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1000 results found for “Glypican”
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Name :
HEPACAM2 HumanDescription:
HEPACAM2 Human Recombinant
HEPACAM family member 2 isoform 1, MIKI, HEPACAM family member 2, Mitotic kinetics regulator, HEPACAM2, UNQ305/PRO346.
Product # :
PRO-1672Price :
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Shipped with Ice Packs
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Description
HEPACAM2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (32-351) and having a molecular mass of 37.9 kDa.HEPACAM2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HEPACAM2 solution (1mg/ml) contains 20mM 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
HEPACAM2 is necessary during prometaphase for centrosome maturation. Following poly-ADP-ribosylation (PARsylation) by TNKS, HEPACAM2 translocates from the Golgi apparatus to mitotic centrosomes and takes a significant part in the formation of robust microtubules for quick movement of chromosomes.
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Synonyms
HEPACAM family member 2 isoform 1, MIKI, HEPACAM family member 2, Mitotic kinetics regulator, HEPACAM2, UNQ305/PRO346.
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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 MGSLKVTVPS HTVHGVRGQA LYLPVHYGFH TPASDIQIIW LFERPHTMPK YLLGSVNKSV VPDLEYQHKF TMMPPNASLL INPLQFPDEG NYIVKVNIQG NGTLSASQKI QVTVDDPVTK PVVQIHPPSG AVEYVGNMTL TCHVEGGTRL AYQWLKNGRP VHTSSTYSFS PQNNTLHIAP VTKEDIGNYS CLVRNPVSEM ESDIIMPIIY YGPYGLQVNS DKGLKVGEVF TVDLGEAILF DCSADSHPPN TYSWIRRTDN TTYIIKHGPR LEVASEKVAQ KTMDYVCCAY NNITGRQDET HFTVIITSVG LEKLAQKGKS LSP.
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 :
HIF1A Human, HisDescription:
Hypoxia-Inducible Factor-1 Alpha Human Recombinant, His Tag
Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.
Product # :
PRO-415Price :
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Description
HIF1A Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 231 amino acids (576-785 a.a.) and having a molecular mass of 25.1 kDa. The HIF1A is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HIF1A Human solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.2M NaCl & 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
HIF1A has a role as a master transcriptional monitor of the adaptive response to hypoxia. Under hypoxic conditions HIF1A activates the transcription of over 40 genes, including, erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, and genes whose protein products increase oxygen release or facilitate metabolic adaptation to hypoxia. HIF1A functions as an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease.
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Synonyms
Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.
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Physical Appearance
Sterile filtered colorless solution.
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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 MSFDQLSPLE SSSASPESAS PQSTVTVFQQ TQIQEPTANA TTTTATTDEL KTVTKDRMED IKILIASPSP THIHKETTSA TSSPYRDTQS RTASPNRAGK GVIEQTEKSH PRSPNVLSVA LSQRTTVPEE ELNPKILALQ NAQRKRKMEH DGSLFQAVGI GTLLQQPDDH AATTSLSWKR VKGCKSSEQN GMEQKTIILI PSDLACRLLG Q.
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 :
GDI1 HumanDescription:
GDP Dissociation Inhibitor 1 Human Recombinant
Rab GDP dissociation inhibitor alpha, Rab GDI alpha, GDP Dissociation Inhibitor 1, GDI1, Guanosine diphosphate dissociation inhibitor 1, GDI-1, Oligophrenin-2, XAP-4, GDIL, OPHN2, RABGDIA, XAP4, MRX41, MRX48, 1A, RABGD1A.
Product # :
PRO-2023Price :
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Shipped with Ice Packs
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Description
GDI1 Human Recombinant produced in E. coli is a single polypeptide chain containing 470 amino acids (1-447) and having a molecular mass of 53 kDa.GDI1 is fused to 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GDI1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
GDP Dissociation Inhibitor 1 (GDI1) is expressed mainly in neural and sensory tissues. GDI1 regulates the GDP/GTP exchange reaction of nearly all Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. GDI1 is also promoting the dissociation of GDP-bound Rab proteins from the membrane and inhibits their activation. Mutations in GDI1 have been associated with X-linked nonspecific mental retardation.
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Synonyms
Rab GDP dissociation inhibitor alpha, Rab GDI alpha, GDP Dissociation Inhibitor 1, GDI1, Guanosine diphosphate dissociation inhibitor 1, GDI-1, Oligophrenin-2, XAP-4, GDIL, OPHN2, RABGDIA, XAP4, MRX41, MRX48, 1A, RABGD1A.
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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 MGSMDEEYDV IVLGTGLTEC ILSGIMSVNG KKVLHMDRNP YYGGESSSIT PLEELYKRFQ LLEGPPESMG RGRDWNVDLI PKFLMANGQL VKMLLYTEVT RYLDFKVVEG SFVYKGGKIY KVPSTETEAL ASNLMGMFEK RRFRKFLVFV ANFDENDPKT FEGVDPQTTS MRDVYRKFDL GQDVIDFTGH ALALYRTDDY LDQPCLETVN RIKLYSESLA RYGKSPYLYP LYGLGELPQG FARLSAIYGG TYMLNKPVDD IIMENGKVVG VKSEGEVARC KQLICDPSYI PDRVRKAGQV IRIICILSHP IKNTNDANSC QIIIPQNQVN RKSDIYVCMI SYAHNVAAQG KYIAIASTTV ETTDPEKEVE PALELLEPID QKFVAISDLY EPIDDGCESQ VFCSCSYDAT THFETTCNDI KDIYKRMAGT AFDFENMKRK QNDVFGEAEQ.
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 :
CLPP HumanDescription:
ClpP Caseinolytic Peptidase Human Recombinant
Putative ATP-dependent Clp protease proteolytic subunit mitochondrial, Endopeptidase Clp, CLPP.
Product # :
ENZ-115Price :
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Description
CLPP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (57-277 a.a.) and having a molecular mass of 24.2kDa.CLPP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CLPP solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 7.5), 2mM DTT, 20% glycerol and 100mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ATP-dependent Clp protease proteolytic subunit (CLPP) is a member of the peptidase family S14. CLPP cleaves peptides in a variety of proteins in a manner which requires ATP hydrolysis. CLPP being the catalytic core of the Clp proteolytic complex is commonly involved in many cellular processes via the regulation of intracellular protein quality. CLPP is responsible for a somewhat general and central housekeeping function rather than for the degradation of specific substrates.
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Synonyms
Putative ATP-dependent Clp protease proteolytic subunit mitochondrial, Endopeptidase Clp, CLPP.
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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
MPLIPIVVEQ TGRGERAYDI YSRLLRERIV CVMGPIDDSV ASLVIAQLLF LQSESNKKPI HMYINSPGGV VTAGLAIYDT MQYILNPICT WCVGQAASMG SLLLAAGTPG MRHSLPNSRI MIHQPSGGAR GQATDIAIQA EEIMKLKKQL YNIYAKHTKQ SLQVIESAME RDRYMSPMEA QEFGILDKVL VHPPQDGEDE PTLVQKEPVE AAPAAEPVPA ST.
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 :
Cyclophilin A HumanDescription:
Cyclophilin-A Human Recombinant
Peptidylprolyl isomerase A, CYPA, CYPH, MGC12404, MGC23397, MGC117158, PPIase A, Rotamase A, PPIA, Peptidyl-prolyl cis-trans isomerase A, EC 5.2.1.8, Cyclophilin A, Cyclosporin A-binding protein.
Product # :
ENZ-359Price :
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Shipped with Ice Packs
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Description
Cyclophilin-A 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 185 amino acids (1-165 a.a.) and having a molecular mass of 20 kDa. PPIase-A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1 mg/ml solution containing 20mM Tris-HCl 8.0, 20mM NaCl, 0.5mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 650 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmole of suc-AAFP-PNA per minute at 37°C in Tris-HCl pH8.0 using chymotrypsin.
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Introduction
PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.
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Synonyms
Peptidylprolyl isomerase A, CYPA, CYPH, MGC12404, MGC23397, MGC117158, PPIase A, Rotamase A, PPIA, Peptidyl-prolyl cis-trans isomerase A, EC 5.2.1.8, Cyclophilin A, Cyclosporin A-binding protein.
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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 MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALSTGEKGFGYKG SCFHRIIPGF MCQGGDFTRH NGTGGKSIYG EKFEDENFIL KHTGPGILSMANAGPNTNGS QFFICTAKTE WLDGKHVVFG KVKEGMNIVE AMERFGSRNG KTSKKITIADCGQLE.
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 :
ANXA8 HumanDescription:
Annexin A8 Human Recombinant
ANX8, Annexin-8, Annexin VII, Vascular anticoagulant-beta, VAC-beta.
Product # :
PRO-548Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ANXA8 Human Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 347 amino acids (1-327 a.a.)and having a total molecular mass of 39 kDa. ANXA8 is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ANXA8 1mg/ml protein solution contains 20mM Tris-HCL pH-8, 1mM DTT,1mM EDTA, 0.1M NaCl and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ANXA8 is part of the annexin family of evolutionarily conserved Ca2+ and phospholipid binding proteins. ANXA8 is an anticoagulant protein that functions as an indirect inhibitor of the thromboplastin-specific complex, which takes part in the blood coagulation cascade. Where co-expressed in the same tissues, ANXA8 is expressed at a 100-fold lower level than Annexin A5. Though, ANXA8 is preferentially expressed in acute promyelocytic leukemia (APL) cells which suggests its involvement in hematopoietic cell differentiation.
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Synonyms
ANX8, Annexin-8, Annexin VII, Vascular anticoagulant-beta, VAC-beta.
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Physical Appearance
Sterile Filtered colorless 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. Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAWWKSWIEQ EGVTVKSSSH FNPDPDAETL YKAMKGIGTN EQAIIDVLTK RSNTQRQQIA KSFKAQFGKD
LTETLKSELS GKFERLIVAL MYPPYRYEAK ELHDAMKGLG TKEGVIIEIL ASRTKNQLRE IMKAYEEDYG SSLEEDIQAD TSGYLERILV
CLLQGSRDDV SSFVDPGLAL QDAQDLYAAG EKIRGTDEMK FITILCTRSA THLLRVFEEY EKIANKSIED SIKSETHGSL EEAMLTVVKC
TQNLHSYFAE RLYYAMKGAG TRDGTLIRNI VSRSEIDLNL IKCHFKKMYG KTLSSMIMED TSGDYKNALL SLVGSDP.
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 :
SNAP25 C.elegansDescription:
Synaptosomal-associated protein 25kDa C.elegans Recombinant
Super-Protein, SUP, RIC4, SEC9, SNAP, RIC-4, SNAP25, SNAP-25, Synaptosomal-associated protein 25, Synaptosomal-associated 25 kDa protein, FLJ23079, bA416N4.2, dJ1068F16.2.
Product # :
PRO-396Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant C.elegans SNAP-25 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids and having a molecular mass of 23kDa. SNAP-25 gene was amplified by PCR from C.elegans and cloned into an E. coli expression vector. SNAP-25 was purified by using conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein contains 20mM Tris-HCl pH7.5, 50mM NaCl, 5mM DTT, 1mM EDTA and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Synaptic vesicle membrane docking and fusion is mediated by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) located on the vesicle membrane (v-SNAREs) and the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE complex consists of a bundle of four helices, one of which is supplied by v-SNARE and the other three by t-SNARE. For t-SNAREs on the plasma membrane, the protein syntaxin supplies one helix and the protein encoded by this gene contributes the other two. Therefore, SNAP25 product is a presynaptic plasma membrane protein involved in the regulation of neurotransmitter release. The synaptosomal-associated protein (SNAP-25) is an essential component of the core complex that mediates presynaptic vesicle trafficking. Thus, SNAP-25 is directly involved in the release of neurotransmitters.
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Synonyms
Super-Protein, SUP, RIC4, SEC9, SNAP, RIC-4, SNAP25, SNAP-25, Synaptosomal-associated protein 25, Synaptosomal-associated 25 kDa protein, FLJ23079, bA416N4.2, dJ1068F16.2.
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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
MSGDDDIPEG LEAINLKMNA TTDDSLESTR RMLALCEESK EAGIKTLVML DDQGEQLERCEGALDTINQD MKEAEDHLKG MEKCCGLCVL PWNKTDDFEK TEFAKAWKKD DDGGVISDQPRITVGDSSMG PQGGYITKIT NDAREDEMDE NVQQVSTMVG NLRNMAIDMS TEVSNQNRQL DRIHDKAQSN EVRVESANKR AKNLITK.
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 :
Frataxin HumanDescription:
Frataxin Human Recombinant
FXN, Friedreich ataxia protein, Frataxin mitochondrial, FRDA, X25, FA, CyaY, FARR, MGC57199, Frataxin.
Product # :
PRO-761Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Frataxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 190 amino acids (42-210 a.a.) and having a molecular mass of 21.1 kDa. The Frataxin is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Frataxin solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.5), 1mM DTT, 0.1M NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Frataxin is a mitochondrial iron binding protein that is part of the FRATAXIN family. Frataxin functions in regulating mitochondrial iron transport and respiration. The expansion of intronic trinucleotide repeat GAA results in Friedreich ataxia. Frataxin plays a role in iron homeostasis. Frataxin is an anti-apoptotic protein which prevents mitochondrial damage and reactive oxygen species (ROS) production.
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Synonyms
FXN, Friedreich ataxia protein, Frataxin mitochondrial, FRDA, X25, FA, CyaY, FARR, MGC57199, Frataxin.
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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 MLRTDIDATC TPRRASSNQR GLNQIWNVKK QSVYLMNLRK SGTLGHPGSL DETTYERLAE ETLDSLAEFF EDLADKPYTF EDYDVSFGSG VLTVKLGGDL GTYVINKQTP NKQIWLSSPS SGPKRYDWTG KNWVYSHDGV SLHELLAAEL TKALKTKLDL SSLAYSGKDA.
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 :
CIRBP HumanDescription:
Cold Inducible RNA Binding Protein Human Recombinant
Cold-inducible RNA-binding protein, A18 hnRNP, Glycine-rich RNA-binding protein CIRP, CIRBP, A18HNRNP, CIRP.
Product # :
PRO-746Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CIRBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 192 amino acids (1-172 a.a.) and having a molecular mass of 20.8kDa.CIRBP is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CIRBP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Cold inducible RNA-binding protein (CIRBP) has a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. CIRBP localizes to the nucleus and contains one RRM (RNA recognition motif) domain. Expressed ubiquitously, CIRBP is believed to play a crucial role in the suppression of cellular proliferation in response to UV irradiation or extreme cold.
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Synonyms
Cold-inducible RNA-binding protein, A18 hnRNP, Glycine-rich RNA-binding protein CIRP, CIRBP, A18HNRNP, CIRP.
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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 MASDEGKLFV GGLSFDTNEQ SLEQVFSKYG QISEVVVVKD RETQRSRGFG FVTFENIDDA KDAMMAMNGK SVDGRQIRVD QAGKSSDNRS RGYRGGSAGG RGFFRGGRGR GRGFSRGGGD RGYGGNRFES RSGGYGGSRD YYSSRSQSGG YSDRSSGGSY
RDSYDSYATH NE.
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 :
CLCF1 Human, HisDescription:
Neurotrophin-1 Human Recombinant, His Tag
Cardiotrophin-like cytokine factor 1, B-cell-stimulating factor 3, BSF-3, Novel neurotrophin-1, NNT-1, CLCF1, BSF3, CLC, NNT1, NR6, CISS2.
Product # :
CYT-071Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
CLCF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (28-225 a.a) and having a molecular mass of 24.6kDa.CLCF1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CLCF1 protein solution (1mg/ml) containing 20mM sodium citrate (pH 3.5), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Cardiotrophin-like cytokine factor 1 (CLCF1) is a member of the interleukin 6 family of cytokines, which are involved in cell signaling via phosphorylation of gp130. CLCF1 has a sequence of 225 amino acids with a 27 aa signal peptide, having a molecular mass of 22kDa in the mature form, and the maximum homology to cardiotrophin-1 and ciliary neurotrophic factor. CLCF1 is actively secreted from cells by forming a complex with soluble type I CRLF1 or soluble CNTFR. Defects in the CLCF1 gene cause cold-induced sweating syndrome 2 (CISS2). The CISS2 syndrome is typified by profuse sweating after exposure to cold as well as congenital physical abnormalities of the head and spine.
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Synonyms
Cardiotrophin-like cytokine factor 1, B-cell-stimulating factor 3, BSF-3, Novel neurotrophin-1, NNT-1, CLCF1, BSF3, CLC, NNT1, NR6, CISS2.
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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 MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.
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Background
Cardiotrophin-Like Cytokine Factor 1 Human Recombinant: A Significant Player in Neuronal Development and Immune Regulation
Cardiotrophin-like cytokine factor 1 (CLCF1) has emerged as a crucial player in neuronal development and immune regulation. As a heterodimeric neurotropic cytokine, CLCF1 in complex with cytokine-like factor-1 (CLF-1) has demonstrated vital roles in neuronal development. Studies show that mice lacking this heterodimer exhibit reduced motor neurons and die shortly after birth due to suckling defects. In humans, mutations in the genes encoding for CLCF1 and CLF-1 manifest as Sohar-Crisponi or cold-induced sweating syndrome, with individuals at high risk of early death1.
CLCF1 also exhibits a significant role in the regulation of hematopoiesis, particularly skewing towards myeloid cell differentiation. It has been demonstrated that in mice, CLCF1 promotes B-cell expansion, enhances humoral responses, and triggers autoimmunity. Further, CLCF1 administration resulted in an increase in circulating myeloid cells, along with augmented hematopoietic progenitor cells in the bone marrow. These findings underscore CLCF1's crucial role in modulating the immune system, particularly in the context of bonemarrow transplants and recovery following sub-lethal irradiation2.
Interestingly, CLCF1 is a member of the IL-6 family of cytokines, known for their significant roles in immune regulation and stem cell biology. Like other family members, CLCF1 is secreted as a composite cytokine with CRLF1 and signals through the heterodimerization of the signaling chains LIFRβ and gp130. This suggests overlapping functions with leukemia inhibitor factor (LIF), another IL-6 family member. Expression of CLCF1 is documented in lymph nodes, spleen, and circulating lymphocytes, further establishing its role in immune modulation. However, the comprehensive implications of CLCF1 in immune regulation and hematopoiesis remain an active area of investigation3.
In summary, Cardiotrophin-like cytokine factor 1 human recombinant represents a promising area of research with potential therapeutic implications in neurodevelopmental disorders and immune regulation.
What is the molecular weight/Mw of CLCF Protein?
CLCF Protein has a total Mw of 24.6kDa.
What is the source or expression system of CLCF Protein?
Escherichia Coli.
What is the Purity of CLCF Protein?
CLCF Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CLCF Protein?
The biological functionality of CLCF Protein will be determined in the future.
What is the amino acid sequence of CLCF Protein?
MGSSHHHHHH SSGLVPRGSH MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.
What applications can CLCF Protein be used in?
CLCF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CLCF Protein?
The endotoxin level is minimal, CLCF Protein was purified using conventional chromatography techniqu
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 :
GSTP1 MouseDescription:
Glutathione S-Transferase pi 1 Mouse Recombinant
Glutathione S-transferase P 1, Gst P1, GST YF-YF, GST class-pi, GST-piB, Preadipocyte growth factor.
Product # :
ENZ-909Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GSTP1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a) and having a molecular mass of 26kDa. GSTP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GSTP1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 40 units/mg, and is defined as the amount of enzyme that conjugate 1.0 umole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.More Info
-
Introduction
GSTP1 is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are believed to function in xenobiotic metabolism and have a part in susceptibility to cancer, and other diseases. GSTP1 is a glutathione S-transferase belonging to the pi class. GST family enzymes play a significant role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based upon the biochemical, immunologic and structural properties of the soluble GSTs they are grouped into 4 main classes: alpha, mu, pi, and theta. The GSTP1 enzyme acts by catalyzing the reaction of glutathione with an acceptor molecule to form a Sulfur-substituted glutathione. The reactions employing glutathione contribute the transformation of a broad range of electrophiles, including reactive products of lipid, protein, carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress.
The GSTP1 inactivation through CpG hypermethylation is frequent in pituitary adenomas and may be a factor in aggressive pituitary tumor behavior. GSTP1 is may be a transcriptional target of the p53 tumor suppressor gene. Single-nucleotide polymorphism in GSTP1 is linked to modified protein binding, which influence GSTP1's contribution to carcinogen and drug metabolism, and possibly disease pathogenesis and/or drug response. GST-pi might have central roles in proliferation of androgen-independent human prostate cancer cells. -
Synonyms
Glutathione S-transferase P 1, Gst P1, GST YF-YF, GST class-pi, GST-piB, Preadipocyte growth factor.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPPYTIV YFPVRGRCEA MRMLLADQGQ SWKEEVVTID TWMQGLLKPT CLYGQLPKFE DGDLTLYQSN AILRHLGRSL GLYGKNQREA AQMDMVNDGV EDLRGKYVTL IYTNYENGKN DYVKALPGHL KPFETLLSQN QGGKAFIVGD QISFADYNLL DLLLIHQVLA PGCLDNFPLL SAYVARLSAR PKIKAFLSSP EHVNRPINGN GKQ.
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 :
COPS8 HumanDescription:
COP9 Constitutive Photomorphogenic 8 Human Recombinant
COP9 signalosome complex subunit 8, SGN8, Signalosome subunit 8, COP9 homolog, hCOP9, JAB1-containing signalosome subunit 8, COPS8, CSN8, COP9.
Product # :
PRO-983Price :
Quantity :
Shipping Method :
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Description
COPS8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (1-209) and having a molecular mass of 25.3kDa.COPS8 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The COPS8 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
COP9 signalosome complex subunit 8 isoform 1 (COPS8) is one of the 8 subunits of COP9 signalosome, which is a much conserved protein complex that functions as an imperative regulator in multiple signaling pathways. The structure and function of COP9 signalosome is analogous to that of the 19S regulatory particle of 26S proteasome. COP9 signalosome interacts with SCF-type E3 ubiquitin ligases and acts as a positive regulator of E3 ubiquitin ligases.
-
Synonyms
COP9 signalosome complex subunit 8, SGN8, Signalosome subunit 8, COP9 homolog, hCOP9, JAB1-containing signalosome subunit 8, COPS8, CSN8, COP9.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPVAVMAESA FSFKKLLDQC ENQELEAPGG IATPPVYGQL LALYLLHNDM NNARYLWKRI PPAIKSANSE LGGIWSVGQR IWQRDFPGIY TTINAHQWSE TVQPIMEALR DATRRRAFAL VSQAYTSIIA DDFAAFVGLP VEEAVKGILE QGWQADSTTR
MVLPRKPVAG ALDVSFNKFI PLSEPAPVPP IPNEQQLARL TDYVAFLEN.
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 :
CPLX1 HumanDescription:
Complexin-1 Human Recombinant
CPLX-1, CPXI, CPX-I, CPX1, CPX-1, Synaphin2, Synaphin-2, Complexin-1, Complexin I, CPX I, CPLX1.
Product # :
PRO-645Price :
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Shipping Method :
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Description
CPLX1 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 154 amino acids (1-134 a.a) and having a molecular mass of 17.1kDa (molecular weight on SDS-PAGE will appear higher).The CPLX1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CPLX1protein solution contains 20mM Tris-HCl pH-8 and 10% glycerol.
Purity
Greater than 90% by SDS-PAGE.
More Info
-
Introduction
CPLX1 is part of the SNARE family complex binding proteins that are catalysts or inhibitors of vesicle exocytosis. CPLX1 shows reduced Ca2+-triggered fast neurotransmitter release at hippocampal glutamatergic synapses, indicating that CPLX1 is a positive regulator of transmitter release. In contrast, CPLX1 inhibits SNARE-mediated liposome and cell fusions in vitro, that result in hypothesis thus acts as a fusion clamp of synaptic exocytosis. CPLX1 regulates a late step in synaptic vesicle exocytosis.
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Synonyms
CPLX-1, CPXI, CPX-I, CPX1, CPX-1, Synaphin2, Synaphin-2, Complexin-1, Complexin I, CPX I, CPLX1.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEFVMKQALG GATKDMGKML GGDEEKDPDA AKKEEERQEA LRQAEEERKA KYAKMEAERE AVRQGIRDKYGIKKKEEREA EAQAAMEANS EGSLTRPKKA IPPGCGDEVE EEDESILDTV IKYLPGPLQD MLKK.
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 :
RGS19 HumanDescription:
Regulator of G-Protein Signaling 19 Human Recombinant
GAIP, Regulator of G-protein signalling 19, G alpha interacting protein, GNAI3IP.
Product # :
PRO-037Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RGS19 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-217a.a.) and having a molecular mass of 26.7kDa.RGS19 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RGS19 protein solution (0.5mg/1ml) is formulated in Phosphate Buffered Saline (pH7.4) and 10% Glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
RGS19 is a member of RGS (regulator of G protein signaling) family and negatively regulates G protein coupled receptor signaling. RGS19 protein specifically cooperates with heterotrimeric GTP-binding protein G alpha i3 (GAI3).
-
Synonyms
GAIP, Regulator of G-protein signalling 19, G alpha interacting protein, GNAI3IP.
-
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.Please avoid freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPTPHEAEKQ ITGPEEADRP PSMSSHDTAS PAAPSRNPCC LCWCCCCSCS WNQERRRAWQ ASRESKLQPL PSCEVCATPS PEEVQSWAQS FDKLMHSPAG RSVFRAFLRT EYSEENMLFW LACEELKAEA NQHVVDEKAR LIYEDYVSIL SPKEVSLDSR VREGINKKMQ EPSAHTFDDA QLQIYTLMHR DSYPRFLSSP TYRALLLQGP SQSSSEA
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin qA Mouse, PEGDescription:
Leptin Quadruple Antagonist Pegylated Mouse Recombinant
Product # :
CYT-1244Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Antagonist Quadruple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Mouse Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin Quadruple anatagonist Pegylated runs as a 55 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Mouse Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Pegylated Mouse Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated recombinant mouse leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super mouse leptin antagonist but in vivo it has profound weight gain effect, resulting mainly from increased food intake. Its in vivo activity compared to that of PEG-MLA is 9-27 fold higher.
More Info
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leptin Antagonist Quadruple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin produced mainly by adipocytes. Leptin mostly regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 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.
- View Data Sheet
Name :
PDPN P56F7AT AntibodyDescription:
Podoplanin clone P56F7AT, Mouse Anti Human
Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.
Product # :
ANT-641Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
Introduction
Podoplanin is a small mucin-like type-1 transmembrane protein, typically expressed in various specialized cell types throughout the body. Podoplanin is a type-I integral membrane glycoprotein with diverse distribution in human tissues. PDPN physiological function is related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor.
PDPN is expressed in lymphatic progenitor cells and afterwards during mouse development in lymphatic endothelial cells. Podoplanin is a specific marker for lymph vessel endothelial cells. Over-expression of podoplanin significantly elevates endothelial cell adhesion, migration, and tube formation. Inhibition of Podoplanin expression decreases cell adhesion in human dermal lymphatic endothelial cells. Podoplanin is used as a specific marker for lymphatic endothelium in histopathology.
Podoplanin expression is increased in nearly all human colon, rectum, and small intestine tumors. AGGRUS may serve as a diagnostic marker that distinguishes seminomas, the majority of which over express the protein, from embryonal carcinoma in testicular germ cell tumors. -
Synonyms
Podoplanin, Glycoprotein 36, PA2.26 antigen, T1A, GP36, GP40, Gp38, OTS8, T1A2, HT1A-1, PA2.26, T1-alpha, PDPN.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human PDPN mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PDPN amino acids 99-207 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and k light chain.
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Clone
P56F7AT.
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Applications
PDPN antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
-
Purification Method
PDPN antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GDNF RatDescription:
Glial-Derived Neurotrophic Factor Rat Recombinant
ATF1, ATF2, HFB1-GDNF, GDNF.
Product # :
CYT-403Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Glial derived Neurotrophic Factor Rat Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 134 amino acids and having a total molecular mass of 29.8 kDa.
Source
Escherichia Coli.
Formulation
GDNF was lyophilized from a sterile solution containing 1xPBS, pH 7.4.
Purity
Greater than 98.0% as determined by HPLC analysis and by SDS-PAGE.
Biological Activity
Recombinant rat GDNF has full biological activity when compared to standards. The ED50, determined by a cell proliferation assay using rat C6 cells, is less than 0.2ng/ml corresponding to a specific activity of more than 5,000,000IU/mg.More Info
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Introduction
GDNF promotes the survival and differentiation of neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
GDNF enhances survival and morphological differentiation of neurons and increases their high-affinity uptake. -
Synonyms
ATF1, ATF2, HFB1-GDNF, GDNF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Glial-derived Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDNF 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 Glial Derived Neurotrophic Factor 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
SPDKQAALP RRENRNRQAAA ASPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCESAETMYD KILKNLSRSR RLTSDKVGQA CCRPVAFDDD LSFLDDNLVY HILRKHSAKR CGCI
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Background
What is the molecular weight/Mw of GDNF RAT Protein?
GDNF RAT Protein has a total Mw of 29.8kDa.
What is the source or expression system of GDNF RAT Protein?
Escherichia Coli.
What is the Purity of GDNF RAT Protein?
GDNF RAT Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of GDNF RAT Protein?
Recombinant rat GDNF has full biological activity when compared to standards. The ED50, determined by a cell proliferation assay using rat C6 cells, is less than 0.2ng/ml corresponding to a specific activity of more than 5,000,000IU/mg.
What is the amino acid sequence of GDNF RAT Protein?
SPDKQAALP RRENRNRQAAA ASPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCESAETMYD KILKNLSRSR RLTSDKVGQA CCRPVAFDDD LSFLDDNLVY HILRKHSAKR CGCI
What applications can GDNF RAT Protein be used in?
GDNF RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDNF RAT Protein?
The endotoxin level is minimal, GDNF RAT Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GH Gilthead SeabreamDescription:
Growth Hormone Gilthead Seabream Recombinant
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
Product # :
CYT-529Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Somatotropin Gilthead Seabream Recombinant Sparus Aurata produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids with an additional Ala at the N-terminus and having a molecular mass of 21.4 kDa. The Gilthead Seabream Growth-Hormone Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Binding assays of the 125I-labeled gilthead seabream GH to dolphin fish liver microsomal fraction resulted in high specific binding characterized by a Ka of 1.93 nM and a Bmax of 540 fmol/mg microsomal fraction protein. Recombinant gilthead seabream Growth Hormone, like ovine placental lactogen, exhibited growth-stimulating activity when applied orally to Sparus aurata larvae or intraperitoneally to juvenile fish.More Info
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Introduction
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
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Synonyms
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Growth-Hormone Gilthead Seabream although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions 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 Growth-Hormone Gilthead Seabream in 0.4% NaHCO3 or water adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.
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Amino Acid Sequence
AQPITDGQRLFSIAVSRVQHLHLLAQRLFSDFESSLQTEEQPQLNKIFLQ
DFCNCDYIISPIDKHETQRSSVLKLLSISYRLVESWEFPSRSLSGGSAPR
NQISPKLSELKTGIHLLIRANEDGAEIFPDRSALQLAPYGNYYQSLGTDE
SLRRTYELLACFKKDMHKVETYLTVAKCRLSPEANCTL
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 :
OPG Human, Hi-5Description:
Osteoprotegerin Human Recombinant, Hi-5
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.
Product # :
CYT-633Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant Osteoprotegerin produced in baculovirus is a signle, glycosylated polypeptide chain containing 389 amino acid residues (22-401 a.a.), having a calculated molecular mass of 44.7 kDa. The Osteoprotegerin is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Hi-5.
Formulation
Osteoprotegerin protein contains PBS pH-7.4 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range ≤ 8 ng/ml and is measured by its ability to inhibit cytotoxicity using Jurkat human acute T cell leukemia cells in the presence of 2ng/ml of human TRAIL (CAT# cyt-1014).
More Info
-
Introduction
Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.
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Synonyms
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.
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Physical Appearance
Sterile Filtered colorless 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. Please avoid freeze thaw cycles.
-
Amino Acid Sequence
ADPETFPPKY LHYDEETSHQ LLCDKCPPGT YLKQHCTAKW KTVCAPCPDH YYTDSWHTSD ECLYCSPVCK ELQYVKQECN RTHNRVCECK EGRYLEIEFC LKHRSCPPGF GVVQAGTPER NTVCKRCPDG FFSNETSSKA PCRKHTNCSV FGLLLTQKGN ATHDNICSGN SESTQKCGID VTLCEEAFFR FAVPTKFTPN WLSVLVDNLP GTKVNAESVE RIKRQHSSQE QTFQLLKLWK HQNKDQDIVK KIIQDIDLCE NSVQRHIGHA NLTFEQLRSL MESLPGKKVG AEDIEKTIKA CKPSDQILKL LSLWRIKNGD QDTLKGLMHA LKHSKTYHFP KTVTQSLKKT IRFLHSFTMY KLYQKLFLEM IGNQVQSVKI SCLSHHHHHH.
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 :
GZMH Human, sf9Description:
Granzyme-H Human Recombinant, sf9
Granzyme H, Granzyme H (Cathepsin G-Like 2, Protein H-CCPX), Cytotoxic T-Lymphocyte Proteinase, Cathepsin G-Like 2, CTSGL2, CCP-X, CSP-C, Cytotoxic T-Lymphocyte-Associated Serine Esterase 1, Cathepsin G-Like 2, Protein H-CCPX, Cytotoxin Serine Protease-C, Cytotoxic Serine Protease C, Protein H-CCPX, EC 3.4.21.79, EC 3.4.21, EC 3.4.21, CTLA1, CGL-2 , CGL2.
Product # :
ENZ-961Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GZMH produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 234 amino acids (19-246 a.a.) and having a molecular mass of 26.2kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). GZMH is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
GZMH protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Granzyme H also known as GZMH belongs to the peptidase S1 family. GZMH is an essential part for HBV eradication. The HBx protein, which is required for the replication of HBV, is cleaved at Met(79) by GZMH. Furthermore, GZMH inhibitor can abolish GZNH- as well as lymphokine-activated killer cell-mediated HBx degradation and HBV clearance. A HBx-deficient HBV is resistant to GzmH- in addition to lymphokine-activated killer cell-mediated viral clearance.
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Synonyms
Granzyme H, Granzyme H (Cathepsin G-Like 2, Protein H-CCPX), Cytotoxic T-Lymphocyte Proteinase, Cathepsin G-Like 2, CTSGL2, CCP-X, CSP-C, Cytotoxic T-Lymphocyte-Associated Serine Esterase 1, Cathepsin G-Like 2, Protein H-CCPX, Cytotoxin Serine Protease-C, Cytotoxic Serine Protease C, Protein H-CCPX, EC 3.4.21.79, EC 3.4.21, EC 3.4.21, CTLA1, CGL-2 , CGL2.
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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
EEIIGGHEAK PHSRPYMAFV QFLQEKSRKR CGGILVRKDF VLTAAHCQGS SINVTLGAHN IKEQERTQQF IPVKRPIPHP AYNPKNFSND IMLLQLERKA KWTTAVRPLR LPSSKAQVKP GQLCSVAGWG YVSMSTLATT LQEVLLTVQK DCQCERLFHG NYSRATEICV GDPKKTQTGF KGDSGGPLVC KDVAQGILSY GNKKGTPPGV YIKVSHFLPW IKRTMKRLHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ASF1A HumanDescription:
ASF1 Anti-Silencing Function 1 Homolog A Human Recombinant
CGI-98, HSPC146, DKFZp547E2110, ASF1A, Histone chaperone ASF1A, Anti-silencing function protein 1 homolog A, hAsf1, hAsf1a, CCG1-interacting factor A, CIA, hCIA.
Product # :
PRO-682Price :
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Shipping Method :
Shipped with Ice Packs
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Description
ASF1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (1-204 a.a.) and having a molecular mass of 27kDa.ASF1A is fused to a 36 amino acid His Tag and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ASF1A protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ASF1A is part of the H3/H4 family of histone chaperone proteins corresponding to the anti-silencing function-1 gene in yeast. ASF1A is an important element of the histone donor complex that functions in nucleosome assembly. ASF1A interacts with histones H3 and H4, and functions together with a chromatin assembly factor during DNA replication and repair. Deletion of ASF1A in yeast and Drosophila confers sensitivity to various DNA damaging agents and inhibitors of DNA replication, increases genomic instability and sister chromatid exchange, and activates the DNA damage checkpoint.
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Synonyms
CGI-98, HSPC146, DKFZp547E2110, ASF1A, Histone chaperone ASF1A, Anti-silencing function protein 1 homolog A, hAsf1, hAsf1a, CCG1-interacting factor A, CIA, hCIA.
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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 KDRWGSMAKV QVNNVVVLDN PSPFYNPFQF EITFECIEDL SEDLEWKIIY VGSAESEEYD QVLDSVLVGP VPAGRHMFVF QADAPNPGLI PDADAVGVTV VLITCTYRGQ EFIRVGYYVN NEYTETELRE NPPVKPDFSK LQRNILASNPRVTRFHINWE DNTEKLEDAE SSNPNLQSLL STDALPSASK GWSTSENSLN VMLESHMDCM.
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 :
HTF HumanDescription:
Holo Transferrin Human
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.
Product # :
PRO-315Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Holo Transferrin is a glycoprotein of approximately 77 kDa.
Source
Human serum.
Formulation
The protein (10mg/ml) was lyophilized from 20mM NH4HC03 solution.
May contain traces of buffer salts.Purity
Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.
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Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells. -
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.
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Physical Appearance
Sterile Filtered Pink lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Holo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Holo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Human Virus Test
FDA approved Plasma from each donor has been tested and found negative for antibodies to HIV-1 & 2, HCV, HBsAG, HBc, HBV, HAV, HIV and Syphilis.
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Iron Content
The Iron content was estimated by ICP and was found to be 1232 ppm.
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 :
S.Typhi OMPDescription:
Salmonella Typhi Outer Membrane Protein Recombinant
Product # :
STY-002Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Salmonella Typhi Outer Membrane Protein produced in E.coli contains 315 amino acids, and fused to a 6 His Tag at C-terminus, migrating as a 33kDa band on SDS-PAGE.S. typhi outer membrane protein is a central pathogen in S. typhi infection, and is directly exposed to the outside to interact with the human immune system.
Source
Escherichia Coli.
Formulation
Sterile Filtered solution containing 10mM Tris-HCl, 1mM EDTA and 50mM arginine.
Purity
Protein is >95% pure as determined by 12% PAGE (coomassie staining).
More Info
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Introduction
Salmonella Typhi is a pathogen causing typhoid fever, affecting over 17 million people with approximately 600,000 deaths annually worldwide. If untreated, typhoid fever cases result in mortality rates ranging from 12-30%.
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Physical Appearance
Sterile Filtered solution.
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Stability
S.Typhi OMP although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HB-EGF HumanDescription:
HB-EGF Human Recombinant
HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.
Product # :
CYT-119Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
HB-EGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 87 amino acids and having a molecular mass of 9.9kDa. The HB-EGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM sodium phosphate pH-7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.
More Info
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Introduction
HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind HPR sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.
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Synonyms
HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Human HB-EGF Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HB-EGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Human HB-EGF in sterile 18M-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
MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
KYVKELRAPS CICHPGYHGE RCHGLSL.
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Background
What is the molecular weight/Mw of HB-EGF Protein?
HB-EGF Protein has a total Mw of 9.9kDa.
What is the source or expression system of HB-EGF Protein?
Escherichia Coli.
What is the Purity of HB-EGF Protein?
HB-EGF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of HB-EGF Protein?
The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.
What is the amino acid sequence of HB-EGF Protein?
MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
KYVKELRAPS CICHPGYHGE RCHGLSL.
What applications can HB-EGF Protein be used in?
HB-EGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for HB-EGF Protein?
The endotoxin level is minimal, HB-EGF 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.