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1000 results found for “Dynactin”
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Name :
CoV-2 S1 (16-685), BiotinDescription:
Coronavirus 2019 Spike Glycoprotein-S1 (16-685 a.a.), Biotinylated Recombinant
Product # :
SARS-028Price :
Quantity :
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Shipped at Room temp
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Description
The HEK293 derived Biotinylated recombinant protein contains the Coronavirus 2019 CoV-2 Spike Glycoprotein S1, Wuhan-Hu-1 strain, amino acids 16-685 fused to His tag & Avi-tag at C-terminal.
Source
HEK293 Cells.
Formulation
CoV-2 S1 protein is supplied in 1x PBS pH-7.4 & 5% trehalose.
Purity
Protein is >90% pure as determined SDS-PAGE.
Citations
More Info
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Introduction
A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.
The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.
While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Cov-2 Spike S1 Glycoprotein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CoV2 Spike protein 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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Purification Method
Purified by Metal-Afinity chromatographic technique.
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 :
CCNB1 HumanDescription:
Cyclin-B1 Human Recombinant
G2/mitotic-specific cyclin-B1, cyclin B1, CCNB.
Product # :
PKA-037Price :
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Shipped with Ice Packs
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Description
CCNB1 Human Recombinant produced in E. coli is a single polypeptide chain containing 457 amino acids (1-433) and having a molecular mass of 50.9 kDa.CCNB1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CCNB1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM NaCl and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Cyclin B1 (CCNB1) is a regulatory protein involved in mitosis. CCNB1 creates a complex with p34(cdc2) to form the maturation-promoting factor (MPF). CCNB1 is vital for the control of the cell cycle at the G2/M (mitosis) transition. CCNB1 builds up steadily during the G2 and is immediately destroyed at mitosis. The 2 alternative transcripts produce a constitutively expressed transcript and a cell cycle-regulated transcript which is expressed predominantly during G2/M phase. These transcripts are a result of alternate transcription initiation sites.
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Synonyms
G2/mitotic-specific cyclin-B1, cyclin B1, CCNB.
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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 MGSHMALRVT RNSKINAENK AKINMAGAKR VPTAPAATSK PGLRPRTALG DIGNKVSEQL QAKMPMKKEA KPSATGKVID KKLPKPLEKV PMLVPVPVSE PVPEPEPEPE PEPVKEEKLS PEPILVDTAS PSPMETSGCA PAEEDLCQAF SDVILAVNDV DAEDGADPNL CSEYVKDIYA YLRQLEEEQA VRPKYLLGRE VTGNMRAILI DWLVQVQMKF RLLQETMYMT VSIIDRFMQN NCVPKKMLQL VGVTAMFIAS KYEEMYPPEI GDFAFVTDNT YTKHQIRQME MKILRALNFG LGRPLPLHFL RRASKIGEVD VEQHTLAKYL MELTMLDYDM VHFPPSQIAA GAFCLALKIL DNGEWTPTLQ HYLSYTEESL LPVMQHLAKN VVMVNQGLTK HMTVKNKYAT SKHAKISTLP QLNSALVQDL AKAVAKV.
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 :
HMGB1 HumanDescription:
High-Mobility Group Box 1 Human Recombinant
HMG1, HMG3, SBP-1, Amphoterin, HMGB1, High-Mobility Group Box 1.
Product # :
PRO-581Price :
Quantity :
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Shipped at Room temp
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Description
HMG1 Human Recombinant fused with 6X His tag produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 223 amino acids and having a molecular mass of 26 kDa.The HMGB-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HMG1 (1mg/ml) was lyophilized after extensive dialyses against 1x PBS pH-7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
High-mobility group box 1 protein (HMGB1), previously known as HMG-1 or amphoterin, is a member of the high mobility group box family of non-histone chromosomal proteins. Human HMGB1 is expressed as a 30 kDa, 215 amino acid (aa) single chain polypeptide containing three domains: two N-terminal globular, 70 aa positively charged DNA-binding domains (HMG boxes A and B), and a negatively charged 30 aa C-terminal region that contains only Asp and Glu.4, 5 Residues 27 - 43 and 178 - 184 contain a NLS. Posttranslational modifications of the molecule have been reported, with acetylation occurring on as many as 17 lysine residues. HMGB1 is expressed at high levels in almost all cells. It was originally discovered as a nuclear protein that could bend DNA. Such bending stabilizes nucleosome formation and regulates the expression of select genes upon recruitment by DNA binding proteins.
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Synonyms
HMG1, HMG3, SBP-1, Amphoterin, HMGB1, High-Mobility Group Box 1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized HMGB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HMGB1 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 HMGB1 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
MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERW
KTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPS
AFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLK
EKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEEDEEDEEDEEEEEDEED
EDEEEDDDDELEHHHHHH
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 :
Troponin C-I-T HumanDescription:
Cardiac Troponin C-I-T Complex Human Recombinant
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817, Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
Product # :
PRO-344Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant Human Cardiac Troponin C-I-T complex produced in E.Coli is a single, non-glycosylated, polypeptide chain having the Molar ratio on cTnC to cTnI to cTnT of 1:1:1. Mw is approximately 90kDa.The Cardiac Troponin C-I-T complex is purified by proprietary chromatographic techniques
Source
Escherichia Coli.
Formulation
Human Cardiac Troponin C-I-T complex solution contains 500 mM NaCl, 20mM Tris-HCl, 4mM CaCl2, 4mM MgCl2and 60 mM B-mercaptoethanol, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Synonyms
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817, Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
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Physical Appearance
Sterile Filtered colourless liquid formualtion.
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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.
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Name :
Prelamin-ADescription:
Prelamin-A Recombinant
Prelamin-A/C, LMNA, LMN1, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.
Product # :
PRO-689Price :
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Shipped with Ice Packs
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Description
Recombinant Prelamin-A is a 74kDa precursor of the nuclear lamin A protein. Prelamin-A is a structural component of the nuclear lamina and it is encoded by lamin A/C gene (LMNA). Due to the presence of a CAAX box sequence at carboxyl terminus, Prelamin-A in vivo goes through a serial of post-translational modifications, resulting in the farnesylation of the cysteine thiol, removal of the AAX tripeptide, carboxyl-methylation of the cysteinyl carboxy group and proteolysis of 18 C-terminal amino acids residues that lead to mature lamin A. Diverse mutations in the lamin A/C gene are associated with different deseases that are collectively called laminophaties, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome. Recombinant human prelamin A is fused to a 6 Histidine tag at the N-terminus.
Source
Escherichia Coli.
Formulation
The Prelamin-A solution (0.1mg/ml) contains 10% Glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Synonyms
Prelamin-A/C, LMNA, LMN1, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.
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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
HHHHHH-METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVHSLETENAGLRLRITES
EEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQA
RLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRL
QTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKE
LEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLA
RERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSP
TSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRN
KSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNT
WGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRS
RTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRSYL
LGNSSPRTQSPQNCSIM
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 :
p59-Fyn HumanDescription:
p59-Fyn Human Recombinant
Proto-oncogene tyrosine-protein kinase Fyn, EC 2.7.10.2, p59-Fyn, Protooncogene Syn, SLK, FYN, MGC45350, Fyn p59.
Product # :
PRO-506Price :
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Shipped with Ice Packs
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Description
p59-Fyn Human Recombinant (a.a. 23-216) expressed in E.coli, shows a 50 kDa SDS-PAGE (Including GST tag).The p59-Fyn is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
p59-Fyn in 50mM Tris-Acetate, pH7.5, 1mM EDTA and 20% Glycerol.
Citations
More Info
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Introduction
p59-Fyn is a member of the protein-tyrosine kinase oncogene family. p59fyn is a membrane-associated non-receptor protein tyrosine kinase that belongs to the Src-family of kinases. p59-Fyn encodes a membrane-associated tyrosine kinase which is implicated in the control of cell growth. p59-Fyn associates with the p85 subunit of phosphatidylinositol 3-kinase and interacts with the fyn-binding protein. The unique N-terminal domain of p59fyn interacts with the CD3 and eta chains of the TcR. p59fyn can bind other proteins (p82 and p116) through its SH2 and SH3 domains, which may act as substrates or regulators of fyn activity. p59fyn is highly expressed in brain suggesting that it may have a role in the sensory nervous network and in myelination at early stages of CNS formation. Distinct isoforms exist due to alternative splicing.
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Synonyms
Proto-oncogene tyrosine-protein kinase Fyn, EC 2.7.10.2, p59-Fyn, Protooncogene Syn, SLK, FYN, MGC45350, Fyn p59.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.
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Applications
• ELISA
• Inhibition Assays
• Western Blotting.
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 :
Leptin-B TilapiaDescription:
Leptin-B Tilapia Recombinant
Product # :
CYT-1110Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin-B Tilapia Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids and having a molecular mass of 15,243 Dalton. The Leptin-B Tilapia is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing NaHCO3 at 1:2 salt: protein ratio.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Tilapia leptins were found to be biologically active in promoting proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor, but their activity was lower than that of mammalian leptin. Furthermore, the Tilapia leptins were biologically active in promoting STAT‐LUC activation in COS7 cells transfected with Tilapia leptin receptor but not in cells transfected with human leptin receptor. Tilapia Leptin A was more active than Tilapia Leptin B.
Citations
More Info
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Introduction
Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin-B Tilapia although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin-B Tilapia 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 Leptin-B Tilapia 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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Amino Acid Sequence
The first six N-terminal amino acids of recombinant Tilapia leptin B are Ala-Leu-Leu-Thr-Lys-Gly.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.19 for 1 mg/ml Leptin-B Tilapia as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.
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 :
SPG21 HumanDescription:
Spastic Paraplegia 21 Human Recombinant
MAST, ACP33, GL010, BM-019, MASPARDIN, SPG21, Spastic paraplegia 21 autosomal recessive Mast syndrome protein, Acid cluster protein 33.
Product # :
PRO-677Price :
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Description
SPG21 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 328 amino acids (1-308 a.a.) and having a molecular mass of 94.4 kDa.SPG21 is expressed with a 20 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SPG21 protein solution contains 20mM Tris-HCl, pH-8.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SPG21 binds to the hydrophobic C-terminal amino acids of CD4 which take part in suppression of CD-4 dependant T cell activation. The interaction with CD4 is mediated by the noncatalytic alpha/beta hydrolase fold domain. SPG21 adapts the stimulatory activity of CD4. SPG21 is broadly expressed in diverse tissues including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Mutations in SPG21 cause Mast syndrome, an autosomal-recessive complicated form of hereditary spastic paraplegia characterized by dementia, thin corpus callosum and white matter abnormalities.
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Synonyms
MAST, ACP33, GL010, BM-019, MASPARDIN, SPG21, Spastic paraplegia 21 autosomal recessive Mast syndrome protein, Acid cluster protein 33.
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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 MGEIKVSPDY NWFRGTVPLK KIIVDDDDSK IWSLYDAGPR SIRCPLIFLP PVSGTADVFF RQILALTGWG YRVIALQYPV YWDHLEFCDG FRKLLDHLQL DKVHLFGASL GGFLAQKFAE YTHKSPRVHS LILCNSFSDT SIFNQTWTAN SFWLMPAFML KKIVLGNFSS GPVDPMMADA IDFMVDRLES LGQSELASRL TLNCQNSYVE PHKIRDIPVT IMDVFDQSAL STEAKEEMYK LYPNARRAHL KTGGNFPYLC RSAEVNLYVQ IHLLQFHGTK YAAIDPSMVS AEELEVQKGS LGISQEEQ.
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 :
SERPINA3Description:
Alpha-1 AntiChymotrypsin Human Recombinant
Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.
Product # :
PRO-750Price :
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Shipping Method :
Shipped with Ice Packs
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Description
SERPINA3 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 421 amino acids (24-423 a.a.) and having a molecular mass of 47.6 kDa.The SERPINA3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SERPINA3 solution contains 20mM Tris-HCl buffer pH-8, 1mM DTT, and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Alpha 1 ACT is an early-stage acute-phase plasma protein and a serpin that preferentially inactivates chymotrypsin, cathepsin G, and chymase. Alpha-1-ACT, a serine protease inhibitor, is tightly associated with amyloid plaques in Alzheimer's disease (AD) and in normal aged human and monkey brain.
Regulation of the serine proteases and serine protease inhibitors plays an important role in neuromuscular differentiation. Prostate specific antigen (PSA), a chymotrypsin-like serine protease, is predominantly complexed to Alpha-1-ACT. -
Synonyms
Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.
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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 MHPNSPLDEE NLTQENQDRG THVDLGLASA NVDFAFSLYK QLVLKAPDKN VIFSPLSIST ALAFLSLGAH NTTLTEILKG LKFNLTETSE AEIHQSFQHL LRTLNQSSDE LQLSMGNAMF VKEQLSLLDR FTEDAKRLYG SEAFATDFQD SAAAKKLIND YVKNGTRGKI TDLIKDLDSQ TMMVLVNYIF FKAKWEMPFD PQDTHQSRFY LSKKKWVMVP MMSLHHLTIP YFRDEELSCT VVELKYTGNA SALFILPDQD KMEEVEAMLL PETLKRWRDS LEFREIGELY LPKFSISRDY NLNDILLQLG IEEAFTSKAD LSGITGARNL AVSQVVHKAV LDVFEEGTEA SAATAVKITL LSALVETRTI VRFNRPFLMI IVPTDTQNIF FMSKVTNPKQ A.
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 :
NIP7 HumanDescription:
Nuclear Import 7 Homolog Human Recombinant
Nuclear Import 7 Homolog, 60S ribosome subunit biogenesis protein NIP7 homolog KD93, CGI-37, HSPC031, FLJ10296, NIP7.
Product # :
PRO-780Price :
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Description
NIP7 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-180 a.a.) and having a molecular mass of 21.5kDa. NIP7 is fused to 8 amino acids His Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NIP7 protein solution contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
60S ribosome subunit biogenesis protein NIP7 homolog (NIP7) belongs to NIP7 family and contains 1 PUA domain. NIP7 interacts with pre-ribosome complex and may bind to RNA. NIP7 is vital for proper 27S pre-rRNA processing and 60S ribosome subunit assembly.
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Synonyms
Nuclear Import 7 Homolog, 60S ribosome subunit biogenesis protein NIP7 homolog KD93, CGI-37, HSPC031, FLJ10296, NIP7.
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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
MRPLTEEETR VMFEKIAKYI GENLQLLVDR PDGTYCFRLH NDRVYYVSEK IMKLAANISG DKLVSLGTCFGKFTKTHKFR LHVTALDYLA PYAKYKVWIK PGAEQSFLYG NHVLKSGLGR ITENTSQYQG VVVYSMADIPLGFGVAAKST QDCRKVDPMA IVVFHQADIG EYVRHEETLT 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 :
BAG1 HumanDescription:
BCL2-Associated Athanogene 1 Human Recombinant
BAG-1, Bcl-2-associated athanogene 1, RAP46, Bcl-2-binding protein, HAP.
Product # :
PRO-817Price :
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Description
BAG1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 230 amino acids (1-230 a.a.) and having a molecular mass of 25.9 kDa. BAG1 protein is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
BAG1 Human solution containing 20mM Tris-HCl pH-7.5, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
BAG1 binds to BCL2 and is also called BCL2-associated athanogene. BAG1 increases the anti-apoptotic effects of BCL2 and is characterizes as a link between growth factor receptors and anti-apoptotic mechanisms. BAG1 inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. BAG1 inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. BAG1 enhances the anti-cell death function of BCL2 induced by various stimuli.
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Synonyms
BAG-1, Bcl-2-associated athanogene 1, RAP46, Bcl-2-binding protein, HAP.
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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
MNRSQEVTRD EESTRSEEVT REEMAAAGLT VTVTHSNEKH DLHVTSQQGS SEPVVQDLAQ VVEEVIGVPQ SFQKLIFKGK SLKEMETPLS ALGIQDGCRV MLIGKKNSPQ EEVELKKLKH LEKSVEKIAD QLEELNKELT GIQQGFLPKD LQAEALCKLD RRVKATIEQF MKILEEIDTL ILPENFKDSR LKRKGLVKKV QAFLAECDTV EQNICQETER LQSTNFALAE.
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 :
CDC34 HumanDescription:
Cell Division Cycle 34 Human Recombinant
UB2R1, CDC-34, Ubiquitin-conjugating enzyme E2 R1, Ubiquitin-protein ligase R1, Ubiquitin-conjugating enzyme E2-32 kDa complementing, E2-CDC34, CDC34, EC 6.3.2.19, UBC3, UBE2R1.
Product # :
ENZ-1103Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
Cell Division Cycle 34 Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 236 amino acids and having a molecular mass of 26.7kDa. CDC34 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CDC34 is supplied as a 0.2 μm filtered solution conteining 50mM HEPES, pH 7.0, 10 % Glycerol, 125mM NaCl, , 5 % Trehalose and 1 mM DTT.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
CDC34 takes part in the control of cell cycle and DNA replication. Cdc34 in association with different E3 complexes, including SCF, targets many different substrates for ubiquitination and degradation during cell division, signal transduction, and development. Cdc34 substrates that have been characterized include B-Myb, Wee1, MyoD, ATF5, p27Xic1, and p27Kip1. Additionally, substrates such as p21Cip1, E2F, cyclin E, and cyclin D are putative substrates of Cdc34 by virtue of their SCF requirement for proteolysis. Cdc34 is self-associate through a domain in the C-terminus, and is phosphorylated and ubiquitinylated in vivo. CDC34is useful for in vitro ubiquitinylation reactions.
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Synonyms
UB2R1, CDC-34, Ubiquitin-conjugating enzyme E2 R1, Ubiquitin-protein ligase R1, Ubiquitin-conjugating enzyme E2-32 kDa complementing, E2-CDC34, CDC34, EC 6.3.2.19, UBC3, UBE2R1.
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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
MARPLVPSSQ KALLLELKGL QEEPVEGFRV TLVDEGDLYN WEVAIFGPPN TYYEGGYFKA RLKFPIDYPY SPPAFRFLTK MWHPNIYETG DVCISILHPP VDDPQSGELP SERWNPTQNV RTILLSVISL LNEPNTFSPA NVDASVMYRK WKESKGKDRE YTDIIRKQVL GTKVDAERDG VKVPTTLAEY CVKTKAPAPD EGSDLFYDDY YEDGEVEEEA DSCFGDDEDD SGTEES.
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 :
Avidin ProteinDescription:
Avidin
Avidin, AVD, AVID.
Product # :
PRO-500Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- biological activity
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Description
Avidin is a glycosylated polypeptide chain having a molecular mass of 68kDa and containing 4 subunits each with a binding site for biotin. The Avidin is purified by affinity chromatographic techniques.The purification procedure ensures minimal contamination by other proteins or DNA.The resulting high activity and purity of the product gives very low non-specific binding (NSB).
Source
Hen's egg white.
Biological Activity
15.0 units/mg protein, 1 unit binds 1µg biotin.
Citations
More Info
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Introduction
Avidin is a tetrameric protein of 4 identical subunits (homotetramer) each of which can bind to biotin with a high degree of affinity and specificity. Avidin molecular weight in its tetrameric form is estimated to be between 66-69 kDa. Avidin is produced in the oviducts of birds, reptiles and amphibians and is subsequently deposited in the whites of their eggs. In the chicken egg white, avidin makes up roughly 0.05% of total protein (approximately 1.8 mg per egg). 10% of Avidin’s molecular weight is ascribed to carbohydrate content which is composed of four to five mannose and three N-acetylglucosamine residues. Avidin has at least three distinctive oligosaccharide structural type which are similar in structure and composition. The dissociation constant (KD) of avidin is approximately 10-15M, making it one of the strongest known non-covalent bonds.
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Synonyms
Avidin, AVD, AVID.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Lyophilized Avidin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Avidin 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 Avidin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml 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.
- View Data Sheet
Name :
SERPINH1 HumanDescription:
Heat Shock 47kDa Human Recombinant
HSP47, HSP-47, Colligin-1, CBP1, Collagen Binding Protein-1, Serpin Peptidase Inhibitor Clade-H memebr 1, Serpin H1, Collagen-binding protein, Colligin, 47 kDa heat shock protein, Rheumatoid arthritis-related antigen RA-A47, Arsenic-transactivated protein 3, AsTP3, Cell proliferation-inducing gene 14 protein, SERPINH1, CBP2, gp46, PIG14, PPROM, RA-A47, SERPINH2.
Product # :
HSP-047Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human HSP47 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (18-418 a.a.) and having a molecular mass of 48.9 kDa. HSP47 human recombinant is fused to a 38 amino acid His Tag at N-terminus and purified by convential chromatogrpahy techniques.
Source
Escherichia Coli.
Formulation
The SERPINH1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SERPINH1 is part of the serpin superfamily of serine proteinase inhibitors. SEPINH1 expression is induced by heat shock. HSP47 localizes to the endoplasmic reticulum lumen and binds collagen therefore it is a molecular chaperone which takes part in the maturation of collagen molecules, facilitating the folding and assembly of procollagen molecules, retaining unfolded molecules within the ER, and assisting the transport of correctly folded-molecules from the ER to Golgi apparatus. Autoantibodies to HSP47 protein have been found in rheumatoid arthritis. SERPINH1 binds specifically to collagen and acts as a chaperone in the biosynthetic pathway of collagen.
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Synonyms
HSP47, HSP-47, Colligin-1, CBP1, Collagen Binding Protein-1, Serpin Peptidase Inhibitor Clade-H memebr 1, Serpin H1, Collagen-binding protein, Colligin, 47 kDa heat shock protein, Rheumatoid arthritis-related antigen RA-A47, Arsenic-transactivated protein 3, AsTP3, Cell proliferation-inducing gene 14 protein, SERPINH1, CBP2, gp46, PIG14, PPROM, RA-A47, SERPINH2.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAA EVKKPAAAAA PGTAEKLSPK AATLAERSAG LAFSLYQAMA KDQAVENILV SPVVVASSLG LVSLGGKATT ASQAKAVLSA EQLRDEEVHA GLGELLRSLS NSTARNVTWK LGSRLYGPSS VSFADDFVRS SKQHYNCEHS KINFRDKRSA LQSINEWAAQ TTDGKLPEVT KDVERTDGAL LVNAMFFKPH WDEKFHHKMV DNRGFMVTRS YTVGVMMMHR TGLYNYYDDE KEKLQIVEMP LAHKLSSLII LMPHHVEPLE RLEKLLTKEQ LKIWMGKMQK KAVAISLPKG VVEVTHDLQK HLAGLGLTEA IDKNKADLSR MSGKKDLYLA SVFHATAFEL DTDGNPFDQD IYGREELRSP KLFYADHPFI FLVRDTQSGS LLFIGRLVRP KGDKMRDEL.
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 :
PDK1 HumanDescription:
Pyruvate Dehydrogenase Kinase Isozyme 1 Human Recombinant
Pyruvate dehydrogenase kinase isoform 1, PDK1, Pyruvate dehydrogenase (lipoamide) kinase isozyme 1 mitochondrial.
Product # :
PKA-263Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PDK1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 429 amino acids (29-436) and having a molecular mass of 48.6 kDa. PDK1 is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PDK1 solution containing 20mM Tris pH-7, 0.5mM DTT, 0.1M NaCl, 0.1mM EDTA 0.1mM PMSF, 1mM MgCl2 and 40% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
PDK1 takes part in the regulation of enzymatic activity of mammalian pyruvate dehydrogenase which is part of a mitochondrial multienzyme complex to catalyze the oxidative decarboxylation of pyruvate and is one of the major enzymes responsible for the regulation of homeostasis of carbohydrate fuels in mammals. PDK1 inhibits glioblastoma growth. PDK1 inhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the e1 alpha subunit, therefore contributing to the regulation of glucose metabolism. PDK1 kinase activity is negatively regulated by binding to 14-3-3.
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Synonyms
Pyruvate dehydrogenase kinase isoform 1, PDK1, Pyruvate dehydrogenase (lipoamide) kinase isozyme 1 mitochondrial.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
PDK1 Human Recombinant 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
MGSSHHHHHH SSGLVPRGSH MSSDSGSSPA SERGVPGQVD FYARFSPSPL SMKQFLDFGS VNACEKTSFM FLRQELPVRL ANIMKEISLLPDNLLRTPSV QLVQSWYIQS LQELLDFKDK SAEDAKAIYD FTDTVIRIRN RHNDVIPTMA QGVIEYKESF GVDPVTSQNV QYFLDRFYMS RISIRMLLNQ HSLLFGGKGK GSPSHRKHIG SINPNCNVLE VIKDGYENAR RLCDLYYINS PELELEELNA KSPGQPIQVV YVPSHLYHMVFELFKNAMRA TMEHHANRGV YPPIQVHVTL GNEDLTVKMS DRGGGVPLRK IDRLFNYMYS TAPRPRVETS RAVPLAGFGY GLPISRLYAQ YFQGDLKLYS LEGYGTDAVI YIKALSTDSI ERLPVYNKAA WKHYNTNHEA DDWCVPSREP KDMTTFRSA.
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 :
Mouse OX40LDescription:
OX40 Ligand Mouse Recombinant
Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l
Product # :
CYT-1191Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
OX40L Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 157 amino acids (51-198 aa) and having a molecular mass of 17.7kDa.OX40L is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The OX40L solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Determined by its binding ability in a functional ELISA with Human TNFRSF4 (CAT# cyt-1039).
Citations
More Info
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Introduction
OX40 Ligandis a part of the tumor necrosis factor (TNF)receptor family. OX40L receptor is OX40 which is expressed predominantly on activated CD4+ T cells.OX40 Ligandis expressed on various antigen-presenting cells such asmacrophages, DC2sand activated Blymphocytes. Expression of OX40 is momentary following engagement of T cell receptors. The ligation of OX40-OX40L stimulates proliferation anddifferentiation of activated B cells,increases immunoglobulin secretion and is also a sourceof survival signal for T cells and enables the development of memory T cells.
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Synonyms
Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l
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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
ADPSSSPAKD PPIQRLRGAV TRCEDGQLFI SSYKNEYQTM EVQNNSVVIK CDGLYIIYLK GSFFQEVKID LHFREDHNPI SIPMLNDGRR IVFTVVASLA FKDKVYLTVN APDTLCEHLQ INDGELIVVQ LTPGYCAPEG SYHSTVNQVP LHHHHHH
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 :
Parathormone (1-84) HumanDescription:
Parathyroid Hormone (1-84) Human Recombinant
Parathyrin, PTH, Parathormone.
Product # :
HOR-263Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- sds-page
- Citations
Description
Parathyroid Hormone 1-84 (full length) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 84 amino acids, having an MW of ~9.4kDa.The PTH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS pH7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is calculated by its ability to induce cAMP accumulation in murine MC3T3E1 cells and is <50ng/ml, corresponding to a specific activity of greater than 2.0 x 104 Units/mg.
sds-page
Citations
More Info
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Introduction
Parathyroid hormone (PTH), or parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calciumin the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. PTH acts to increase the concentration of calcium in the blood by acting upon parathyroid hormone receptorin three parts of the body: In the bones- It enhances the release of calcium from the large reservoir contained in the bones. Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL, which can bind to osteoclast precursors containing RANK, a receptor for RANKL. The binding of RANKL to RANK stimulates these precursors to fuse, forming new osteoclasts which ultimately enhances the resorption of bone.
In the kidney- It enhances active reabsorption of calcium from distal tubules and the thick ascending limb.
In the intestine- It enhances the absorption of calcium in the intestine by increasing the production of vitamin D and upregulating the enzyme responsible for 1-alpha hydroxylationof 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D) which effects the actual absorption of calcium (as Ca2+ ions) by the intestine via calbindin.
Recombinant Human full length PTH 1-84 has potential as an anti-osteoporotic agent, due to its properties as a bone formation stimulant, it increases bone turnover, stimulating osteoblasts and reducing both vertebral and non vertebral fractures. -
Synonyms
Parathyrin, PTH, Parathormone.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Parathyrin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PTH 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 Parathormone 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
SVSEIQLMHN LGKHLNSMER VEWLRKKLQD VHNFVALGAP LAPRDAGSQR PRKKEDNVLV ESHEKSLGEA DKADVNVLTK AKSQ.
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Background
What is the molecular weight/Mw of PARATHORMONE (1-84) HUMAN Protein?
PARATHORMONE (1-84) HUMAN Protein has a total Mw of 9.4kDa.
What is the source or expression system of PARATHORMONE (1-84) HUMAN Protein?
Escherichia Coli.
What is the Purity of PARATHORMONE (1-84) HUMAN Protein?
PARATHORMONE (1-84) HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of PARATHORMONE (1-84) HUMAN Protein?
The activity is calculated by its ability to induce cAMP accumulation in murine MC3T3E1 cells and is <50ng/ml, corresponding to a specific activity of greater than 2.0 x 104 Units/mg.
What is the amino acid sequence of PARATHORMONE (1-84) HUMAN Protein?
SVSEIQLMHN LGKHLNSMER VEWLRKKLQD VHNFVALGAP LAPRDAGSQR PRKKEDNVLV ESHEKSLGEA DKADVNVLTK AKSQ.
What applications can PARATHORMONE (1-84) HUMAN Protein be used in?
PARATHORMONE (1-84) HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for PARATHORMONE (1-84) HUMAN Protein?
The endotoxin level is minimal, PARATHORMONE (1-84) HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant PARATHORMONE (1-84) HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of PARATHORMONE (1-84) HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
SNCB HumanDescription:
Beta-Synuclein Human Recombinant
Beta-synuclein, SNCB, b-Synuclein.
Product # :
PRO-394Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human b-Synuclein produced in E.Coli is a single, non-glycosylated polypeptide chain (1-134 a.a) having a molecular mass of 14.2kDa (molecular size on SDS-PAGE will appear higher).
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.1M NaCl and 1mM MgCl2.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
b-synuclein (amino acids 1-134), an acidic neuronal protein of 134 amino acids, is extremely heat-resistant. b-synucelin also has a chaperone-like activity. Recently, b-synuclein has been suggested to inhibit a-synuclein aggregation. b and a-synuclein are abundantly expressed in the brain and putatively inhibit phospholipase D2 selectively. The encoded protein, which may play a role in neuronal plasticity, is abundant in neurofibrillary lesions of patients with Alzheimer disease.
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Synonyms
Beta-synuclein, SNCB, b-Synuclein.
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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
MDVFMKGLSM AKEGVVAAAE KTKQGVTEAA EKTKEGVLYV GSKTREGVVQ GVASVAEKTK EQASHLGGAV FSGAGNIAAA TGLVKREEFP TDLKPEEVAQ EAAEEPLIEP LMEPEGESYE DPPQEEYQEY EPEA.
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 :
T.gondii p40Description:
Toxoplasma Gondii p40 Recombinant
Product # :
TOX-268Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The E.Coli derived recombinant Toxoplasma Gondii p40 having a Mw of 35kDa and fused to a 6 His tag at C-terminus can be used to test the specific IgG and IgM antibody for the diagnosis of Toxoplasma gondii infection.
Source
Escherichia Coli.
Formulation
1x PBS and 25mM arginine.
Purity
Toxoplasma protein is >95% pure as determined by 10% PAGE (coomassie staining).
Citations
More Info
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Introduction
The life cycle of Toxoplasma gondii has two phases. The coccidia like takes place only in members of the Felidae family which makes these animals the parasite's primary host. The asexual part of the life cycle can take place in any warm-blooded animal, like other mammals(including felines) and birds. T. gondii constructing daughter scaffolds within the mother cell. In the intermediate hosts (including felines), the parasite invades cells, forming intracellular so-called parasitophorous vacuoles containing bradyzoites, the slowly replicating form of the parasit. Vacuoles form tissue cysts mainly within the muscles and brain. Since they are within cells, the host's immune system does not detect these cysts. Resistance to antibiotics varies, but the cysts are very difficult to eradicate entirely. Within these vacuoles T. gondii propagates by a series of binary fissions until the infected cell eventually bursts and tachyzoites are released. Tachyzoites are the motile, asexually reproducing form of the parasite. Unlike the bradyzoites, the free tachyzoites are usually efficiently cleared by the host's immune response, although some manage to infect cells and form bradyzoites, thus maintaining the infection.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
T.gondii p40 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Purification Method
Purified by proprietary chromatographic technique.
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 :
Prolactin RatDescription:
Prolactin Rat Recombinant
Mammotropin, Luterotropic hormone, Lutetropin, PRL.
Product # :
CYT-322Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Prolactin Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids and having a molecular mass of 22.6 kDa. The Prolactin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 10mM sodium Phosphate buffer pH=8 and 50mM Nacl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of the proliferation of rat lymphoma, Nb2-11 was found to be < 0.065 ng/ml corresponding to a specific activity of 15,400,000 Units/mg.Citations
More Info
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Introduction
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.
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Synonyms
Mammotropin, Luterotropic hormone, Lutetropin, PRL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Prolactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prolactin 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 Prolactin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Pro-Val-Cys.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
YWHAB HumanDescription:
Tyr-3/Trp- 5 Monooxygenase Activation Protein Beta Human Recombinant
14-3-3 protein beta/alpha, Protein kinase C inhibitor protein 1, Protein 1054, YWHAB, HS1, GW128, KCIP-1, Tyr-3/Trp- 5 Monooxygenase Activation Protein Beta, 14-3-3 Beta.
Product # :
PKA-348Price :
Quantity :
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Shipped with Ice Packs
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Description
YWHAB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 246 amino acids (1-246) and having a molecular mass of 28kDa. YWHAB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The YWHAB protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM EDTA & 50mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
YWHAB belongs to the 14-3-3 family of proteins which are in charge for signal transduction by binding to phosphoserine-containing proteins. YWHAB is found in both plants and mammals. YWHAB protein interacts with RAF1 and CDC25 phosphatases,thus linking mitogenic signaling and the cell cycle machinery. YWHAB is an adapter protein involved in the regulation of a large spectrum of both general and specialized signaling pathway. YWHAB binds to a large number of proteins by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.
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Synonyms
14-3-3 protein beta/alpha, Protein kinase C inhibitor protein 1, Protein 1054, YWHAB, HS1, GW128, KCIP-1, Tyr-3/Trp- 5 Monooxygenase Activation Protein Beta, 14-3-3 Beta.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL ELLDKYLIPN ATQPESKVFY LKMKGDYFRY LSEVASGDNK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD
AGEGEN.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GDF15 MouseDescription:
Growth and Differentiation factor 15 Mouse Recombinant
Growth/differentiation factor 15, GDF-15.
Product # :
CYT-857Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
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- sds-page
- Citations
Description
GDF15 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (189-303 a.a) and having a molecular mass of 14.9kDa. GDF15 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDF15 protein solution (1.0mg/ml) containing 20mM Phosphate buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
Citations
More Info
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Introduction
GDF15 is part of the TGF-Beta superfamily which is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.
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Synonyms
Growth/differentiation factor 15, GDF-15.
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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 MGSSAHAHPR DSCPLGPGRC CHLETVQATL EDLGWSDWVL SPRQLQLSMC VGECPHLYRS ANTHAQIKAR LHGLQPDKVP APCCVPSSYT PVVLMHRTDS GVSLQTYDDL VARGCHCA.
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Background
What is the molecular weight/Mw of GDF15 MOUSE Protein?
GDF15 MOUSE Protein has a total Mw of 14.9kDa.
What is the source or expression system of GDF15 MOUSE Protein?
Escherichia Coli.
What is the Purity of GDF15 MOUSE Protein?
GDF15 MOUSE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF15 MOUSE Protein?
The biological functionality of GDF15 MOUSE Protein will be determined in the future.
What is the amino acid sequence of GDF15 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSSAHAHPR DSCPLGPGRC CHLETVQATL EDLGWSDWVL SPRQLQLSMC VGECPHLYRS ANTHAQIKAR LHGLQPDKVP APCCVPSSYT PVVLMHRTDS GVSLQTYDDL VARGCHCA.
What applications can GDF15 MOUSE Protein be used in?
GDF15 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF15 MOUSE Protein?
The endotoxin level is minimal, GDF15 MOUSE 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 :
CCL26 HumanDescription:
Eotaxin-3 Human Recombinant (CCL26)
C-C motif chemokine 26, Small-inducible cytokine A26, Eotaxin-3, Macrophage inflammatory protein 4-alpha, MIP-4-alpha, Thymic stroma chemokine-1, TSC-1, CC chemokine IMAC, CCL26, SCYA26, IMAC, MIP-4a, MGC126714, MIP-4alpha.
Product # :
CHM-362Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- formulation
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- biological activity
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- SDS-PAGE
- Citations
Description
Eotaxin-3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 71 amino acids and having a molecular mass of 8.4kDa. The Eotaxin-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.
Biological Activity
Determined by its ability to chemoattract BaF3 mouse pro-B cells transfected with mouse CCR3. The ED50 for this effect is typically 0.1-1.0 μg/ml.
SDS-PAGE
Citations
More Info
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Introduction
Eotaxin-3 (CCL26) is a small cytokine that belongs to the CC chemokine family also known as TARC (thymus and activation regulated chemokine). CCL26 is major eotaxin produced and released by alveolar epithelial cells which is involved in autoregulation of CCR3 receptors and other eotaxins. Eotaxin-3 is involved in immunoregulatory and inflammatory processes. Eotaxin-3 specifically binds and stimulates chemotaxis in T cells and elicits its effects by interacting with the chemokine receptor CCR4. CCL26 exhibits chemotactic activity for normal peripheral blood eosinophils and basophils. Eotaxin-3 may play a part in the eosinophil accumulation in atopic diseases. Eotaxin-3 is overexpressed in eosinophilic esophagitis, and the expression level correlates with disease severity. Eotaxin-3 is expressed constitutively in thymus, but only briefly in phytohemagglutinin-stimulated peripheral blood mononuclear cells. CCL26 is one of two Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 7.
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Synonyms
C-C motif chemokine 26, Small-inducible cytokine A26, Eotaxin-3, Macrophage inflammatory protein 4-alpha, MIP-4-alpha, Thymic stroma chemokine-1, TSC-1, CC chemokine IMAC, CCL26, SCYA26, IMAC, MIP-4a, MGC126714, MIP-4alpha.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Eotaxin-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL26 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 Eotaxin-3 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
TRGSDISKTC CFQYSHKPLP WTWVRSYEFT SNSCSQRAVI FTTKRGKKVC THPRKKWVQK YISLLKTPKQ L.
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Background
What is the molecular weight/Mw of CCL26 HUMAN Protein?
CCL26 HUMAN Protein has a total Mw of 8.4kDa.
What is the source or expression system of CCL26 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL26 HUMAN Protein?
CCL26 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL26 HUMAN Protein?
Determined by its ability to chemoattract BaF3 mouse pro-B cells transfected with mouse CCR3. The ED50 for this effect is typically 0.1-1.0 μg/ml.
What is the amino acid sequence of CCL26 HUMAN Protein?
TRGSDISKTC CFQYSHKPLP WTWVRSYEFT SNSCSQRAVI FTTKRGKKVC THPRKKWVQK YISLLKTPKQ L.
What applications can CCL26 HUMAN Protein be used in?
CCL26 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL26 HUMAN Protein?
The endotoxin level is minimal, CCL26 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL26 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CCL26 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
CALB1 HumanDescription:
Calbindin-1 Human Recombinant
Calbindin, Vitamin D-dependent calcium-binding protein, avian-type, Calbindin D28, D-28K, CALB1, CAB27, CALB, calbindin 1 28kDa.
Product # :
PRO-721Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
CALB1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 261 amino acids (1-261 a.a.) and having a molecular mass of 30kDa.The CALB1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CALB1 protein solution contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 10% glycerol and 2mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Calbindin 1 (CALB1) is a calcium binding protein that is a member of the troponin C superfamily. CALB1 plays a vital role in calcium regulation (including calcium transport and uptake, calcification of bone and teeth) and calcium associated signaling in neurons and transiently in embryological development. CALB1 also has a role in protecting neurons from apoptotic cell death. CALB1 buffers cytosolic calcium and may stimulate a membrane Ca2+-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase. The biological function of CALB1 seems to be tied to the redox state of its five cysteine residues.
CALB1 has 4 active calcium-binding domains, and 2 modified domains that seemingly have lost their calcium-binding ability. CALB1 is expressed in neural tissues. In the brain, the CALB1 synthesis is independent of vitamin-D-derived hormones.
Disregulation of the CALB1 is associated with epilepsy, amyotrophic lateral sclerosis, Huntington's disease. The neurons in brains of Huntington disease patients are calbindin-depleted. -
Synonyms
Calbindin, Vitamin D-dependent calcium-binding protein, avian-type, Calbindin D28, D-28K, CALB1, CAB27, CALB, calbindin 1 28kDa.
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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
MAESHLQSSL ITASQFFEIW LHFDADGSGY LEGKELQNLI QELQQARKKA GLELSPEMKT FVDQYGQRDD GKIGIVELAH VLPTEENFLL LFRCQQLKSC EEFMKTWRKY DTDHSGFIET EELKNFLKDL LEKANKTVDD TKLAEYTDLM LKLFDSNNDG KLELTEMARL LPVQENFLLK FQGIKMCGKE FNKAFELYDQ DGNGYIDENE LDALLKDLCE KNKQDLDINN ITTYKKNIMA LSDGGKLYRT DLALILCAGD N.
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.