe tumorigenic protein CD44. Moreover, mutations in SMARCA4 cause rhabdoid tumor predisposition syndrome type 2.
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Synonyms
SWI/SNF Related, Matrix Associated, Actin Dependent Regulator Of Chromatin, Subfamily A, Member 4, Mitotic Growth And Transcription Activator, ATP-Dependent Helicase SMARCA4, BRG1, Global Transcription Activator Homologous Sequence Sucrose Nonfermenting-Like 4, BRG1-Associated Factor 190A, Protein Brahma Homolog 1, BRM/SWI2-Related Gene 1, Homeotic Gene Regulator, Brahma Protein-Like 1 Nuclear Protein GRB1, Protein BRG-1, SNF2-Like 4, SNF2-Beta, BAF190A, SNF2L4, MRD16, RTPS2, SWI/SNF-Related Matrix-Associated Actin-Dependent Regulator Of Chromatin Subfamily A Member 4, Transcription Activator BRG1, EC 3.6.4.-, EC 3.6.1, BAF190, SNF2LB, HSNF2b, SNF2B, SNF2, SWI2, Transcription activator BRG1.
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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 MGSDPVEILQ EREYRLQARI AHRIQELENL PGSLAGDLRT KATIELKALR LLNFQRQLRQ EVVVCMRRDT ALETALNAKA YKRSKRQSLR EARITEKLEK QQKIEQERKR RQKHQEYLNS ILQHAKDFKE YHRSVTGKIQ KLTKAVATYH ANTEREQKKE NERIEKERMR RLMAEDEEGY RKLIDQKKDK R.
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 :
EMG1 HumanDescription:
EMG1 Nucleolar Protein Human Recombinant
EMG1 nucleolar protein homolog (S. cerevisiae), 18S rRNA Psi1248 methyltransferase, 18S rRNA (pseudouridine-N1-)-methyltransferase NEP1, Ribosome biogenesis protein NEP1, essential for mitotic growth 1, ribosomal RNA small subunit methyltransferase NEP1, Protein C2f, BWCNS, Grcc2f, NEP1, EC 2.1.1.-.
Product # :
PRO-1122Price :
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Description
EMG1 Human Recombinant produced in E. coli is a single polypeptide chain containing 267 amino acids (1-244) and having a molecular mass of 29.1kDa.EMG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The EMG1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
EMG1 is a 244 aa protein which has a role in ribosome biogenesis. EMG1 is a key protein in the small ribosomal subunit assembly, controls methylation during ribosome synthesis and takes part in pre-18S rRNA processing. EMG1 is localized to the nucleolus and a mutation in this gene is linked with Bowen-Conradi syndrome.
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Synonyms
EMG1 nucleolar protein homolog (S. cerevisiae), 18S rRNA Psi1248 methyltransferase, 18S rRNA (pseudouridine-N1-)-methyltransferase NEP1, Ribosome biogenesis protein NEP1, essential for mitotic growth 1, ribosomal RNA small subunit methyltransferase NEP1, Protein C2f, BWCNS, Grcc2f, NEP1, EC 2.1.1.-.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAAPSDG FKPRERSGGE QAQDWDALPP KRPRLGAGNK IGGRRLIVVL EGASLETVKV GKTYELLNCD KHKSILLKNG RDPGEARPDI THQSLLMLMD SPLNRAGLLQ VYIHTQKNVL IEVNPQTRIP RTFDRFCGLM VQLLHKLSVR AADGPQKLLK VIKNPVSDHF PVGCMKVGTS FSIPVVSDVR ELVPSSDPIV FVVGAFAHGK VSVEYTEKMV SISNYPLSAA LTCAKLTTAF EEVWGVI
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 :
TAGLN3 HumanDescription:
Transgelin-3 Human Recombinant
Transgelin 3, NP22, NP25, Neuronal protein 22, Neuronal protein NP25.
Product # :
PRO-946Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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Description
TAGLN3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (1-199) and having a molecular mass of 24.6 kDa.The TAGLN3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TAGLN3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
TAGLN3 holds a putative Actin-binding domain, two potential phosphorylation sites, two EF-hand motifs and a calponin-homology (CH) domain. TAGLN3 is homologic to transgelin and calponin, two cytoskeleton-interacting proteins. TAGLN3 is a member of the calponin family, and is co-localized with Actin and tubulin, which indicates that TAGLN3 has a part in neuronal plasticity or as a signaling protein. As a result of a wide-ranging expression pattern, TAGLN3 is able to take different roles in the developing and adult brain.
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Synonyms
Transgelin 3, NP22, NP25, Neuronal protein 22, Neuronal protein NP25.
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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 MANRGPSYGL SREVQEKIEQ KYDADLENKL VDWIILQCAE DIEHPPPGRA HFQKWLMDGT VLCKLINSLY PPGQEPIPKI SESKMAFKQM EQISQFLKAA ETYGVRTTDI FQTVDLWEGK DMAAVQRTLM ALGSVAVTKD DGCYRGEPSW FHRKAQQNRR GFSEEQLRQG QNVIGLQMGS NKGASQAGMT GYGMPRQIM
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 :
PPIF HumanDescription:
Cyclophilin-F Human Recombinant
Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.
Product # :
ENZ-385Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PPIF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 198 amino acids (30-207) and having a molecular mass of 21 kDa. The PPIF is fused to a 20 amino acid His tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PPIF solution containing 20mM Tris-HCl pH-7.5, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 250 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.More Info
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Introduction
PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.
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Synonyms
Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.
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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 CSKGSGDPSS SSSSGNPLVY LDVDANGKPL GRVVLELKAD VVPKTAENFR ALCTGEKGFG YKGSTFHRVI PSFMCQAGDF TNHNGTGGKS IYGSRFPDEN FTLKHVGPGV LSMANAGPNT NGSQFFICTI KTDWLDGKHV VFGHVKEGMD VVKKIESFGS KSGRTSKKIV ITDCGQLS.
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 :
LECT1 (214-333) HumanDescription:
Leukocyte Cell Derived Chemotaxin 1 (214-333 a.a.) Human Recombinant
BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.
Product # :
PRO-1857Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LECT1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 143 amino acids (214-333) and having a molecular mass of 16.2kDa. LECT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LECT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
Leukocyte Cell Derived Chemotaxin 1 (214-333 a.a.), also known as LECT1, is a glycosylated transmembrane protein which is cleaved to form a mature, secreted protein. The mature protein encourages chondrocyte growth and inhibits angiogenesis. The mature protein takes part in endochondral bone development by permitting cartilaginous anlagen to be vascularized and replaced by bone. LECT1 is expressed in the avascular area of prehypertrophic cartilage and its expression reduces during vascular invasion and chondrocyte hypertrophy.
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Synonyms
BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.
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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
MGSSHHHHHH SSGLVPRGSH MGSREVVRKI VPTTTKRPHS GPRSNPGAGR LNNETRPSVQ EDSQAFNPDN PYHQEGESMT FDPRLDHEGI CCIECRRSYT HCQKICEPLG GYYPWPYNYQ GCRSACRVIM PCSWWVARIL GMV.
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 :
CXCL3 Rat betaDescription:
GRO-gamma, CINC-2 beta Rat Recombinant (CXCL3)
Macrophage inflammatory protein 2-beta, MIP2-beta, CXCL3, Growth-regulated protein gamma, GRO-gamma, GRO-gamma (1-73), GRO3, GROg, MIP2B, SCYB3, MIP-2b, CINC-2b, MGSA gamma.
Product # :
CHM-273Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GRO-g Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a total molecular mass of 7.8kDa. GRO-g is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 1×PBS, pH 7.4.
Purity
Greater than 97.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human CXCR2 transfected 293 cells using a concentration range of 10-100ng/ml.More Info
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Introduction
Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.
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Synonyms
Macrophage inflammatory protein 2-beta, MIP2-beta, CXCL3, Growth-regulated protein gamma, GRO-gamma, GRO-gamma (1-73), GRO3, GROg, MIP2B, SCYB3, MIP-2b, CINC-2b, MGSA gamma.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GRO-g although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GRO-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.
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Solubility
It is recommended to reconstitute the lyophilized GRO-g in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
RELRCQCLKT LPRVDFENIQ SLTVTPPGPH CTQTEVIATL KDGQEVCLNP QAPRLQKIIQ KLLKSPSL.
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Background
What is the molecular weight/Mw of CXCL3 RAT BETA Protein?
CXCL3 RAT BETA Protein has a total Mw of 7.8kDa.
What is the source or expression system of CXCL3 RAT BETA Protein?
Escherichia Coli.
What is the Purity of CXCL3 RAT BETA Protein?
CXCL3 RAT BETA Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL3 RAT BETA Protein?
Determined by its ability to chemoattract human CXCR2 transfected 293 cells using a concentration range of 10-100ng/ml.
What is the amino acid sequence of CXCL3 RAT BETA Protein?
RELRCQCLKT LPRVDFENIQ SLTVTPPGPH CTQTEVIATL KDGQEVCLNP QAPRLQKIIQ KLLKSPSL.
What applications can CXCL3 RAT BETA Protein be used in?
CXCL3 RAT BETA Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL3 RAT BETA Protein?
The endotoxin level is minimal, CXCL3 RAT BETA 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 :
CLNS1A HumanDescription:
Chloride Channel, Nucleotide-Sensitive, 1A Human Recombinant
CLNS1A, CLCI, ICLN, CLNS1B, Methylosome subunit pICln, Chloride channel, nucleotide sensitive 1A, Chloride conductance regulatory protein ICln, Chloride ion current inducer protein, Reticulocyte pICln.
Product # :
PRO-1277Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CLNS1A Human Recombinant produced in E. coli is a single polypeptide chain containing 261 amino acids (1-237) and having a molecular mass of 28.8kDa (molecular size on SDS-PAGE will appear higher).CLNS1A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CLNS1A solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 2mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Methylosome subunit pICln (CLNS1A), is a member of the pICln (TC 1.A.47) family. CLNS1A takes part in multiple regulatory pathways. CLNS1A interaction with Sm proteins, inhibits their compilation on U RNA and interferes with snRNP biogenesis. CLNS1A inhibits the binding of survival motor neuron protein (SMN) to Sm proteins. Methylosome subunit pICln is related with the plasma membrane where it functions as a chloride present regulator.
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Synonyms
CLNS1A, CLCI, ICLN, CLNS1B, Methylosome subunit pICln, Chloride channel, nucleotide sensitive 1A, Chloride conductance regulatory protein ICln, Chloride ion current inducer protein, Reticulocyte pICln.
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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 MGSHMSFLKS FPPPGPAEGL LRQQPDTEAV LNGKGLGTGT LYIAESRLSW LDGSGLGFSL EYPTISLHAL SRDRSDCLGE HLYVMVNAKF EEESKEPVAD EEEEDSDDDV EPITEFRFVP SDKSALEAMF TAMCECQALH PDPEDEDSDD YDGEEYDVEA HEQGQGDIPT FYTYEEGLSH LTAEGQATLE RLEGMLSQSV SSQYNMAGVR TEDSIRDYED GMEVDTTPTV AGQFEDADVD H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
VTCN1 HumanDescription:
V-Set Domain Containing T Cell Activation Inhibitor 1 Human Recombinant
V-set domain-containing T-cell activation inhibitor 1, B7 homolog 4, B7-H4, B7h.5, Immune costimulatory protein B7-H4, Protein B7S1, T-cell costimulatory molecule B7x, B7H4, VTCN1, B7S1, B7X, PRO1291, RP11-229A19.4.
Product # :
PRO-1812Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
VTCN1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 258 amino acids (25-259) and having a molecular mass of 28.2 kDa.VTCN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The VTCN1 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
-
Introduction
V-Set Domain Containing T Cell Activation Inhibitor 1, also known as VCTN1, is part of the B7 costimulatory protein family. Proteins in this family are located on the surface of antigen-presenting cells and interact with ligand bound to receptors on the surface of T cells. High level of the encoded protein has been associated with tumor progression. VCTN1 also takes part in promoting epithelial cell transformation.
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Synonyms
V-set domain-containing T-cell activation inhibitor 1, B7 homolog 4, B7-H4, B7h.5, Immune costimulatory protein B7-H4, Protein B7S1, T-cell costimulatory molecule B7x, B7H4, VTCN1, B7S1, B7X, PRO1291, RP11-229A19.4.
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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 MGSLIIGFGI SGRHSITVTT VASAGNIGED GILSCTFEPD IKLSDIVIQW LKEGVLGLVH EFKEGKDELS EQDEMFRGRT AVFADQVIVG NASLRLKNVQ LTDAGTYKCY IITSKGKGNA NLEYKTGAFS MPEVNVDYNA SSETLRCEAP RWFPQPTVVW
ASQVDQGANF SEVSNTSFEL NSENVTMKVV SVLYNVTINN TYSCMIENDI AKATGDIKVT ESEIKRRSHL QLLNSKAS.
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 :
CREG1 MouseDescription:
Cellular Repressor of E1A-Stimulated Genes 1 Mouse Recombinant
Protein CREG1, Cellular repressor of E1A-stimulated genes 1, Creg1, Creg.
Product # :
PRO-2387Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- purity
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Description
CREG1 Mouse Recombinant produced in E. coli is a single polypeptide chain containing 213 amino acids (32-220) and having a molecular mass of 24kDa. CREG1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CREG1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.15M NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Cellular Repressor of E1A-Stimulated Genes 1 (CREG1) both activates and inhibits gene expression to stimulate cellular proliferation and hinder differentiation. CREG1 antagonizes transcriptional activation and cellular transformation by E1A. CREG1 shares partial sequence similarity with E1A and binds both the general transcription factor TBP and the tumor suppressor pRb in vitro. CREG1 contributes to the transcriptional control of cell growth and differentiation.
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Synonyms
Protein CREG1, Cellular repressor of E1A-stimulated genes 1, Creg1, Creg.
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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 MGSMRGGRDH GDWDVDRRLP PLPPREDGPR VARFVTHVSD WGSLATISTI KEVRGWPFAD IISISDGPPG EGTGEPYMYL SPLQQAVSDL QENPEATLTM SLAQTVYCRN HGFDPQSPLC VHIMMSGTVT KVNKTEEDYA RDSLFVRHPE MKHWPSSHNW FFAKLKISRI WVLDYFGGPK VVTPEEYFNV TLQ.
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 :
IFN tau OvineDescription:
IFN-Tau Ovine Recombinant
IFN-tau1, Trophoblast protein 1, TP-1, Trophoblastin, Antiluteolysin, Trophoblast antiluteolytic protein, IFN-tau, IFN tau-1.
Product # :
CYT-377Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
- source
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- biological activity
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Description
IFN-Tau Ovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 19914.7 Dalton.The IFN-Tau is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from (1mg/ml) solution containing PBS pH-7.4.
Purity
Greater than 95.0% as determined by both:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 10,000,000IU/mg.More Info
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Introduction
IFN-tau is also known as TP-1 (trophoblast protein-1) is a new class of type I IFN that is secreted by the trophoblast and is the signal for maternal recognition of pregnancy in sheep. IFN- tau has potent immunosuppressive and antiviral activities similar to other type I IFN but is less cytotoxic than IFN-alpha and IFN-beta. The current investigation concerns the effect of recombinant ovine IFN- tau (rOIFN- tau) on the modulation of MHC class I and II expression on cloned mouse cerebrovascular endothelial (CVE) cells.
IFN-tau induced tyrosine phosphorylation of Stat1 and upregulated the expression of MHC class I on CVE. One proposed action by which type I IFN reduces the relapse rate in MS is via interference with IFN-?-induced MHC class II expression. IFN- tau was shown to downregulate IFN-?-induced MHC class II expression on CVE and, hence, may be of potential therapeutic value in downregulating inflammation in the central nervous system (CNS). IFN- tau did not upregulate the expression of MHC class II on CVE. IFN- tau also inhibited the replication of Theiler's virus in CVE. -
Synonyms
IFN-tau1, Trophoblast protein 1, TP-1, Trophoblastin, Antiluteolysin, Trophoblast antiluteolytic protein, IFN-tau, IFN tau-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IFN-Tau although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Tau 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 IFN Tau 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
The sequence of the first five N-terminal amino acids was determined and was found to be Cys-Tyr-Leu-Ser-Arg.
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Background
What is the molecular weight/Mw of IFN TAU OVINE Protein?
IFN TAU OVINE Protein has a total Mw of 19.9kDa.
What is the source or expression system of IFN TAU OVINE Protein?
Escherichia Coli.
What is the Purity of IFN TAU OVINE Protein?
IFN TAU OVINE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFN TAU OVINE Protein?
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 10,000,000IU/mg.
What is the amino acid sequence of IFN TAU OVINE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Cys-Tyr-Leu-Ser-Arg.
What applications can IFN TAU OVINE Protein be used in?
IFN TAU OVINE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFN TAU OVINE Protein?
The endotoxin level is minimal, IFN TAU OVINE 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 :
GDF15 HumanDescription:
Growth and Differentiation Factor 15 Human Recombinant
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
Product # :
CYT-335Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GDF15 Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, Polypeptide chain containing 2x113 amino acids and having a molecular mass of 24.8 kDa. The GDF15 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDF15 is lyophilized from a sterile filtered solution containing 0.1% Trifluoroacetic Acid (TFA).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.
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Synonyms
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GDF15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF15 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 GDF15 in sterile 18M-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MARNGDHCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.
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Background
What is the molecular weight/Mw of GDF15 HUMAN Protein?
GDF15 HUMAN Protein has a total Mw of 24.8kDa.
What is the source or expression system of GDF15 HUMAN Protein?
Escherichia Coli.
What is the Purity of GDF15 HUMAN Protein?
GDF15 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF15 HUMAN Protein?
The biological functionality of GDF15 HUMAN Protein will be determined in the future.
What is the amino acid sequence of GDF15 HUMAN Protein?
MARNGDHCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.
What applications can GDF15 HUMAN Protein be used in?
GDF15 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF15 HUMAN Protein?
The endotoxin level is minimal, GDF15 HUMAN 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 :
EREG HumanDescription:
Epiregulin Human Recombinant
EREG, Epiregulin, ER.
Product # :
CYT-609Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Epiregulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 49 amino acids and having a molecular mass of 5.6 kDa. Epiregulin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Epiregulin was lyophilized from 0.5mg/ml solution ciontaing 20mM PBS buffer pH-7.4 containing 20mM sodium chloride.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.More Info
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Introduction
Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.
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Synonyms
EREG, Epiregulin, ER.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Epiregulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Epiregulin 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 Epiregulin 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
VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.
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Background
What is the molecular weight/Mw of EREG Protein?
EREG Protein has a total Mw of 5.6kDa.
What is the source or expression system of EREG Protein?
Escherichia Coli.
What is the Purity of EREG Protein?
EREG Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of EREG Protein?
The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.
What is the amino acid sequence of EREG Protein?
VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.
What applications can EREG Protein be used in?
EREG Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EREG Protein?
The endotoxin level is minimal, EREG 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 :
Bcl 2 Human (1-206 a.a.)Description:
B-Cell Leukemia/Lymphoma 2, (1-206 a.a.) Human Recombinant
Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.
Product # :
PRO-630Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
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Description
Bcl-2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 1-206. The wild type Bcl-2 is missing 12 amino acids from C-terminus. C-terminus is fused to His-Tag. C-terminus his-tag, mimics the deleted C-terminus membrane domain thus maintaining its biological activity. Bcl-2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein contains 10mM Tris-HCl pH-8, 1mM EDTA and 250mM NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
BCL2 gene encodes an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants, produced by alternate splicing, differ in their C-terminal ends.
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Synonyms
Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bcl-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bcl-2 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
Suspend Bcl-2 in 100ul of 0.5M Acetic acid, over night at 4°C. Dilute 10 fold into selected buffer system. BCL-2 has tendency to form intramolecular disulfide bond, 5mM DTT is recommended in assay buffer. When running SDS-PAGE gel, 10mM DTT is recommended.
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
Description:
B-Cell Leukemia/Lymphoma 2 Human Recombinant (–BH1)
Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.
Product # :
PRO-631Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
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Description
Bcl-2 Des BH1 domain (136-155 residues) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids 1-135 and 156-218.The Bcl-2 is expressed as His-Tag fusion protein and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein contains 10mM Tris-HCL pH-8, 1mM EDTA and 250mM NaCl.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
BCL2 gene encodes an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants, produced by alternate splicing, differ in their C-terminal ends.
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Synonyms
Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bcl-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bcl-2 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
Suspend Bcl-2 in 100?l of 0.5M Acetic acid, over night at 4°C.
Dilute 10 fold into selected buffer system.
BCL-2 has tendency to form intramolecular disulfide bond, 5mM DTT is recommended in assay buffer. When running SDS-PAGE gel, 10mM DTT is recommended. -
Applications
Input marker or positive control (Western Blotting).
Function study.
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 :
OAZ1 HumanDescription:
Ornithine Decarboxylase Antizyme 1 Human Recombinant
Ornithine decarboxylase antizyme 1, OAZ, ODC-Az, AZI, antizyme 1, MGC138338.
Product # :
PRO-1200Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
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Description
OAZ1 Human Recombinant produced in E. coli is a single polypeptide chain containing 251 amino acids (1-228) and having a molecular mass of 27.8 kDa.OAZ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The OAZ1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
OAZ1 is a member of the ODC antizyme family. OAZ1 is auto-regulated expressed by polyamine-enhanced translational frame shifting. OAZ1 negatively controls polyamine synthesis by increasing the negative feedback loop regulating ornithine decarboxylase (ODC) activity. The OAZ1 protein inhibits ornithine decarboxylase and speeds up its detraction.
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Synonyms
Ornithine decarboxylase antizyme 1, OAZ, ODC-Az, AZI, antizyme 1, MGC138338.
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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 MGSMVKSSLQ RILNSHCFAR EKEGDKPSAT IHASRTMPLL SLHSRGGSSS ESSRVSLHCC SNPGPGPRWC SDAPHPPLKI PGGRGNSQRD HNLSANLFYS DDRLNVTEEL TSNDKTRILN VQSRLTDAKR INWRTVLSGG SLYIEIPGGA LPEGSKDSFA VLLEFAEEQL RADHVFICFH KNREDRAALL RTFSFLGFEI VRPGHPLVPK RPDACFMAYT FERESSGEEE 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.
- View Data Sheet
Name :
RCN1 HumanDescription:
Reticulocalbin 1 Human Recombinant
PIG20, RCAL, RCN.
Product # :
PRO-544Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
RCN1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (30-331 a.a.) and having a molecular mass of 40.4kDa (real molecular weight on SDS-PAGE will be shift up). The RCN1 is fused to 39 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1mg/ml solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
RCN1 is a calcium-binding protein which binds calcium and controls calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment. RCN1 withholds six conserved regions with similarity to a high affinity Ca(+2)-binding motif, the EF-hand.
High conservation of amino acid residues outside of these motifs, in relation to mouse reticulocalbin, is consistent with a biochemical function further to that of calcium binding. In human endothelial and prostate cancer cell lines RCN1 protein is localized to the plasma membrane. -
Synonyms
PIG20, RCAL, RCN.
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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 KDRWGSELEK PTVRKERVVR PDSELGERPP EDNQSFQYDH EAFLGKEDSK TFDQLTPDES
KERLGKIVDR IDNDGDGFVT TEELKTWIKR VQKRYIFDNV AKVWKDYDRD KDDKISWEEY KQATYGYYLG NPAEFHDSSD HHTFKKMLPR
DERRFKAADL NGDLTATREE FTAFLHPEEF EHMKEIVVLE TLEDIDKNGD GFVDQDEYIA DMFSHEENGP EPDWVLSERE QFNEFRDLNK
DGKLDKDEIR HWILPQDYDH AQAEARHLVY ESDKNKDEKL TKEEILENWN MFVGSQATNY GEDLTKNHDE L.
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 :
KRT19 AntibodyDescription:
Cytokeratin 19, Mouse Anti Human
Keratin type I cytoskeletal 19, Cytokeratin-19, CK-19, Keratin-19, K19, KRT19, CK19, K1CS, MGC15366.
Product # :
ANT-472Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
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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Immunogen
Anti-human KRT19 mAb, clone PAT13D10A, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human KRT19 protein purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and Kappa light chain.
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Clone
PAT13D10A.
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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.
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.