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1000 results found for “Dickkopf-Related Protein”
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- View Data Sheet
Name :
IFIT3 HumanDescription:
IFN-Induced Protein With Tetratricopeptide Repeats 3 Human Recombinant
IFN-Induced Protein With Tetratricopeptide Repeats 3, IFN-Induced Protein With Tetratricopeptide Repeats 4, IFIT4, Retinoic Acid-Induced Gene G Protein, IFN-Induced 60 KDa Protein, IFI-60K, CIG-49, IFIT-3, IFIT-4, ISG-60, CIG49, IFI60, ISG60, RIG-G, P60, GARG-49, IRG2, IFN-induced protein with tetratricopeptide repeats 3.
Product # :
CYT-898Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- SDS-PAGE
Description
IFIT3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 513 amino acids (1-490 a.a) and having a molecular mass of 58.4kDa. IFIT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
IFIT3 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
IFN-Induced Protein With Tetratricopeptide Repeats 3, also known as IFIT3 is a member of the IFIT family. IFN-induced antiviral protein which performs as an inhibitor of cellular and viral processes, cell migration, proliferation, signaling, as well as viral replication. Furthermore, IFIT3 is significantly induced upon RNA virus infection. Ectopic expression or alternatively knockdown of IFIT3 might, respectively, enhance or impair IRF3-mediated gene expression.
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Synonyms
IFN-Induced Protein With Tetratricopeptide Repeats 3, IFN-Induced Protein With Tetratricopeptide Repeats 4, IFIT4, Retinoic Acid-Induced Gene G Protein, IFN-Induced 60 KDa Protein, IFI-60K, CIG-49, IFIT-3, IFIT-4, ISG-60, CIG49, IFI60, ISG60, RIG-G, P60, GARG-49, IRG2, IFN-induced protein with tetratricopeptide repeats 3.
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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 MGSMSEVTKN SLEKILPQLK CHFTWNLFKE DSVSRDLEDR VCNQIEFLNT EFKATMYNLL AYIKHLDGNN EAALECLRQA EELIQQEHAD QAEIRSLVTW GNYAWVYYHL GRLSDAQIYV DKVKQTCKKF SNPYSIEYSE LDCEEGWTQL KCGRNERAKV CFEKALEEKP NNPEFSSGLA IAMYHLDNHP EKQFSTDVLK QAIELSPDNQ YVKVLLGLKL QKMNKEAEGE QFVEEALEKS PCQTDVLRSA AKFYRRKGDL DKAIELFQRV LESTPNNGYL YHQIGCCYKA KVRQMQNTGE SEASGNKEMI EALKQYAMDY SNKALEKGLN PLNAYSDLAE FLETECYQTP FNKEVPDAEK QQSHQRYCNL QKYNGKSEDT AVQHGLEGLS ISKKSTDKEE IKDQPQNVSE NLLPQNAPNY WYLQGLIHKQ NGDLLQAAKC YEKELGRLLR DAPSGIGSIF LSASELEDGS EEMGQGAVSS SPRELLSNSE QLN.
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Background
What is the molecular weight/Mw of IFIT3 HUMAN Protein?
IFIT3 HUMAN Protein has a total Mw of 58.4kDa.
What is the source or expression system of IFIT3 HUMAN Protein?
Escherichia Coli.
What is the Purity of IFIT3 HUMAN Protein?
IFIT3 HUMAN Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of IFIT3 HUMAN Protein?
The biological functionality of IFIT3 HUMAN Protein will be determined in the future.
What is the amino acid sequence of IFIT3 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSMSEVTKN SLEKILPQLK CHFTWNLFKE DSVSRDLEDR VCNQIEFLNT EFKATMYNLL AYIKHLDGNN EAALECLRQA EELIQQEHAD QAEIRSLVTW GNYAWVYYHL GRLSDAQIYV DKVKQTCKKF SNPYSIEYSE LDCEEGWTQL KCGRNERAKV CFEKALEEKP NNPEFSSGLA IAMYHLDNHP EKQFSTDVLK QAIELSPDNQ YVKVLLGLKL QKMNKEAEGE QFVEEALEKS PCQTDVLRSA AKFYRRKGDL DKAIELFQRV LESTPNNGYL YHQIGCCYKA KVRQMQNTGE SEASGNKEMI EALKQYAMDY SNKALEKGLN PLNAYSDLAE FLETECYQTP FNKEVPDAEK QQSHQRYCNL QKYNGKSEDT AVQHGLEGLS ISKKSTDKEE IKDQPQNVSE NLLPQNAPNY WYLQGLIHKQ NGDLLQAAKC YEKELGRLLR DAPSGIGSIF LSASELEDGS EEMGQGAVSS SPRELLSNSE QLN.
What applications can IFIT3 HUMAN Protein be used in?
IFIT3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFIT3 HUMAN Protein?
The endotoxin level is minimal, IFIT3 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 :
Midkine Human, HisDescription:
Midkine Human Recombinant, His Tag
NEGF-2, Neurite Growth-Promoting Factor 2, MK, Neurite outgrowth-promoting protein, Midgestation and kidney protein, Amphiregulin-associated protein, ARAP, Neurite outgrowth-promoting factor 2, FLJ27379, Midkine, MK1, NEGF2.
Product # :
CYT-444Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Midkine Human Recombinant is manufactured with N-terminal fusion of His Tag, having a molecular mass of 14.6 kDa protein and containing 121 amino acid residues of the Midkine human and 10 additional amino acid residues – His Tag (underlined).
Source
Escherichia Coli.
Formulation
Lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.1M NaCl, pH 7.2.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Midkine (MK) is the product of a retinoic acid responsive gene, MK, and is a member of a family of heparin binding factors. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis. -
Synonyms
NEGF-2, Neurite Growth-Promoting Factor 2, MK, Neurite outgrowth-promoting protein, Midgestation and kidney protein, Amphiregulin-associated protein, ARAP, Neurite outgrowth-promoting factor 2, FLJ27379, Midkine, MK1, NEGF2.
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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 0.2 ml of PBS pH 7.2 and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
MKHHHHHHHM KKKDKVKKGG PGSECAEWAW GPCTPSSKDC GVGFREGTCG AQTQRIRCRV PCNWKKEFGA DCKYKFENWG ACDGGTGTKV RQGTLKKARY NAQCQETIRV TKPCTPKTKA KAKAKKGKGK D.
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 :
AP3S1 HumanDescription:
Assembly Protein Complex 3 Subunit-1 Human Recombinant
CLAPS3, Sigma3A ,AP-3 complex subunit sigma-1, AP-3 complex subunit sigma-3A, Adapter-related protein complex 3 sigma-1 subunit, Clathrin-associated/assembly/adapter protein, small 3, Sigma-3A-adaptin, Sigma-adaptin 3a.
Product # :
PRO-1280Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AP3S1 Human Recombinant produced in E. coli is a single polypeptide chain containing 213 amino acids (1-193) and having a molecular mass of 23.8 kDa. AP3S1 is fused to 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The AP3S1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
AP-3 complex subunit sigma-1 (AP3S1) belongs to the AP-3 complex, an adapter-related complex which is not clathrin-associated. AP3S1 is linkd with the Golgi region in addition to more peripheral structures. AP3S1 facilitates the budding of vesicles from the Golgi membrane and involved in trafficking to lysosomes.
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Synonyms
CLAPS3, Sigma3A ,AP-3 complex subunit sigma-1, AP-3 complex subunit sigma-3A, Adapter-related protein complex 3 sigma-1 subunit, Clathrin-associated/assembly/adapter protein, small 3, Sigma-3A-adaptin, Sigma-adaptin 3a.
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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 MIKAILIFNN HGKPRLSKFY QPYSEDTQQQ IIRETFHLVS RDENVCNFL EGGLLIGGSD NKLIYRHYAT LYFVFCVDSS ESELGILDLI QVFVETLDKC ENVCELDLI FHVDKVHNIL AEMVMGGMVL ETNMNEIVTQ IDAQNKLEKS EAGLAGAPAR AVSAVKNMNL PEIPRNINIG DISIKVPNLP SFK.
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 :
AHSP HumanDescription:
Alpha Hemoglobin Stabilizing Protein Human Recombinant
Alpha-hemoglobin-stabilizing protein, Erythroid-associated factor, Erythroid differentiation-related factor, AHSP, EDRF, ERAF.
Product # :
PRO-720Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AHSP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 102 amino acids (1-102 a.a.) and having a molecular mass of 11.8kDa.The AHSP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AHSP protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Alpha-hemoglobin stabilizing protein (AHSP) is an erythroid-specific protein that acts as a chaperone to prevent the aggregation of A-hemoglobin during normal erythroid cell development. AHSP specifically protects free A-hemoglobin from precipitation in live cells and in solution. AHSP is expected to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia. Furthermore, AHSP promotes alpha globin chain stability in human erythropoiesis. In addition, the AHSP stabilizes the alpha-Hb chain, thus avoiding its precipitation and its ability to generate ROS, which is implicated in cell death. AHSP is expressed in blood and bone marrow. AHSP subunit is a monomer, it forms a heterodimer with free alpha-hemoglobin. On the other hand, AHSP does not bind beta-hemoglobin nor alpha2beta2 hemoglobin A. AHSP is downregulated in TSEs (transmissible spongiform encephalopathies).
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Synonyms
Alpha-hemoglobin-stabilizing protein, Erythroid-associated factor, Erythroid differentiation-related factor, AHSP, EDRF, ERAF.
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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
MALLKANKDL ISAGLKEFSV LLNQQVFNDP LVSEEDMVTV VEDWMNFYIN YYRQQVTGEP QERDKALQEL RQELNTLANP FLAKYRDFLK SHELPSHPPP SS.
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 :
IFNAR1 HumanDescription:
Interferon Alpha and Beta Receptor Subunit 1 Human Recombinant
IFN-alpha/beta R1, IFNAR1, AVP, IFN-alpha-REC, IFNAR, IFNBR, IFRC, Interferon alpha/beta receptor 1, IFN-R-1, IFN-alpha/beta receptor 1, Cytokine receptor class-II member 1, Cytokine receptor family 2 member 1, CRF2-1, Type I interferon receptor 1.
Product # :
CYT-1138Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- SDS-PAGE
Description
IFNAR1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 415 amino acids (28-436a.a.) and having a molecular mass of 47.9kDa. IFNAR1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
IFNAR1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
Interferon Alpha And Beta Receptor or IFNAR1, is part of the class II cytokine receptor family. IFNAR1 forms one of the two chains of a receptor for interferons alpha and beta. IFNAR1 binds and activates the receptor that stimulates Janus protein kinases, which then phosphorylate few proteins, including STAT1 & STAT2. Furthermore, IFNAR1 also acts as an antiviral factor.
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Synonyms
IFN-alpha/beta R1, IFNAR1, AVP, IFN-alpha-REC, IFNAR, IFNBR, IFRC, Interferon alpha/beta receptor 1, IFN-R-1, IFN-alpha/beta receptor 1, Cytokine receptor class-II member 1, Cytokine receptor family 2 member 1, CRF2-1, Type I interferon receptor 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
KNLKSPQKVE VDIIDDNFIL RWNRSDESVG NVTFSFDYQK TGMDNWIKLS GCQNITSTKC NFSSLKLNVY EEIKLRIRAE KENTSSWYEV DSFTPFRKAQ IGPPEVHLEA EDKAIVIHIS PGTKDSVMWA LDGLSFTYSL VIWKNSSGVE ERIENIYSRH KIYKLSPETT YCLKVKAALL TSWKIGVYSP VHCIKTTVEN ELPPPENIEV SVQNQNYVLK WDYTYANMTF QVQWLHAFLK RNPGNHLYKW KQIPDCENVK TTQCVFPQNV FQKGIYLLRV QASDGNNTSF WSEEIKFDTE IQAFLLPPVF NIRSLSDSFH IYIGAPKQSG NTPVIQDYPL IYEIIFWENT SNAERKIIEK KTDVTVPNLK PLTVYCVKAR AHTMDEKLNK SSVFSDAVCE KTKPGNTSKH HHHHH.
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Background
What is the molecular weight/Mw of IFNAR1 HUMAN Protein?
IFNAR1 HUMAN Protein has a total Mw of 47.9kDa.
What is the source or expression system of IFNAR1 HUMAN Protein?
Sf9, Insect cells.
What is the Purity of IFNAR1 HUMAN Protein?
IFNAR1 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNAR1 HUMAN Protein?
The biological functionality of IFNAR1 HUMAN Protein will be determined in the future.
What is the amino acid sequence of IFNAR1 HUMAN Protein?
KNLKSPQKVE VDIIDDNFIL RWNRSDESVG NVTFSFDYQK TGMDNWIKLS GCQNITSTKC NFSSLKLNVY EEIKLRIRAE KENTSSWYEV DSFTPFRKAQ IGPPEVHLEA EDKAIVIHIS PGTKDSVMWA LDGLSFTYSL VIWKNSSGVE ERIENIYSRH KIYKLSPETT YCLKVKAALL TSWKIGVYSP VHCIKTTVEN ELPPPENIEV SVQNQNYVLK WDYTYANMTF QVQWLHAFLK RNPGNHLYKW KQIPDCENVK TTQCVFPQNV FQKGIYLLRV QASDGNNTSF WSEEIKFDTE IQAFLLPPVF NIRSLSDSFH IYIGAPKQSG NTPVIQDYPL IYEIIFWENT SNAERKIIEK KTDVTVPNLK PLTVYCVKAR AHTMDEKLNK SSVFSDAVCE KTKPGNTSKH HHHHH.
What applications can IFNAR1 HUMAN Protein be used in?
IFNAR1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNAR1 HUMAN Protein?
The endotoxin level is minimal, IFNAR1 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 :
BMP3 HumanDescription:
Bone Morphogenetic protein-3 Human Recombinant
Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.
Product # :
CYT-937Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
BMP3 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 110 amino acids and having a molecular mass of 24.8kDa.The BMP-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BMP-3 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.
Purity
Greater than 95.0% as determined by: (a) Analysis by HPLC. (b) Analysis by SDS-PAGE.
Biological Activity
The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.More Info
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Introduction
Bone Morphogenetic Protein 3 (BMP3) is one of the BMPs, some of which are members of the TGF-beta superfamily (BMP2-7). There are more than 13 BMPs, which are involved in inducing cartilage and bone formation, embryogenesis and morphogenesis of various tissues and organs. In addition, BMPs regulate the growth, differentiation, chemotaxis, and apoptosis of various cell types. Akin to most other TGF-beta family proteins, BMPs are extremely conserved across animal species. At the amino acid sequence level, mature human and rat BMP3 are 98% identical.
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Synonyms
Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BMP3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-3 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 BMP3 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.
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Background
Bone Morphogenetic Protein-3 Human Recombinant: Unveiling the Potential of a Key Regulator in Tissue Regeneration
Abstract:
Bone Morphogenetic Protein-3 (BMP-3) human recombinant is a critical member of the bone morphogenetic protein family, known for its role in tissue development, repair, and regeneration. This research paper provides a comprehensive analysis of BMP-3, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-3 human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.
Introduction:
Tissue regeneration is a complex biological process requiring precise molecular cues. BMP-3, a crucial member of the BMP family, plays a significant role in tissue development and regeneration. This paper explores the unique features of BMP-3 and presents novel approaches for its production and optimization, aiming to unlock its therapeutic potential in various regenerative contexts.
Characteristics and Signaling Pathways:
BMP-3 is a secreted protein that binds to cell surface receptors, initiating intracellular signaling cascades. It influences cell differentiation, proliferation, and extracellular matrix synthesis through both Smad-dependent and Smad-independent signaling pathways. BMP-3 signaling regulates critical processes involved in tissue regeneration, including chondrogenesis and osteogenesis.
Production of BMP-3 Human Recombinant:
Efficient production methodologies are essential for harnessing the therapeutic potential of BMP-3 human recombinant. Recombinant protein expression systems, such as Escherichia coli or mammalian cells, have been utilized to produce functional BMP-3. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding optimization, have been employed to enhance the yield and activity of BMP-3 recombinant protein.
Potential Therapeutic Applications:
BMP-3 human recombinant holds significant promise in the field of regenerative medicine. It plays a crucial role in bone and cartilage regeneration, making it a potential candidate for the treatment of skeletal disorders and tissue injuries. Additionally, BMP-3 signaling influences tissue remodeling and wound healing, suggesting its broader therapeutic applications in other regenerative processes.
Conclusion:
BMP-3 human recombinant represents a key regulator in tissue regeneration, with immense potential in regenerative medicine. Optimizing production methodologies and further unraveling its signaling mechanisms will enhance its therapeutic applications. With its implications in bone and cartilage regeneration and its role in tissue remodeling, BMP-3 human recombinant emerges as a promising tool for promoting tissue repair and regeneration.
What is the molecular weight/Mw of BMP3 Protein?
BMP3 Protein has a total Mw of 24.8kDa.
What is the source or expression system of BMP3 Protein?
Escherichia Coli.
What is the Purity of BMP3 Protein?
BMP3 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP3 Protein?
The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.
What is the amino acid sequence of BMP3 Protein?
QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.
What applications can BMP3 Protein be used in?
BMP3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP3 Protein?
The endotoxin level is minimal, BMP3 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 :
DCT HumanDescription:
Dopachrome Tautomerase Human Recombinant
L-dopachrome tautomerase (EC:5.3.3.12), DCT, DT, L-dopachrome Delta-isomerase Tyrosinase-related protein 2, TRP-2, TRP2, TYRP2.
Product # :
ENZ-874Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DCT Human Recombinant produced in Sf9 Insect cell is a single, glycosylated polypeptide chain containing 455 amino acids (24-472aa.a) and having a molecular mass of 52.1kDa. DCT is fused to a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9 Insect cells.
Formulation
STK3 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Dopachrome Tautomerase also known as DCT, belongs to the tyrosinase family. DCT takes a significant part in the synthesis of the melanin pigment including tyrosinase (Tyr), tyrosinase-related protein 1 (Tyrp1). Which are highly involved in eumelanin synthesis. The change among the eumelanin and the pheomelanin pathways is assumed to depend on the presence of cysteine. Hence, in the lack of cysteine, dopaquinone, the product of tyrosinase action, is transformed to cyclodopa (leucodopachrome) and afterwards to dopachrome (and DOPA).
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Synonyms
L-dopachrome tautomerase (EC:5.3.3.12), DCT, DT, L-dopachrome Delta-isomerase Tyrosinase-related protein 2, TRP-2, TRP2, TYRP2.
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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
QFPRVCMTVD SLVNKECCPR LGAESANVCG SQQGRGQCTE VRADTRPWSG PYILRNQDDR ELWPRKFFHR TCKCTGNFAG YNCGDCKFGW TGPNCERKKP PVIRQNIHSL SPQEREQFLG ALDLAKKRVH PDYVITTQHW LGLLGPNGTQ PQFANCSVYD FFVWLHYYSV RDTLLGPGRP YRAIDFSHQG PAFVTWHRYH LLCLERDLQR LIGNESFALP YWNFATGRNE CDVCTDQLFG AARPDDPTLI SRNSRFSSWE TVCDSLDDYN HLVTLCNGTY EGLLRRNQMG RNSMKLPTLK DIRDCLSLQK FDNPPFFQNS TFSFRNALEG FDKADGTLDS QVMSLHNLVH SFLNGTNALP HSAANDPIFV VLHSFTDAIF DEWMKRFNPP ADAWPQELAP IGHNRMYNMV PFFPPVTNEE LFLTSDQLGY SYAIDLPVSV EETPGWPTTH HHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
FGF 8 HumanDescription:
Fibroblast Growth Factor-8 Human Recombinant
FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.
Product # :
CYT-839Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
FGF 8 Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acids and having a total molecular mass of 22.5kDa.
Source
Escherichia Coli.
Formulation
Lyophilized from a sterile 0.2 micron filtered aqueous solution containing 0.1% TFA.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Biological Activity
The ED50, as determined by its ability to induce proliferation of NR6-R 3T3, is 0.915ng/ml, corresponding to a specific activity of 1.1x106units/mg.
More Info
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Introduction
FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.
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Synonyms
FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized FGF-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-8 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 FGF-8 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
MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGDPFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR.
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Background
What is the molecular weight/Mw of FGF8 Protein?
FGF8 Protein has a total Mw of 22.5kDa.
What is the source or expression system of FGF8 Protein?
Escherichia Coli.
What is the Purity of FGF8 Protein?
FGF8 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF8 Protein?
The ED50, as determined by its ability to induce proliferation of NR6-R 3T3, is 0.915ng/ml, corresponding to a specific activity of 1.1x106units/mg.
What is the amino acid sequence of FGF8 Protein?
MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGDPFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR.
What applications can FGF8 Protein be used in?
FGF8 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF8 Protein?
The endotoxin level is minimal, FGF8 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 :
Leptin Human, PEGDescription:
Leptin Human Recombinant, PEG
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1108Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
Pegylated Leptin Human Recombinant produced in E.Coli is a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Pegylated Leptin Human Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Biological Activity is < than 0.1% as determined by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It’s in vitro activity is 5-7 fold lower than the non-pegylated recombinant human leptin but in vivo it has profound weight reducing effect, resulting mainly from reduced food intake.
More Info
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Introduction
Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Pegylated leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution leptin N82K 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 Pegylated leptin in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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 :
TGIF2LX HumanDescription:
TGFB-Induced Factor Homeobox 2-Like, X-Linked Human Recombinant
Homeobox protein TGIF2LX, TGF-beta-induced transcription factor 2-like protein, TGFB-induced factor 2-like protein, X-linked, TGIF-like on the X, TGIF2LX, TGIFLX, TGFB-Induced Factor Homeobox 2-Like, X-Linked.
Product # :
PRO-1902Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TGIF2LX Human Recombinant produced in E. coli is. a single polypeptide chain containing 264 amino acids (1-241) and having a molecular mass of 29.1kDa.TGIF2LX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TGIF2LX solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
TGFB-Induced Factor Homeobox 2-Like, X-Linked (TGIF2LX) belongs to the TALE/TGIF homeobox family of transcription factors and takes part in spermatogenesis. A homolog of TGIF2LX is located in the male specific region of chromosome Y, in a block of sequence which is the outcome of a large X-to-Y transposition.
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Synonyms
Homeobox protein TGIF2LX, TGF-beta-induced transcription factor 2-like protein,
TGFB-induced factor 2-like protein, X-linked, TGIF-like on the X, TGIF2LX, TGIFLX, TGFB-Induced Factor Homeobox 2-Like, X-Linked. -
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 MGSMEAAADG PAETQSPVEK DSPAKTQSPA QDTSIMSRNN ADTGRVLALP EHKKKRKGNL PAESVKILRD WMYKHRFKAY PSEEEKQMLS EKTNLSLLQI SNWFINARRR ILPDMLQQRR NDPIIGHKTG KDAHATHLQS TEASVPAKSG PSGPDNVQSL PLWPLPKGQM SREKQPDPES APSQKLTGIA QPKKKVKVSV TSPSSPELVS PEEHADFSSF LLLVDAAVQR AAELELEKKQ EPNP.
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 :
ARMS2 HumanDescription:
Age-Related Maculopathy Susceptibility 2 Human Recombinant
Age-related maculopathy susceptibility protein 2, ARMD8
Product # :
PRO-2628Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
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Description
ARMS2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (1-107a.a.) and having a molecular mass of 13.8kDa.ARMS2 is fused to a 23 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
ARMS2 protein solution (0.25mg/ml) containing 20 mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Age-Related Maculopathy Susceptibility 2 or ARMS2 is a protein that is is being researches for its ability to take part in diseases in old age. Mutations in Age-Related Maculopathy Susceptibility 2 is related to age-caused molecular degeneration.
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Synonyms
Age-related maculopathy susceptibility protein 2, ARMD8
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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 MGSMLRLYPG PMVTEAEGKG GPEMASLSSS VVPVSFISTL RESVLDPGVG GEGASDKQRS KLSLSHSMIP AAKIHTELCL PAFFSPAGTQ RRFQQPQHHL TLSIIHTAAR
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 :
CIDEC HumanDescription:
Cell Death-Inducing DFFA-Like Effector C Human Recombinant
Cell Death-Inducing DFFA-Like Effector C, FSP27, CIDE3, FPLD5, Cell Death-Inducing DFFA-Like Effector Protein C, Fat-Specific Protein FSP27 Homolog, Cell Death Activator CIDE-3, Fat Specific Protein 27, CIDE-3, CIDEC.
Product # :
PRO-2026Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- formulation
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Description
CIDEC Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Glu2-Gln238) containing 247 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 28kDa.
Source
Escherichia Coli.
Formulation
CIDEC filtered (0.4µm) solution at a concentration of 0.4mg/ml in 30mM acetate buffer and 10mM dithiothreitol, pH 4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Cell Death-Inducing DFFA-Like Effector C (CIDEC) belongs to the cell death-inducing DNA fragmentation factor-like effector family, whose members have significant roles in apoptosis. CIDEC is expressed mainly in adipocytes, intestine, heart, stomach, and weakly in the brain, kidney and liver. CIDEC overexpression in preadipocytes induces apoptosis. CIDEC regulates enlargement of lipid droplets.
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Synonyms
Cell Death-Inducing DFFA-Like Effector C, FSP27, CIDE3, FPLD5, Cell Death-Inducing DFFA-Like Effector Protein C, Fat-Specific Protein FSP27 Homolog, Cell Death Activator CIDE-3, Fat Specific Protein 27, CIDE-3, CIDEC.
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Physical Appearance
Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MKHHHHHHASEYAMKSLSLL YPKSLSRHVS VRTSVVTQQL LSEPSPKAPR ARPCRVSTAD RSVRKGIMAY SLEDLLLKVR DTLMLADKPF FLVLEEDGTT VETEEYFQAL AGDTVFMVLQ KGQKWQPPSE QGTRHPLSLS HKPAKKIDVA RVTFDLYKLN PQDFIGCLNV KATFYDTYSL SYDLHCCGAK RIMKEAFRWA LFSMQATGHV LLGTSCYLQQ LLDATEEGQP PKGKASSLIP TCLKILQ.
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 :
TIMM8A HumanDescription:
Translocase of Inner Mitochondrial Membrane 8 Homolog A Human Recombinant
Mitochondrial import inner membrane translocase subunit Tim8 A, TIMM8A, Translocase of Inner Mitochondrial Membrane 8 Homolog A, DDP, DDP1, DFN1, MTS, TIM8, Deafness dystonia protein 1, X-linked deafness dystonia protein.
Product # :
PRO-1818Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TIMM8A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 120 amino acids (1-97) and having a molecular mass of 13.4 kDa.TIMM8A is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TIMM8A solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Translocase of Inner Mitochondrial Membrane 8 Homolog A (TIMM8A) takes part in the import and insertion of hydrophobic membrane proteins from the cytoplasm into the mitochondrial. TIMM8A plays a role as a chaperone-like protein which protects the hydrophobic precursors from aggregation and leads them through the mitochondrial intermembrane space. TIMM8A is essential for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Defects in TIMM8A cause Jensen syndrome. TIMM8A and TIMM13, forms a 70 kDa heterohexamer.
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Synonyms
Mitochondrial import inner membrane translocase subunit Tim8 A, TIMM8A, Translocase of Inner Mitochondrial Membrane 8 Homolog A, DDP, DDP1, DFN1, MTS, TIM8, Deafness dystonia protein 1, X-linked deafness dystonia protein.
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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 MGSMDSSSSS SAAGLGAVDP QLQHFIEVET QKQRFQQLVH QMTELCWEKC MDKPGPKLDS RAEACFVNCV ERFIDTSQFI LNRLEQTQKS KPVFSESLSD.
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 :
GroEL HumanDescription:
GroEL (HSP60) Human Recombinant
CPN60, GROEL, HSP60, HSP65, SPG13, CHA60, GROL, crpA, mopA, 60 kDa heat shock protein mitochondrial, Heat shock protein 60, HSP-60, 60 kDa chaperonin, Chaperonin 60, Mitochondrial matrix protein P1, P60 lymphocyte protein, HuCHA60, HSPD1.
Product # :
HSP-016Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
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Description
Recombinant Human GroEL, HSP60 produced in E.Coli is a single, non-glycosylated polypeptide chain fused to a 20 a.a. His tag at N-terminus containing 593 amino acids (1-573 a.a.) and having a molecular mass of 63kDa.The HSP60 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GroEL protein contains 20mM Tris-HCl buffer pH-8.0, 5mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GroEL, HSP60 is a chaperonin located in the mitochondria which is responsible for the transportation & refolding of proteins from the cytoplasm directly into the mitochondrial matrix. GroEL is regulated by the HSP10 cochaperonin, which is a single heptameric protein ring having a molecular mass of 10 kDa which form a unique complex with HSP60. HSP10, GroES coordinates the ATPase activity of the HSP60 subunits in order to allow the release of bound polypeptide in a manner that is productive for its correct folding.
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Synonyms
CPN60, GROEL, HSP60, HSP65, SPG13, CHA60, GROL, crpA, mopA, 60 kDa heat shock protein mitochondrial, Heat shock protein 60, HSP-60, 60 kDa chaperonin, Chaperonin 60, Mitochondrial matrix protein P1, P60 lymphocyte protein, HuCHA60, HSPD1.
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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 MLRLPTVFRQ MRPVSRVLAP HLTRAYAKDV KFGADARALMLQGVDLLADA VAVTMGPKGR TVIIEQSWGS PKVTKDGVTV AKSIDLKDKY KNIGAKLVQDVANNTNEEAG DGTTTATVLA RSIAKEGFEK ISKGANPVEI RRGVMLAVDA VIAELKKQSKPVTTPEEIAQ VATISANGDK EIGNIISDAM KKVGRKGVIT VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ DAYVLLSEKK ISSIQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL TLNLEDVQPH DLGKVGEVIV TKDDAMLLKG KGDKAQIEKR IQEIIEQLDV TTSEYEKEKL NERLAKLSDG VAVLKVGGTS DVEVNEKKDR VTDALNATRA AVEEGIVLGG GCALLRCIPA LDSLTPANED QKIGIEIIKR TLKIPAMTIA KNAGVEGSLI VEKIMQSSSE VGYDAMAGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT TAEVVVTEIP KEEKDPGMGA MGGMGGGMGG GMF.
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 :
BD 3 RatDescription:
Beta Defensin-3 Rat Recombinant
Beta-defensin 3, BD-3, Defensin beta 3, Defb3.
Product # :
CYT-063Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
BD-3 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 41 amino acids and having a molecular mass of 4.5kDa.The BD-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BD-3 protein was lyophilized from a 0.2µm filtered concentrated 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
Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 4-20µg/ml, corresponding to a specific activity of 50,000-250,000units/mg.More Info
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Introduction
Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103A, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.
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Synonyms
Beta-defensin 3, BD-3, Defensin beta 3, Defb3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BD-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-3 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 BD-3 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
KKVYNAVSCM TNGGICWLKC SGTFREIGSC GTRQLKCCKK K.
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Background
What is the molecular weight/Mw of BD3 Protein?
BD3 Protein has a total Mw of 4.5kDa.
What is the source or expression system of BD3 Protein?
Escherichia Coli.
What is the Purity of BD3 Protein?
BD3 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of BD3 Protein?
Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 4-20µg/ml, corresponding to a specific activity of 50,000-250,000units/mg.
What is the amino acid sequence of BD3 Protein?
KKVYNAVSCM TNGGICWLKC SGTFREIGSC GTRQLKCCKK K.
What applications can BD3 Protein be used in?
BD3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BD3 Protein?
The endotoxin level is minimal, BD3 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 :
Aprotinin ProteinDescription:
Aprotinin
Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.
Product # :
PRO-285Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- More Info
Description
Aprotinin is a natural proteinase inhibitor polypeptide consisting of fifty-eight amino acids {C284H432N84O79S7} arranged in a single polypeptide chain, cross-linked by three disulfide bridges and having a molecular mass of 6512.
Source
Bovine Lung.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
More Info
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Introduction
Aprotinin inhibits the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin and trypsin. Aprotinin is present in blood and in most tissues, with a high concentration in lung. Aprotinin inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. In platelets, aprotinin reduces glycoprotein loss (e.g., GpIb, GpIIb/IIIa), while in granulocytes it prevents the expression of pro-inflammatory adhesive glycoproteins (e.g., CD11b).
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Synonyms
Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Aprotinin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Aprotinin 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 Aprotinin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Specific Activity
5,940 KIU (Kallikrein Inactivator Units) per mg, 3.3 pH.Eur.U/mg.
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 :
TGFBRAP1 HumanDescription:
Transforming Growth Factor Beta Receptor Associated Protein 1 Human Recombinant
TRAP-1, TRAP1, Transforming growth factor-beta receptor-associated protein 1, TGF-beta receptor-associated protein 1.
Product # :
PRO-1890Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TGFBRAP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (601-860 a.a) and having a molecular mass of 33kDa.TGFBRAP1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TGFBRAP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
TGF-beta receptor-associated protein 1 also known as TGFBRAP1 takes part in the TGF-beta/activin signaling pathway. TGFBRAP1 is related with inactive heteromeric TGF-beta and activin receptor complexes, mainly through the type II receptor, and is released upon activation of signaling. TGFBRAP1recruits SMAD4 to the vicinity of the receptor complex and smoothes the progress of its interaction with receptor-regulated Smads, such as SMAD2.
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Synonyms
TRAP-1, TRAP1, Transforming growth factor-beta receptor-associated protein 1, TGF-beta receptor-associated protein 1.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSKRLQ KEEYHTHLAV LYLEEVLLQR ASASGKGAEA TETQAKLRRL LQKSDLYRVH FLLERLQGAG LPMESAILHG KLGEHEKALH ILVHELQDFA AAEDYCLWCS EGRDPPHRQQ LFHTLLAIYL HAGPTAHELA VAAVDLLNRH ATEFDAAQVL QMLPDTWSVQ LLCPFLMGAM RDSIHARRTM QVALGLARSE NLIYTYDKMK LKGSSIQLSD KKLCQICQNP FCEPVFVRYP NGGLVHTHCA ASRHTNPSSS SPGTRT
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 :
RQCD1 HumanDescription:
RCD1 Required for Cell Differentiation1 Human Recombinant
Cell differentiation protein RCD1 homolog, Rcd-1, RQCD1, RCD1, CNOT9, CT129, RCD1+.
Product # :
PRO-008Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
RQCD1 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 319 amino acids (1-299 a.a.) and having a molecular mass of 35.7kDa. The RQCD1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RQCD1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
RQCD1 is a novel transcriptional cofactor which mediates retinoic acid-induced cell differentiation. RQCD1 down-regulates MYB- and JUN-dependent transcription and may have a role in cell differentiation. RQCD1 also has a role in retinoic acid-controlled lung development.
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Synonyms
Cell differentiation protein RCD1 homolog, Rcd-1, RQCD1, RCD1, CNOT9, CT129, RCD1+.
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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 MHSLATAAPV PTTLAQVDRE KIYQWINELS SPETRENALL ELSKKRESVP DLAPMLWHSF GTIAALLQEI VNIYPSINPP TLTAHQSNRV CNALALLQCV ASHPETRSAF LAAHIPLFLY PFLHTVSKTR PFEYLRLTSL GVIGALVKTD EQEVINFLLT TEIIPLCLRI MESGSELSKT VATFILQKIL LDDTGLAYIC QTYERFSHVA MILGKMVLQL SKEPSARLLK HVVRCYLRLS DNPRAREALR QCLPDQLKDT TFAQVLKDDT TTKRWLAQLV KNLQEGQVTD PRGIPLPPQ.
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 :
MMACHC HumanDescription:
Methylmalonic Aciduria cblC type, with Homocystinuria Human Recombinant
Methylmalonic aciduria and homocystinuria type C protein, MMACHC, cblC, RP11-291L19.3.
Product # :
PRO-1119Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MMACHC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 306 amino acids (1-282 a.a) and having a molecular mass of 34.3kDa.MMACHC is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MMACHC protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Though the exact role of MMACHC is unknown, its C-terminal region shows similarity to TonB, which is a bacterial protein involved in energy transduction for cobalamin (vitamin B12) uptake. Therefore, it is suggested that MMACHC may have a role in the binding and intracellular trafficking of cobalamin. MMACHC mutations are linked with methylmalonic aciduria and homocystinuria type cblC. MMACHC is widely expressed, it is expressed at higher level in the fetal liver, however it is also expressed in the spleen, lymph node, thymus and bone marrow. MMACHC is weakly or not expressed in the peripheral blood leukocytes.
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Synonyms
Methylmalonic aciduria and homocystinuria type C protein, MMACHC, cblC, RP11-291L19.3.
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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 MGSHMEPKVA ELKQKIEDTL CPFGFEVYPF QVAWYNELLP PAFHLPLPGP TLAFLVLSTP AMFDRALKPF LQSCHLRMLT DPVDQCVAYH LGRVRESLPE LQIEIIADYE VHPNRRPKIL AQTAAHVAGA AYYYQRQDVE ADPWGNQRIS GVCIHPRFGG
WFAIRGVVLL PGIEVPDLPP RKPHDCVPTR ADRIALLEGF NFHWRDWTYR DAVTPQERYS EEQKAYFSTP PAQRLALLGL AQPSEKPSSP SPDLPFTTPA PKKPGNPSRA RSWLSPRVSP PASPGP.
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 :
DCPS HumanDescription:
Decapping Enzyme, Scavenger Human Recombinant
Scavenger mRNA-decapping enzyme DcpS, DCS-1, Hint-related 7meGMP-directed hydrolase, Histidine triad protein member 5, HINT-5, DCPS, DCS1, HINT5, HSPC015, HSL1.
Product # :
ENZ-159Price :
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Shipped with Ice Packs
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Description
DCPS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-337 a.a.) and having a molecular mass of 40.7kDa.DCPS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DCPS protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Scavenger mRNA-decapping enzyme (DCPS) is a member of the HIT family. DCPS is required for the complete degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. It was shown that DCPS hydrolyzes the residual m7GpppN cap structure after the complete 3'–5' degradation of the mRNA by the exosome. Furthermore, DCPS releases m7GMP and is incapable of cleaving cap structures attached to a long RNA chain.
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Synonyms
Scavenger mRNA-decapping enzyme DcpS, DCS-1, Hint-related 7meGMP-directed hydrolase, Histidine triad protein member 5, HINT-5, DCPS, DCS1, HINT5, HSPC015, HSL1.
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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 MADAAPQLGK RKRELDVEEA HAASTEEKEA GVGNGTCAPV RLPFSGFRLQ KVLRESARDK IIFLHGKVNE ASGDGDGEDA VVILEKTPFQ VEQVAQLLTG SPELQLQFSN DIYSTYHLFP PRQLNDVKTT VVYPATEKHL QKYLRQDLRL IRETGDDYRN ITLPHLESQS LSIQWVYNIL DKKAEADRIV FENPDPSDGF VLIPDLKWNQ QQLDDLYLIA ICHRRGIRSL RDLTPEHLPL LRNILHQGQE AILQRYRMKG DHLRVYLHYL PSYYHLHVHF TALGFEAPGS GVERAHLLAE VIENLECDPR HYQQRTLTFA LRADDPLLKL LQEAQQS.
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 :
PDXK HumanDescription:
Pyridoxal Kinase Human Recombinant
Pyridoxal kinase, Pyridoxine kinase, PDXK, C21orf124, C21orf97, PKH, PNK, PRED79, FLJ31940, FLJ37311, MGC15873, MGC31754, MGC52346, DKFZp566A071.
Product # :
PKA-326Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PDXK Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 336 amino acids (1-312 a.a.) and having a molecular mass of 37.6kDa. The PDXK is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PDXK solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
PDXK converts vitamin B6 to Pyridoxal-5-phosphate (PLP), which is a vital cofactor in the intermediate metabolism of amino acids and neurotransmitters. PDXK is cytoplasmic and probably acts as a homodimer. The biological validity of the alternatively spliced transcript variants has not been determined.
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Synonyms
Pyridoxal kinase, Pyridoxine kinase, PDXK, C21orf124, C21orf97, PKH, PNK, PRED79, FLJ31940, FLJ37311, MGC15873, MGC31754, MGC52346, DKFZp566A071.
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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 MGSHMEEECR VLSIQSHVIR GYVGNRAATF PLQVLGFEID AVNSVQFSNH TGYAHWKGQV LNSDELQELY EGLRLNNMNK YDYVLTGYTR DKSFLAMVVD IVQELKQQNP RLVYVCDPVL GDKWDGEGSM YVPEDLLPVY KEKVVPLADI ITPNQFEAELLSGRKIHSQE EALRVMDMLH SMGPDTVVIT SSDLPSPQGS NYLIVLGSQR RRNPAGSVVM ERIRMDIRKV DAVFVGTGDL FAAMLLAWTH KHPNNLKVAC EKTVSTLHHV LQRTIQCAKA QAGEGVRPSP MQLELRMVQS KRDIEDPEIV VQATVL.
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 :
DNAL4 HumanDescription:
Dynein Axonemal Light Chain 4 Human Recombinant
Dynein light chain 4 axonemal, DNAL4, PIG27.
Product # :
PRO-227Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DNAL4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids (1-105 a.a) and having a molecular mass of 14.1kDa.DNAL4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DNAL4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
DNAL4 is a member of the dynein light chain family. DNAL4 is a component of the dynein motor complex in cells that converts the chemical energy contained in ATP into the mechanical energy of movement. Dynein transports various cellular cargos by moving the length of cytoskeletal microtubules towards the minus-end of the microtubule, which is typically oriented towards the cell center.
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Synonyms
Dynein light chain 4 axonemal, DNAL4, PIG27.
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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 MGETEGKKDE ADYKRLQTFP LVRHSDMPEE MRVETMELCV TACEKFSNNN ESAAKMIKET MDKKFGSSWH VVIGEGFGFE ITHEVKNLLY LYFGGTLAVC VWKCS.
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 :
DLK1 HumanDescription:
Delta-Like 1 Human Recombinant
DLK1, Delta-Like 1 Homolog (Drosophila), PREF1, DLK-1, FA1, DLK, PG2, Delta-Like Homolog (Drosophila), Protein Delta Homolog 1, Preadipocyte Factor 1, Fetal Antigen 1, Secredeltin, DELTA1, Pref-1, ZOG.
Product # :
PRO-2256Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DLK1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 288 amino acids (24-303 a.a) and having a molecular mass of 30.7kDa.DLK1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
DLK1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Delta-Like 1, also known as DLK1 is a member of the Notch/Delta/Serrate family of epidermal growth factor (EGF)-like repeat-containing proteins which act as ligands in the Notch signaling pathway. Furthermore, DLK1 has six highly conserved epidermal-growth-factor motifs and it also contains up to ten O-glycosylation and N-glycosylation locations, six of them are differentially glycosylated.
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Synonyms
DLK1, Delta-Like 1 Homolog (Drosophila), PREF1, DLK-1, FA1, DLK, PG2, Delta-Like Homolog (Drosophila), Protein Delta Homolog 1, Preadipocyte Factor 1, Fetal Antigen 1, Secredeltin, DELTA1, Pref-1, ZOG.
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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
AECFPACNPQ NGFCEDDNVC RCQPGWQGPL CDQCVTSPGC LHGLCGEPGQ CICTDGWDGE LCDRDVRACS SAPCANNGTC VSLDDGLYEC SCAPGYSGKD CQKKDGPCVI NGSPCQHGGT CVDDEGRASH ASCLCPPGFS GNFCEIVANS CTPNPCENDG VCTDIGGDFR CRCPAGFIDK TCSRPVTNCA SSPCQNGGTC LQHTQVSYEC LCKPEFTGLT CVKKRALSPQ QVTRLPSGYG LAYRLTPGVH ELPVQQPEHR ILKVSMKELN KKTPLLTEGQ LEHHHHHH.
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 :
FABP5 Human, HisDescription:
Fatty Acid Binding Protein 5 Human Recombinant, His Tag
Fatty acid-binding protein epidermal, E-FABP, Fatty acid-binding protein 5, Psoriasis-associated fatty acid-binding protein homolog, PA-FABP, FABP5, EFABP, PAFABP.
Product # :
PRO-666Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FABP5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids and having a molecular mass of 19.66kDa. FABP5 is fused to His tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
FABP5 His-Tag is supplied in 20mM Tris HCl pH-8 and 50% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Human Fatty Epidermal Acid Binding Protein FABP also called FABP-5 is a 15 kD member of the intracellular fatty acid binding protein (FABP) family, which is known for the ability to bind fatty acids and related compounds ( bile acids or retinoids). In an internal cavity. The fatty acid binding proteins aP2 (fatty acid binding protein [FABP]-4) and mal1 (EFABP) are closely related and both are expressed in adipocytes. Absence of EFABP/mal1 resulted in increased systemic insulin sensitivity in two models of obesity and insulin resistance. Adipocytes isolated from mal1-deficient mice also exhibited enhanced insulin-stimulated glucose transport capacity. In contrast, mice expressing high levels of mal1 in adipose tissue display reduced systematic insulin activity.
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Synonyms
Fatty acid-binding protein epidermal, E-FABP, Fatty acid-binding protein 5, Psoriasis-associated fatty acid-binding protein homolog, PA-FABP, FABP5, EFABP, PAFABP.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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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.Please avoid 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.