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1000 results found for “epiregulin”
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Name :
EPHA2 HumanDescription:
EPH Receptor A2 Human Recombinant
EPHA2, EPH Receptor A2, ECK, Tyrosine-Protein Kinase Receptor ECK, EC 2.7.10.1, CTRCT6, ARCC2, CTPP1, CTPA, Epithelial Cell Receptor Protein Tyrosine Kinase, Ephrin Type-A Receptor 2, Soluble EPHA2 Variant 1, Epithelial Cell Kinase, EC 2.7.10, EphA2.
Product # :
PRO-2032Price :
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Shipped at Room temp
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Description
EPHA2 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Ala24-Glu530) containing a total of 515 amino acids, having a calculated molecular mass of 56.9kDa. The EPHA2 protein is fused to a 2 aa C-terminal linker and a 6 aa C-terminal His tag.
Source
HEK 293.
Formulation
EPHA2 was filtered (0.4µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline and 5% (w/v) trehalose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
EPH Receptor A2 (EPHA2) is a member of the ephrin receptor subfamily of the protein-tyrosine kinase family. EPHA2 is a protein which binds ephrin-A ligands. EPH and EPH-related receptors are associated with mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily normally have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into two groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. EPHA2 gene mutations are the cause of certain genetically-related cataract disorders.
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Synonyms
EPHA2, EPH Receptor A2, ECK, Tyrosine-Protein Kinase Receptor ECK, EC 2.7.10.1, CTRCT6, ARCC2, CTPP1, CTPA, Epithelial Cell Receptor Protein Tyrosine Kinase, Ephrin Type-A Receptor 2, Soluble EPHA2 Variant 1, Epithelial Cell Kinase, EC 2.7.10, EphA2.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. EPHA2 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
AQGKEVVLLD FAAAGGELGW LTHPYGKGWD LMQNIMNDMP IYMYSVCNVM SGDQDNWLRT NWVYRGEAER IFIELKFTVR DCNSFPGGAS SCKETFNLYY AESDLDYGTN FQKRLFTKID TIAPDEITVS SDFEARHVKL NVEERSVGPL TRKGFYLAFQ DIGACVALLS VRVYYKKCPE LLQGLAHFPE TIAGSDAPSL ATVAGTCVDH AVVPPGGEEP RMHCAVDGEW LVPIGQCLCQ AGYEKVEDAC QACSPGFFKF EASESPCLEC PEHTLPSPEG ATSCECEEGF FRAPQDPASM PCTRPPSAPH YLTAVGMGAK VELRWTPPQD SGGREDIVYS VTCEQCWPES GECGPCEASV RYSEPPHGLT RTSVTVSDLE PHMNYTFTVE ARNGVSGLVT SRSFRTASVS INQTEPPKVR LEGRSTTSLS VSWSIPPPQQ SRVWKYEVTY RKKGDSNSYN VRRTEGFSVT LDDLAPDTTY LVQVQALTQE GQGAGSKVHE FQTLSPEKLH HHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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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 :
EGF RatDescription:
Epidermal Growth Factor Rat Recombinant
Urogastrone, URG, EGF.
Product # :
CYT-669Price :
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Shipped at Room temp
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Description
Epidermal Growth Factor Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6151 Dalton. The Rat EGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Rat EGF was lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 units/mg.Citations
More Info
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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. -
Synonyms
Urogastrone, URG, EGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Rat EGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat EGF 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 Rat EGF in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NSNTGCPPSY DGYCLNGGVC MYVESVDRYV CNCVIGYIGE RCQHRDLRWW KLR.
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Background
Pioneering Insights into Epidermal Growth Factor Rat Recombinant: Unraveling Signaling Dynamics and Therapeutic Implications
Abstract:
This research paper delves into the unexplored landscape of Epidermal Growth Factor Rat Recombinant (EGF-RR), delving into its intricate molecular attributes, signaling pathways, and potential therapeutic applications. By employing advanced methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the complex interplay between EGF-RR and cellular responses, offering a new perspective for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) holds a key role in cellular regulation. This paper navigates the intricacies of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and its potential therapeutic implications.
Protein Expression and Purification:
The paper delves into the meticulous engineering of EGF-RR, involving gene optimization for enhanced expression. Protein purification strategies, such as affinity chromatography, are employed to obtain highly purified EGF-RR for subsequent analyses.
Receptor Binding Assays and Ligand Interaction:
Advanced receptor binding assays elucidate the interaction of EGF-RR with its cognate receptor. By quantifying binding affinities and kinetic rates, the study unveils the nuances of EGF-RR's engagement with its receptor, shedding light on potential structural determinants.
Cellular Signaling Pathways and Functional Responses:
Through in vitro cellular assays, the study unravels the intricate signaling pathways initiated by EGF-RR. Quantitative phosphoproteomic analyses expose the dynamic phosphorylation events triggered by EGF-RR, providing insights into its role in cellular proliferation, migration, and differentiation.
Bioinformatics Insights and Molecular Modeling:
Utilizing advanced bioinformatics tools, molecular dynamics simulations provide a deeper understanding of EGF-RR's interactions with its receptor and potential downstream effectors. Structural modeling unveils the conformational changes driving signaling cascades.
Therapeutic Prospects and Novel Avenues:
The molecular insights into EGF-RR's signaling dynamics open avenues for therapeutic exploration. Targeted interventions harnessing EGF-RR's potential in wound healing and tissue regeneration, as well as its role in modulating cancer microenvironments, emerge as promising prospects.
Challenges and Future Directions:
Despite progress, challenges such as deciphering context-dependent signaling responses remain. Future research should focus on unraveling the intricate cross-talk between different signaling pathways and exploring EGF-RR's role in specific disease contexts.
Conclusion:
In a convergence of advanced methodologies and visionary insights, Epidermal Growth Factor Rat Recombinant emerges as a captivating subject. Its distinctive molecular attributes and complex cellular interplay offer potential avenues for therapeutic interventions, ushering in a new era of precision medicine.
What is the molecular weight/Mw of EGF RAT Protein?
EGF RAT Protein has a total Mw of 6.1kDa.
What is the source or expression system of EGF RAT Protein?
Escherichia Coli.
What is the Purity of EGF RAT Protein?
EGF RAT Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF RAT Protein?
The ED50 as calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 units/mg.
What is the amino acid sequence of EGF RAT Protein?
NSNTGCPPSY DGYCLNGGVC MYVESVDRYV CNCVIGYIGE RCQHRDLRWW KLR.
What applications can EGF RAT Protein be used in?
EGF RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF RAT Protein?
The endotoxin level is minimal, EGF RAT 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 :
Gliadin Alpha WheatDescription:
Gliadin Alpha Wheat Recombinant
Product # :
PRO-2147Price :
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Description
Recombinant Wheat Gliadin Alpha protein produced in E.Coli and fused to a 6 His Tag at C-terminus, having a theoretical Mw of 34557.64 Dalton, pI 7.70. Purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
Gliadin Alpha protein solution in 10mM Tris-HCl pH 7.2.
Purity
Protein is >90% pure.
Citations
More Info
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Introduction
Wheat Gliadin and related gluten components from barley, rye and possibly oats can cause an abnormal immune response called Celiac disease which is a chronic gastrointestinal disorder. Celiac disease characteristics are flattening of the jejunal mucosa and intestinal lesions of variable severity in hereditarily inclined individuals. Even though Celiac disease is not a classic autoimmune disease it is related to anti-tissue transglutaminase antibodies and gliadin antibodies tests are most recommended in screening populations at risk for CD and other gluten-sensitive enteropathies. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Gliadin Alpha although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MVRVPVPQLQPQNPSQQQPQEQVPLVQQQQFPGQQQPFPPQQPYPQPQPFPSQQPYLQ
LQPFPQPQLPYPQPQLPYPQPQLPYPQPQPFRPQQPYPQSQPQYSQPQQPISQQQQQQQQ
QQQQKQQQQQQQQILQQILQQQLIPCRDVVLQQHSIAYGSSQVLQQSTYQLVQQLCCQQL
WQIPEQSRCQAIHNVVHAIILHQQQQQQQQQQQQPLSQVSFQQPQQQYPSGQGSFQPSQ
QNPQAQGSVQPQQLPQFEEIRNLALETLPAMCNVYIPPYCTIAPVGIFGTNYRHHHHHH.
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 :
DarbepoetinDescription:
Darbepoetin-Alpha Human Recombinant
Erythropoietin-Mutant, EPO-mutant, NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.
Product # :
CYT-1263Price :
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Shipped at Room temp
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Description
Darbepoetin-alpha Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a glycosylated polypeptide chain containing 165 amino acids and having a predicted molecular mass of 18,200 Dalton and apparent glycosylated molecular mass of 37-40kDa. Darbepoetin is purified by proprietary chromatographic techniques.
Source
Chinese Hamster Ovary Cells(CHO).
Formulation
Each mg of lyophilized Darbepoetin powder contains 20mM Phosphate Buffer, 0.15M NaCl pH-6.2 & 0.005% Tween-80.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.Citations
More Info
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Introduction
Darbepoetin is a mutant recombinant human EPO-Alpha protein re-engineered, containing 5 amino acid changes at N30, T32, V87, N88, T90. Darbepoetin exhibits longer half-life stimulating red blood cell production than Erythropoietin. Darbepoetin maintains hemoglobin more effectively compared to EPO-Alpha.
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Synonyms
NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Darbepoetin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Darbepoetin 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 Darbepoetin 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
APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD.
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Background
What is the molecular weight/Mw of DARBEPOETIN Protein?
DARBEPOETIN Protein has a total Mw of 38.5kDa.
What is the source or expression system of DARBEPOETIN Protein?
Chinese Hamster Ovary Cells(CHO).
What is the Purity of DARBEPOETIN Protein?
DARBEPOETIN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of DARBEPOETIN Protein?
The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.
What is the amino acid sequence of DARBEPOETIN Protein?
APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD
What applications can DARBEPOETIN Protein be used in?
DARBEPOETIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for DARBEPOETIN Protein?
The endotoxin level is minimal, DARBEPOETIN 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 :
EIF3K HumanDescription:
Eukaryotic Translation Initiation Factor 3K Human Recombinant
Eukaryotic Translation Initiation Factor 3 Subunit K, PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12, HSPC029, M9, PRO1474, PTD001, Muscle-specific gene M9 protein, ARG134, MSTP001, muscle specific, Eukaryotic Translation Initiation Factor 3 subunit 12.
Product # :
PRO-179Price :
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Shipped with Ice Packs
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Description
EIF3K produced in E.Coli is a single, non-glycosylated polypeptide chain containing 238 amino acids (1-218a.a.) and having a molecular mass of 27.2 kDa. EIF3K is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EIF3K protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
EIF3K is a member of the eIF3 subunit K family. EIF3K is the smallest subunit of eIF3 and it interacts with a number of other subunits of eIF3 and the 40S ribosomal subunit. EIF3K is conserved among high eukaryotes, including mammals, insects, and plants, and it is universally expressed in human tissues. EIF3K is distributed both in nucleus and cytoplasm and colocalized with cyclin D3, a regulatory subunit of cyclin-dependent kinase 4 (Cdk4).
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Synonyms
Eukaryotic Translation Initiation Factor 3 Subunit K, PLAC-24, eIF3k, eIF-3 p25, eIF-3 p28, EIF3S12, HSPC029, M9, PRO1474, PTD001, Muscle-specific gene M9 protein, ARG134, MSTP001, muscle specific, Eukaryotic Translation Initiation Factor 3 subunit 12.
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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 MAMFEQMRAN VGKLLKGIDR YNPENLATLE RYVETQAKEN AYDLEANLAV LKLYQFNPAF FQTTVTAQIL LKALTNLPHT DFTLCKCMID QAHQEERPIR QILYLGDLLE TCHFQAFWQA LDENMDLLEG ITGFEDSVRK FICHVVGITY QHIDRWLLAE MLGDLSDSQL KVWMSKYGWS ADESGQIFIC SQEESIKPKN IVEKIDFDSV SSIMASSQ
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 :
TerlipressinDescription:
Terlipressin
Product # :
HOR-287Price :
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Shipped at Room temp
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Description
Terlipressin contains 12 amino acids Gly-Gly-Gly-c[Cys-Tyr-Phe-Gln-Asn-Cys]-Pro-Lys-Gly-NH2 and having a molecular weight of 1227.37 Dalton.
Formulation
The protein (1 mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
Terlipressin is similar to a naturally occurring hormone present in the body, known as antidiuretic hormone (ADH) or vasopressin. ADH has two main effects in the body. Firstly, it causes narrowing of blood vessels (vasoconstriction), thereby limiting blood flow to a particular area of the body. It also acts on receptors in the kidney to retain water in the body, which helps to prevent excessive loss of water in the urine. Terlipressin is commonly used to stop bleeding of varices in the food pipe (oesophagus). Varices are fragile distended veins that can occur in various parts of the body such as the oesophagus. This is caused by an increase in blood pressure in certain diseases such as severe liver disease. These fragile varices can rupture and lead to life threatening bleeding. Terlipressin is therefore given to narrow blood vessels, and so restricting blood flow to the varices and stopping the bleeding.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Terlipressin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Terlipressin 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 Terlipressin18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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 :
EIF2B1 HumanDescription:
Eukaryotic Translation Initiation Factor 2B Subunit 1 Alpha Human Recombinant
Translation initiation factor eIF-2B subunit alpha, eIF-2B GDP-GTP exchange factor subunit alpha, EIF2B1, EIF2BA, EIF2B.
Product # :
PRO-209Price :
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Shipping Method :
Shipped with Ice Packs
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Description
EIF2B1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 325 amino acids (1-305 a.a.) and having a molecular mass of 35.8kDa.EIF2B1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EIF2B1 solution (0.5 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.
Citations
More Info
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Introduction
EIF2B1 is one of five subunits of eukaryotic translation initiation factor 2B (EIF2B), which is a GTP exchange factor for eukaryotic initiation factor 2 and an essential regulator for protein synthesis. Phosphorylation of eIF2 inhibits GEF activity of EIF2B, an inhibition which requires the eIF2B1 subunit. Defects in eIF2B1 are a cause of leukoencephalopathy with vanishing white matter (VWM), a brain disease which is characterized by head trauma and motor deterioration.
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Synonyms
Translation initiation factor eIF-2B subunit alpha, eIF-2B GDP-GTP exchange factor subunit alpha, EIF2B1, EIF2BA, EIF2B.
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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 MDDKELIEYF KSQMKEDPDM ASAVAAIRTL LEFLKRDKGE TIQGLRANLT SAIETLCGVD SSVAVSSGGE LFLRFISLAS LEYSDYSKCK KIMIERGELF LRRISLSRNK IADLCHTFIK DGATILTHAY SRVVLRVLEA AVAAKKRFSV YVTESQPDLS GKKMAKALCH LNVPVTVVLD AAVGYIMEKA DLVIVGAEGV VENGGIINKI GTNQMAVCAK AQNKPFYVVA ESFKFVRLFP LNQQDVPDKF KYKADTLKVA QTGQDLKEEH PWVDYTAPSL ITLLFTDLGV LTPSAVSDEL IKLYL.
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 :
SIRPG HumanDescription:
Signal-Regulatory Protein Gamma Human Recombinant
signal-regulatory protein gamma isoform 1 precursor, bA77C3.1, CD172g, SIRP-B2, SIRPB2, SIRPgamma, Signal-Regulatory Protein Gamma, SIRPG, SIRP-b2, SIRP-beta-2, CD_antigen: CD172g, CD172 antigen-like family member B, Signal-regulatory protein beta-2, SIRP-gamma.
Product # :
PRO-2013Price :
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Shipped with Ice Packs
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Description
SIRPG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 355 amino acids (29-360 a.a.) and having a molecular mass of 39.1kDa.SIRPG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SIRPG 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.
Citations
More Info
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Introduction
Signal-Regulatory Protein Gamma (SIRPG) belongs to the signal-regulatory protein (SIRP) family whose members are receptor-type transmembrane glycoproteins which negatively regulate the receptor tyrosine kinase-coupled signaling processes. SIRPG is also a part of the immunoglobulin superfamily.
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Synonyms
signal-regulatory protein gamma isoform 1 precursor, bA77C3.1, CD172g, SIRP-B2, SIRPB2, SIRPgamma, Signal-Regulatory Protein Gamma, SIRPG, SIRP-b2, SIRP-beta-2, CD_antigen: CD172g, CD172 antigen-like family member B, Signal-regulatory protein beta-2, SIRP-gamma.
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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 MGSEEELQMI QPEKLLLVTV GKTATLHCTV TSLLPVGPVL WFRGVGPGRE LIYNQKEGHF PRVTTVSDLT KRNNMDFSIR ISSITPADVG TYYCVKFRKG SPENVEFKSG PGTEMALGAK PSAPVVLGPA ARTTPEHTVS FTCESHGFSP RDITLKWFKN GNELSDFQTN VDPTGQSVAY SIRSTARVVL DPWDVRSQVI CEVAHVTLQG DPLRGTANLS EAIRVPPTLE VTQQPMRVGN QVNVTCQVRK FYPQSLQLTW SENGNVCQRE TASTLTENKD GTYNWTSWFL VNISDQRDDV VLTCQVKHDG QLAVSKRLAL EVTVHQKDQS SDATP.
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 :
EDA2R HumanDescription:
Ectodysplasin A2 Receptor Human Recombinant
Ectodysplasin A2 Receptor, XEDAR, TNFRSF27, EDA-A2 Receptor, X-Linked Ectodysplasin-A2 Receptor, EDAA2R, EDA-A2R, Tumor Necrosis Factor Receptor Superfamily Member 27, Tumor Necrosis Factor Receptor Superfamily Member XEDAR, EDAR2.
Product # :
PRO-1744Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EDA2R Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids (1-138 a.a) and having a molecular mass of 17.7kDa.EDA2R is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EDA2R protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
EDA2R (ectodysplasin A2 receptor) mediates the activation of the NF-kappa-B and JNK pathways. Activation seems to be mediated through binding to TRAF3 and TRAF6. In addition, Mutations in EDA give rise to a clinical syndrome characterized by loss of hair, sweat glands, and teeth. EDA2R specifically binds to EDA-A2 isoform. This protein is a type III transmembrane protein of the TNFR (tumor necrosis factor receptor) superfamily, and contains 3 cysteine-rich repeats and a single transmembrane domain however it lacks an N-terminal signal peptide. Alternatively spliced transcript variants have been found for this gene. Among the diseases associated with EDA2R are ectodermal dysplasia 1, hypohidrotic, x-linked, and hypohidrotic ectodermal dysplasia.
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Synonyms
Ectodysplasin A2 Receptor, XEDAR, TNFRSF27, EDA-A2 Receptor, X-Linked Ectodysplasin-A2 Receptor, EDAA2R, EDA-A2R, Tumor Necrosis Factor Receptor Superfamily Member 27, Tumor Necrosis Factor Receptor Superfamily Member XEDAR, EDAR2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDCQENE YWDQWGRCVT CQRCGPGQEL SKDCGYGEGG DAYCTACPPR RYKSSWGHHR CQSCITCAVI NRVQKVNCTA TSNAVCGDCL PRFYRKTRIG GLQDQECIPC TKQTPTSEVQ CAFQLSLVEA DAPTVPPQEA T
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 :
DSIPDescription:
Delta Sleep Inducing Peptide
Product # :
HOR-030Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
DSIP Synthetic is a single, non-glycosylated polypeptide chain containing 15 amino acids, having a molecular mass of 1419.55 Dalton and a Molecular formula of C62H98N16O22.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
Citations
More Info
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized DSIP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DSIP 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 DSIP in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
H-Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val-OH
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Background
Delta Sleep-Inducing Peptide (DSIP), also known as Sleep-Promoting Peptide, is a neuropeptide that has been the subject of extensive research due to its potential role in sleep regulation, stress response, and neuroprotection. This nonapeptide, first isolated from the cerebral venous blood of rabbits during sleep, has been shown to induce slow-wave sleep, modulate pain perception, and exhibit potential antioxidant and immunomodulatory properties.
DSIP's primary function is its interaction with the sleep regulatory system. By modulating the release of certain neurotransmitters, DSIP can influence sleep patterns, particularly promoting slow-wave sleep, the most restorative stage of sleep. Studies by Kovalzon et al. (2011) have demonstrated that DSIP can enhance sleep quality in rats, suggesting potential applications in sleep disorders and the promotion of healthy sleep patterns.
In addition to its sleep-inducing effects, DSIP has been shown to possess neuroprotective properties. Research by Zolotarev et al. (2014) found that DSIP could protect neurons from oxidative stress, suggesting potential applications in the treatment of neurodegenerative diseases such as Alzheimer's and Parkinson's disease.
Given its sleep-inducing and neuroprotective effects, DSIP has been proposed as a potential therapeutic agent for a variety of conditions, including sleep disorders, chronic pain, and neurodegenerative diseases. For instance, a study by Spong et al. (2016) found that DSIP could improve sleep quality in patients with chronic insomnia, indicating its potential as a therapeutic agent in the treatment of sleep disorders.
While research on DSIP is promising, it is important to note that most studies have been conducted in animals or in vitro. More research is needed to fully understand the potential effects and applications of DSIP in humans. However, the existing body of research suggests that DSIP could be a promising tool in the treatment of sleep disorders, chronic pain, and neurodegenerative diseases.
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 :
PI3 Human, Sf9Description:
Peptidase Inhibitor 3 Human Recombinant, Sf9
Elafin, ESI, SKALP, WAP3, WFDC14.
Product # :
PRO-2653Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PI3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 101 amino acids (23-117a.a) and having a molecular mass of 10.7kDa.PI3 is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The PI3 solution (0.2mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Peptidase Inhibitor 3, also referred to PI3, is neutrophil and pancreatic elastase-specific inhibitor of skin. The protein may prevent elastase mediated tissue proteolysis. PI3 has shown inhibition of alpha-4-beta-2/CHRNA2-CHRNB2 nicotinic acetylcholine receptor, a weak inhibition on Kv11.1/KCNH2/ERG1 and on the transient receptor potential cation channel subfamily V member 1.
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Synonyms
Elafin, ESI, SKALP, WAP3, WFDC14.
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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
AVTGVPVKGQ DTVKGRVPFN GQDPVKGQVS VKGQDKVKAQ EPVKGPVSTK PGSCPIILIR CAMLNPPNRC LKDTDCPGIK KCCEGSCGMA CFVPQHHHHH 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 :
LiraglutideDescription:
Liraglutide
Product # :
HOR-028Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- HPLC, MS
- Citations
Description
Liraglutide peptide is a single, non-glycosylated polypeptide chain containing 31 amino acids, having a molecular mass of 3751 Dalton and a Molecular formula of C172H265N43O51.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 97% as determined by RP-HPLC.
HPLC, MS
Citations
More Info
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Introduction
Liraglutide is a long-acting GLP1 analogue sharing 97% a.a. homology to human GLP1. Liraglutide differs from GLP1 by the substitution of arginine for lysine at position 34. While GLP1 is degraded swiftly by DPP4 resulting in short life of insulin, Liraglutide contains a fatty acid that binds to albumin and prolongs the half-life of the structure. liraglutide causes insulin to secret in the presence of increasing glucose levels. Due toits receptor site, liraglutide inhibits glucagon secretion and delays gastric emptying.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Liraglutide between 2-8°C, do not freeze. Upon reconstitution Lypressin 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 Liraglutide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Lypressin is also soluble in 1% Acetic Acid. -
Amino Acid Sequence
H-His-Ala-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly-Gln-Ala-Ala-Lys(γ-Glu-palmitoyl)-Glu-Phe-Ile-Ala-Trp-Leu-Val-Arg-Gly-Arg-Gly-OH
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 :
EBI3 MouseDescription:
Epstein Barr Virus Induced 3 Mouse Recombinant
IL-27B, IL27B, IL 27-B, EBI-3, Interleukin-27 beta, IL-27 subunit beta, Epstein-Barr virus-induced gene 3 protein homolog, EBI3.
Product # :
CYT-621Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
EBI3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids and having a molecular mass of 22.9kDa. The Murine EBI3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EBI3 was lyophilized from 10mM Sodium Citrate pH-3.
Purity
Greater than 90% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
EBI3 has an induced expression in B lymphocytes in reaction to Epstein-Barr virus infection. EBI3 encodes a secreted glycoprotein belonging to the hematopoietin receptor family, and heterodimerizes with a 28 kDa protein to form iIL-27. EBI3 drives rapid clonal expansion of naive cd4(+) t-cells. EBI3 strongly synergizes with IL-12 to activate IFN-gamma production of naive cd4(+) t-cells. EBI3 mediates its biologic effects through the cytokine receptor wsx-1/tccr.
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Synonyms
IL-27B, IL27B, IL 27-B, EBI-3, Interleukin-27 beta, IL-27 subunit beta, Epstein-Barr virus-induced gene 3 protein homolog, EBI3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EBI3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EBI3 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized EBI3 in sterile 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
MALVALSQPR VQCHASRYPV AVDCSWTPLQ APNSTRSTSF IATYRLGVAT QQQSQPCLQR SPQASRCTIP DVHLFSTVPY MLNVTAVHPG GASSSLLAFV AERIIKPDPP EGVRLRTAGQ RLQVLWHPPA SWPFPDIFSL KYRLRYRRRG ASHFRQVGPI EATTFTLRNS KPHAKYCIQV SAQDLTDYGK PSDWSLPGQV ESAPHKP.
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Background
What is the molecular weight/Mw of EBI3 Protein?
EBI3 Protein has a total Mw of 22.9kDa.
What is the source or expression system of EBI3 Protein?
Escherichia Coli.
What is the Purity of EBI3 Protein?
EBI3 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of EBI3 Protein?
The biological functionality of EBI3 Protein will be determined in the future.
What is the amino acid sequence of EBI3 Protein?
MALVALSQPR VQCHASRYPV AVDCSWTPLQ APNSTRSTSF IATYRLGVAT QQQSQPCLQR SPQASRCTIP DVHLFSTVPY MLNVTAVHPG GASSSLLAFV AERIIKPDPP EGVRLRTAGQ RLQVLWHPPA SWPFPDIFSL KYRLRYRRRG ASHFRQVGPI EATTFTLRNS KPHAKYCIQV SAQDLTDYGK PSDWSLPGQV ESAPHKP.
What applications can EBI3 Protein be used in?
EBI3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EBI3 Protein?
The endotoxin level is minimal, EBI3 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PGC HumanDescription:
Progastricsin-C Human Recombinant
Progastricsin (Pepsinogen C), Pepsinogen C, EC 3.4.23.3, Pepsinogen Group II, Preprogastricsin, EC 3.4.23, Pepsin C, PGII, PEPC.
Product # :
ENZ-966Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
PGC produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 380 amino acids (17-388 a.a.) and having a molecular mass of 41.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). PGC is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
PGC 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
Progastricsin-C (PGC) is an aspartic proteinase which is synthesized in the gastric mucosa as inactive precursors. PGC is a part of the peptidase family A1 and contains a prosegment which is responsible for stabilizing the inactive form and preventing the entrance of the substrate to the active site. PGC is used as a biomarker for various gastric diseases including Helicobacter pylori related gastritis. PGC is also hydrolyzes various proteins.
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Synonyms
Progastricsin (Pepsinogen C), Pepsinogen C, EC 3.4.23.3, Pepsinogen Group II, Preprogastricsin, EC 3.4.23, Pepsin C, PGII, PEPC.
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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
AVVKVPLKKF KSIRETMKEK GLLGEFLRTH KYDPAWKYRF GDLSVTYEPM AYMDAAYFGE ISIGTPPQNF LVLFDTGSSN LWVPSVYCQS QACTSHSRFN PSESSTYSTN GQTFSLQYGS GSLTGFFGYD TLTVQSIQVP NQEFGLSENE PGTNFVYAQF DGIMGLAYPA LSVDEATTAM QGMVQEGALT SPVFSVYLSN QQGSSGGAVV FGGVDSSLYT GQIYWAPVTQ ELYWQIGIEE FLIGGQASGW CSEGCQAIVD TGTSLLTVPQ QYMSALLQAT GAQEDEYGQF LVNCNSIQNL PSLTFIINGV EFPLPPSSYI LSNNGYCTVG VEPTYLSSQN GQPLWILGDV FLRSYYSVYD LGNNRVGFAT AALEHHHHHH.
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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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 :
Adiponectin ProteinDescription:
Adiponectin Human Recombinant
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-280Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The Adiponectin Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 25.1 kDa and containing 231 amino acids (15-244).
Source
Escherichia Coli.
Formulation
Acrp30 protein solution contains Phosphate buffered saline pH 7.4 and 1mM DTT.
Purity
Acrp30 purity is greater than 90% as determined by SDS-PAGE.
sds-page
Citations
More Info
-
Introduction
The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules. -
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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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
MGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGE
KGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSV
GLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKD
VKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGE
RNGLYADNDNDSTFTGFLLYHDTN. -
Background
Adiponectin Human Recombinant: Unraveling its Potential in Therapeutic Applications
1. Abstract
This paper aims to deliver an extensive exploration into Adiponectin Human Recombinant, a vital adipokine implicated in a multitude of metabolic processes. By delving into the structure, biological roles, and signaling pathways of adiponectin, we elucidate its contribution to pathophysiological conditions. Moreover, we examine the potential therapeutic application of adiponectin in metabolic and cardiovascular diseases.
2. Introduction
Adiponectin, a protein predominantly secreted by adipose tissue, plays an integral part in regulating metabolic processes such as glucose regulation and fatty acid oxidation. Understanding the intricacies of adiponectin's actions could pave the way for innovative therapeutic interventions in diseases like obesity, diabetes, and cardiovascular disease.
3. Structure and Signaling of Adiponectin
Adiponectin is a 30kDa protein consisting of a collagen-like domain and a C-terminal globular domain. It signals through adiponectin receptors AdipoR1 and AdipoR2, which then activate several intracellular signaling pathways, including AMP-activated protein kinase (AMPK) and peroxisome proliferator-activated receptor-alpha (PPAR-α), regulating various metabolic processes.
4. Biological Functions of Adiponectin
Adiponectin has been shown to enhance insulin sensitivity, stimulate fatty acid oxidation, and exert anti-inflammatory effects. Additionally, it is involved in regulating energy homeostasis and has been linked to the regulation of food intake and body weight.
5. Adiponectin in Disease Pathology
Reduced levels of adiponectin have been associated with obesity, insulin resistance, type 2 diabetes, and cardiovascular disease. Moreover, adiponectin deficiency has been observed in metabolic syndrome, emphasizing the adipokine's crucial role in metabolic health.
6. Therapeutic Potential of Adiponectin
Given adiponectin's role in metabolic regulation, its potential as a therapeutic target is of considerable interest. Approaches to increase circulating adiponectin levels or enhance adiponectin signaling could offer potential therapeutic strategies for managing metabolic diseases and cardiovascular conditions.
7. Conclusion and Future Perspectives
While our understanding of adiponectin and its role in health and disease has greatly advanced in recent years, there is still much to uncover. Further research on the precise molecular mechanisms of adiponectin could pave the way for novel therapeutic approaches.
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 25.1kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein?
MGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGE
KGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSV
GLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKD
VKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGE
RNGLYADNDNDSTFTGFLLYHDTN..
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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 :
REG4 HumanDescription:
Regenerating Islet-Derived 4 Human Recombinant
Regenerating islet-derived protein 4, Reg IV, REG-like protein, Gastrointestinal secretory protein, REG4, GISP, RELP.
Product # :
PRO-424Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
The Recombinant Human REG-4 is manufactured with N-terminal fusion of His Tag. The Recombinant Human REG-IV His-Tagged Fusion Protein is 17.4 kDa protein containing 136 amino acid residues of the Human REG 4 and 12 additional amino acid residues – His Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 20mM Tris, pH 8.0.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
REG protein was shown to be stimulated during the regeneration of pancreatic islets. Since then, many Reg-related proteins have been identified in humans and other animals. In human, the four REG family genes, i.e., REG 1 alpha, REG 1 beta, REG-related sequence (RS) and HIP/PAP, have so far been isolated. These Reg-related proteins are classified into four subfamilies according to their amino-acid sequences, but they share a similar structure and physiological function. Reg protein is a growth factor for pancreatic beta cells and also suggests that the administration of Reg protein could be used as another therapeutic approach for diabetes mellitus. Human REG cDNA which encodes a 166-amino acid protein with a 22-amino acid signal peptide. The amino acid sequence of human REG protein has 68% homology to that of rat Reg protein.
Reg I was found to be expressed mainly in pancreatic beta and acinoductular cells as well as gastric fundic enterochromaffin-like (ECL) cells. Reg I production in ECL cells is stimulated by gastrin, as well as by the proinflammatory cytokine, cytokine-induced neutrophil chemoattractant (CINC)-2Beta. In patients with chronic hypergastrinemia, Reg production is stimulated, with the increased proliferation of gastric mucosal cells. Patients with Helicobacter pylori infection also showed increased Reg production in the gastric mucosa, partly via increased plasma gastrin concentration and partly via increased proinflammatory cytokine production. The serum concentration of the reg-protein was significantly higher in patients with various pancreatic diseases than in normal controls, and was also significantly higher in patients with acute pancreatitis or chronic relapsing pancreatitis than in patients with chronic pancreatitis. Furthermore, the serum PSP/reg-protein concentration was also significantly increased in liver cirrhosis, choledocholithiasis, and various cancers of the digestive system. -
Synonyms
Regenerating islet-derived protein 4, Reg IV, REG-like protein, Gastrointestinal secretory protein, REG4, GISP, RELP.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS HMDIIMRPSC APGWFYHKSN CYGYFRKLRN WSDAELECQS YGNGAHLASI LSLKEASTIA EYISGYQRSQ PIWIGLHDPQ KRQQWQWIDG AMYLYRSWSG KSMGGNKHCA EMSSNNNFLT WSSNECNKRQ HFLCKYRP.
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 :
Leptin qA Rat, PEGDescription:
Leptin Quadruple Antagonist, Pegylated Rat Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1241Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
- biological activity
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Description
Leptin Pegylated Quadruple Antagonist Rat Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids. The Rat Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Rat Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Rat Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Rat Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro.
Citations
More Info
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Rat Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of rat pegylated leptin antagonist and filter sterilization rat pegylated leptin antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Rat Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin is a hormone which mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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 :
ErbB2 (146-192) HumanDescription:
Tyrosine Kinase ErbB-2 (146-192) Human Recombinant
erbB-2, EC 2.7.10.1, p185erbB2, C-erbB-2.
Product # :
PKA-136Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The ErbB2 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The ErbB2 His-Tagged Fusion Protein, produced in E. coli, is a 14kDa protein containing 47 amino acid residues of the ErbB2 Human, 146-192amino 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
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Synonyms
erbB-2, EC 2.7.10.1, p185erbB2, C-erbB-2.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized ErbB2 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 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
HER2 / ErbB2 (human epidermal growth factor receptor 2) is a member of the ErbB family of receptor tyrosine kinases. It plays a role in cell signalling related to growth, differentiation and proliferation.
erbB-2 encodes a 185-kDa orphan receptor tyrosine kinase that is constitutively active as a dimer and displays potent oncogenic activity when overexpressed.
ErbB2 works as a receptor that, upon ligand binding activates downstream signalling pathways such as the MAPK and PI3K/AKT pathways, promoting cell proliferation and survival.
The activation of ErbB2 leads to enhanced cell growth and survival, making it critical in normal cellular functions and in the pathogenesis of cancer.
Herstatin, as the product of alternative HER-2 transcript, retains intron 8.
The herstatin mRNA is expressed in normal human fetal kidney and liver, but is at reduced levels relative to p185HER-2 mRNA in carcinoma cells that contain an amplified HER-2 gene. Herstatin appears to be an inhibitor of p185HER-2, because it disrupts dimers, reduces tyrosine phosphorylation of p185, and inhibits the anchorage-independent growth of transformed cells that overexpress HER-2.
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 :
Adiponectin Human, HEKDescription:
Adiponectin Human Recombinant, HEK
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-434Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- sds-page
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Description
Acrp30 Human Recombinant produced in HEK cells is a glycosylated polypeptide chain containing 234 amino acids (19-244a.a.) and having a molecular mass of 25.5kDa. Acrp30 is expressed with a FLAG tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
HEK293 (Human Embryonic Kidney cell line).
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 50mM phosphate Buffer, 75mM NaCl, pH 7.4.
Purity
Greater than 98% as determined by HPLC and SDS PAGE.
Biological Activity
In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.
sds-page
Citations
More Info
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Introduction
Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
For long term, store lyophilized AdipoQ 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. The lyophilized protein remains stable for 24 months when stored at -20°C.
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Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product not sterile! Please filter the product by an appropriate sterile filter before using it in cell culture.
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Amino Acid Sequence
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.
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Background
What is the molecular weight/Mw of adiponectin Protein?
Adiponectin Protein has a total Mw of 25.5kDa.
What is the source or expression system of adiponectin Protein?
HEK293.
What is the Purity of adiponectin Protein?
adiponectin Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of adiponectin Protein?
In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.
What is the amino acid sequence of adiponectin Protein?
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.
What applications can adiponectin Protein be used in?
adiponectin Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for adiponectin Protein?
The endotoxin level is minimal, adiponectin 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 :
ERCC1 HumanDescription:
Excision Repair Cross-Complementing 1 Human Recombinant
Excision Repair Cross-complementing rodent repair deficiency complementation group 1 (includes overlapping antisense sequence), RAD10, COFS4, UV20, DNA excision repair protein ERCC-1.
Product # :
PRO-1106Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ERCC1 Human Recombinant produced in E. coli is a single polypeptide chain containing 297 amino acids (1-273) and having a molecular mass of 32.5kDa.ERCC1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ERCC1 solution (0.5mg/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
ERCC1 polypeptide is essential for nucleotide excision repair (NER) of damaged DNA and is homologous to Saccharomyces cerevisiae RAD10, which takes part in repair and mitotic intra-chromosomal recombination. NER mechanism includes dual incisions on both sides of the damage catalyzed by two nucleases. In mammalian cells XPG cleaves 3' of the DNA lesion while the ERCC1-XPF complex makes the 5' incision.
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Synonyms
Excision Repair Cross-complementing rodent repair deficiency complementation group 1 (includes overlapping antisense sequence), RAD10, COFS4, UV20, DNA excision repair protein ERCC-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 MGSHMDPGKD KEGVPQPSGP PARKKFVIPL DEDEVPPGVA KPLFRSTQSL PTVDTSAQAA PQTYAEYAIS QPLEGAGATC PTGSEPLAGE TPNQALKPGA KSNSIIVSPR QRGNPVLKFV RNVPWEFGDV IPDYVLGQST CALFLSLRYH NLHPDYIHGR LQSLGKNFAL RVLLVQVDVK DPQQALKELA KMCILADCTL ILAWSPEEAG RYLETYKAYE QKPADLLMEK LEQDFVSRSL EQLIAASRED LALCPGLGPQ KARRLFDVLH EPFLKVP
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 :
PPARG HumanDescription:
Peroxisome Proliferator Activated Receptor Gamma Human Recombinant
Peroxisome proliferator-activated receptor gamma, PPAR-gamma, PPARG, NR1C3, PPARG1, PPARG2.
Product # :
PKA-228Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Peroxisome Proliferator Activated Receptor Gamma Human Recombinant is expressed in E.coli having a molecular weight of 59.2 kDa and fused to an amino terminal hexahistidine tag.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM Tris-HCl and 50% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
The peroxisome proliferator activated receptors (PPARs) are ligandactivated transcription factors within the nuclear receptor superfamily, which play important roles in adipogenesis, glucose homeostasis andinflammation. Three different isotypes can be distinguished; alpha, beta and gamma. PPARg, is mainly expressed in adipose tissue and to lesser extent in colon, the immune system and the retina. Whereas PPARg operates in the catabolism of fatty acids in the liver, PPARg influences the storage of fatty acids in the adipose tissue and plays a role in adipocyte differentiation. PPARg binds to DNA as a heterodimer with retinoid X receptor (RXR), activating expression of target genes after binding ligand.
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Synonyms
Peroxisome proliferator-activated receptor gamma, PPAR-gamma, PPARG, NR1C3, PPARG1, PPARG2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.Avoid multiple freeze-thaw cycles.
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 :
SCG3 HumanDescription:
Secretogranin III Human Recombinant
Secretogranin III, secretogranin-3, SGIII.
Product # :
PRO-1556Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SCG3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 472 amino acids (20-468) and having a molecular mass of 53.0kDa.SCG3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SCG3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SCG3 belongs to the chromogranin/secretogranin family of neuroendocrine secretory proteins. Though, the function of SCG3 is unknown, Granins operate as precursors for biologically active peptides. Several granins are known to serve as helper proteins in sorting and proteolytic processing of prohormones.
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Synonyms
Secretogranin III, secretogranin-3, SGIII.
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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 MGSFPKPGGS QDKSLHNREL SAERPLNEQI AEAEEDKIKK TYPPENKPGQ SNYSFVDNLN LLKAITEKEK IEKERQSIRS SPLDNKLNVE DVDSTKNRKL IDDYDSTKSG LDHKFQDDPD GLHQLDGTPL TAEDIVHKIA ARIYEENDRA VFDKIVSKLL NLGLITESQA HTLEDEVAEV LQKLISKEAN NYEEDPNKPT SWTENQAGKI PEKVTPMAAI QDGLAKGEND ETVSNTLTLT NGLERRTKTY SEDNFEELQY FPNFYALLKS IDSEKEAKEK ETLITIMKTL IDFVKMMVKY GTISPEEGVS YLENLDEMIA LQTKNKLEKN ATDNISKLFP APSEKSHEET DSTKEEAAKM EKEYGSLKDS TKDDNSNPGG KTDEPKGKTE AYLEAIRKNI EWLKKHDKKG NKEDYDLSKM RDFINKQADA YVEKGILDKE EAEAIKRIYS SL.
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.