Search results
1000 results found for “Transferrin”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
THAP11 HumanDescription:
THAP Domain Containing, Apoptosis Associated Protein 11 Human Recombinant
THAP domain-containing protein 11, CTG-B43a, CTG-B45d, HRIHFB2206, RONIN, THAP domain-containing protein 11, THAP11.
Product # :
PRO-2009Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
THAP11 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314) and having a molecular mass of 36.8kDa.THAP11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The THAP11 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
-
Introduction
THAP Domain Containing, Apoptosis Associated Protein 11 (THAP11) is a part of the thanatos-associated protein family. THAP11 plays a role as a transcriptional repressor and interacts with HCF1 through a coiled coil domain. THAP11 which is localized to the nucleus and cytoplasm takes part in embryogenesis and pluripotency of embryonic stem cells by recruiting epigenetic modifiers.
-
Synonyms
THAP domain-containing protein 11, CTG-B43a, CTG-B45d, HRIHFB2206, RONIN, THAP domain-containing protein 11, THAP11.
-
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 MGSMPGFTCC VPGCYNNSHR DKALHFYTFP KDAELRRLWL KNVSRAGVSG CFSTFQPTTG HRLCSVHFQG GRKTYTVRVP TIFPLRGVNE RKVARRPAGA AAARRRQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQSSPSA STAQTAQLQP NLVSASAAVL LTLQATVDSS QAPGSVQPAP ITPTGEDVKP IDLTVQVEFA AAEGAAAAAA ASELQAATAG LEAAECPMGP QLVVVGEEGF PDTGSDHSYS LSSGTTEEEL LRKLNEQRDI LALMEVKMKE MKGSIRHLRL TEAKLREELR EKDRLLAMAV IRKKHGM.
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 :
RNMT HumanDescription:
RNA (guanine-7-) Methyltransferase Human Recombinant
mRNA cap guanine-N7 methyltransferase, RG7MT1, mRNA (guanine-N(7)-)-methyltransferase, mRNA cap methyltransferase, hCMT1, hMet, hcm1p, RNMT, KIAA0398, MET, RG7MT1, hCMT1c, DKFZp686H1252.
Product # :
ENZ-114Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
RNMT produced in E.Coli is a single, non-glycosylated polypeptide chain containing 496 amino acids (1-476 a.a.) and having a molecular mass of 57kDa.RNMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RNMT solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) 2mM DTT, 20% glycerol and 100mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
RNMT is a widely expressed nuclear protein which is a member of the mRNA cap methyltransferase family. Cap-dependent mRNA translation requires the methylation of the mRNA guanosine cap by RNMT. RNMT catalyzes the transfer of a methyl group from AdoMet (S-adenosylmethionine) to the GpppN end of the growing mRNA at the N-7 position, thus producing AdoHyc (S-adenosylhomocysteine) and m7GpppN terminated RNA.
-
Synonyms
mRNA cap guanine-N7 methyltransferase, RG7MT1, mRNA (guanine-N(7)-)-methyltransferase, mRNA cap methyltransferase, hCMT1, hMet, hcm1p, RNMT, KIAA0398, MET, RG7MT1, hCMT1c, DKFZp686H1252.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
RNMT Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MANSAKAEEY EKMSLEQAKA SVNSETESSF NINENTTASG TGLSEKTSVC RQVDIARKRK EFEDDLVKES SSCGKDTPSK KRKLDPEIVP EEKDCGDAEG NSKKRKRETE DVPKDKSSTG DGTQNKRKIA LEDVPEKQKN LEEGHSSTVA AHYNELQEVG LEKRSQSRIF YLRNFNNWMK SVLIGEFLEK VRQKKKRDIT VLDLGCGKGG DLLKWKKGRI NKLVCTDIAD VSVKQCQQRY EDMKNRRDSE YIFSAEFITA DSSKELLIDK FRDPQMCFDI CSCQFVCHYS FESYEQADMM LRNACERLSP GGYFIGTTPN SFELIRRLEA SETESFGNEI YTVKFQKKGD YPLFGCKYDF NLEGVVDVPE FLVYFPLLNE MAKKYNMKLV YKKTFLEFYE EKIKNNENKM LLKRMQALEP YPANESSKLV SEKVDDYEHA AKYMKNSQVR LPLGTLSKSE WEATSIYLVF AFEKQQ.
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 :
NDUFS3 HumanDescription:
Histidine NADH Dehydrogenase Fe-S Protein 3 Human Recombinant
CI-30, NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondria, Complex I-30kD, CI-30kD, NADH-ubiquinone oxidoreductase 30 kDa subunit.
Product # :
ENZ-662Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Human NDUFS3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 249amino acids (37-264 a.a.) and having a molecular mass of 28.7 kDa. NDUFS3 is fused to a 21 amino acid His Tag at N-terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The NDUFS3 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
NADH dehydrogenase [ubiquinone] iron-sulfur protein 3 (NDUFS3) is a member of the complex I 30 kDa subunit family. NDUFS3 is one of the iron-sulfur protein (IP) components of mitochondrial NADH:ubiquinone oxidoreductase (complex I). This complex is the first enzyme complex in the electron transport chain of mitochondria. The iron-sulfur protein (IP) fraction of complex I consists of seven subunits. NDUFS3 gene mutations are linked with Leigh syndrome resulting from mitochondrial complex indefficiency.
-
Synonyms
CI-30, NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondria, Complex I-30kD, CI-30kD, NADH-ubiquinone oxidoreductase 30 kDa subunit.
-
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 MESAGADTRP TVRPRNDVAH KQLSAFGEYV AEILPKYVQQ VQVSCFNELE VCIHPDGVIP VLTFLRDHTN AQFKSLVDLT AVDVPTRQNR FEIVYNLLSL RFNSRIRVKT YTDELTPIES AVSVFKAANW YEREIWDMFG VFFANHPDLR RILTDYGFEG HPFRKDFPLS GYVELRYDDE VKRVVAEPVE LAQEFRKFDL NSPWEAFPVY RQPPESLKLE AGDKKPDAK
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 :
CD105 Human, HisDescription:
Endoglin Human Recombinant, His-Tag
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
Product # :
CYT-823Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- sds-page
Description
Endoglin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 594 amino acids (26-586) and having a molecular mass of 64.9 kDa. Endoglin is fused to a 36 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The Endoglin solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 150mM NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
sds-page
More Info
-
Introduction
Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.The Endoglin protein consists of a homodimer of 180 kDA with disulfide links. Endoglin has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Endoglin has been found to be part of the TGF-beta1 receptor complex. Endoglin thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Endoglin expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.
-
Synonyms
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSETVH CDLQPVGPER DEVTYTTSQV SKGCVAQAPN AILEVHVLFL EFPTGPSQLE LTLQASKQNG TWPREVLLVL SVNSSVFLHL QALGIPLHLA YNSSLVTFQE PPGVNTTELP SFPKTQILEW AAERGPITSA AELNDPQSIL LRLGQAQGSL SFCMLEASQD MGRTLEWRPR TPALVRGCHL EGVAGHKEAH ILRVLPGHSA GPRTVTVKVE LSCAPGDLDA VLILQGPPYV SWLIDANHNM QIWTTGEYSF KIFPEKNIRG FKLPDTPQGL LGEARMLNAS IVASFVELPL ASIVSLHASS CGGRLQTSPA PIQTTPPKDT CSPELLMSLI QTKCADDAMT LVLKKELVAH LKCTITGLTF WDPSCEAEDR GDKFVLRSAY SSCGMQVSAS MISNEAVVNI LSSSSPQRKK VHCLNMDSLS FQLGLYLSPH FLQASNTIEP GQQSFVQVRV SPSVSEFLLQ LDSCHLDLGP EGGTVELIQG RAAKGNCVSL LSPSPEGDPR FSFLLHFYTV PIPKTGTLSC TVALRPKTGS QDQEVHRTVF MRLNIISPDL SGCTSKG
-
Background
What is the molecular weight/Mw of CD105 Protein?
CD105 Protein has a total Mw of 64.9kDa.
What is the source or expression system of CD105 Protein?
Escherichia Coli.
What is the Purity of CD105 Protein?
CD105 Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of CD105 Protein?
The biological functionality of CD105 Protein will be determined in the future.
What is the amino acid sequence of CD105 Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSETVH CDLQPVGPER DEVTYTTSQV SKGCVAQAPN AILEVHVLFL EFPTGPSQLE LTLQASKQNG TWPREVLLVL SVNSSVFLHL QALGIPLHLA YNSSLVTFQE PPGVNTTELP SFPKTQILEW AAERGPITSA AELNDPQSIL LRLGQAQGSL SFCMLEASQD MGRTLEWRPR TPALVRGCHL EGVAGHKEAH ILRVLPGHSA GPRTVTVKVE LSCAPGDLDA VLILQGPPYV SWLIDANHNM QIWTTGEYSF KIFPEKNIRG FKLPDTPQGL LGEARMLNAS IVASFVELPL ASIVSLHASS CGGRLQTSPA PIQTTPPKDT CSPELLMSLI QTKCADDAMT LVLKKELVAH LKCTITGLTF WDPSCEAEDR GDKFVLRSAY SSCGMQVSAS MISNEAVVNI LSSSSPQRKK VHCLNMDSLS FQLGLYLSPH FLQASNTIEP GQQSFVQVRV SPSVSEFLLQ LDSCHLDLGP EGGTVELIQG RAAKGNCVSL LSPSPEGDPR FSFLLHFYTV PIPKTGTLSC TVALRPKTGS QDQEVHRTVF MRLNIISPDL SGCTSKG
What applications can CD105 Protein be used in?
CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CD105 Protein?
The endotoxin level is minimal, CD105 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 :
TFAM HumanDescription:
Transcription Factor-A Recombinant Human
Transcription factor A, mitochondrial, TCF6, TCF6L2, Mitochondrial transcription factor 1, Transcription factor 6-like 2, MtTF1, mtTFA, TCF6L1, TCF6L3.
Product # :
PRO-095Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TFAM produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (43-246.a.a) and having a molecular mass of 26.6kDa. TFAM is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TFAM protein solution (0.25mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
TFAM is a mitochondrial transcription factor which is a main activator of mitochondrial transcription and is also a participant in mitochondrial genome replication. TFAM is situated primarily in the nuclei of elongated spermatids and takes part in the regulation of gene expression of the haploid male genome. TFAM is linked to mitochondrial disorder in humans characterized by ocular myopathy, exercise intolerance and muscle wasting.
-
Synonyms
Transcription factor A, mitochondrial, TCF6, TCF6L2, Mitochondrial transcription factor 1, Transcription factor 6-like 2, MtTF1, mtTFA, TCF6L1, TCF6L3.
-
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 MSSVLASCPK KPVSSYLRFS KEQLPIFKAQ NPDAKTTELI RRIAQRWREL PDSKKKIYQD AYRAEWQVYK EEISRFKEQL TPSQIMSLEK EIMDKHLKRK AMTKKKELTL LGKPKRPRSA YNVYVAERFQ EAKGDSPQEK LKTVKENWKN LSDSEKELYI QHAKEDETRY HNEMKSWEEQ MIEVGRKDLL RRTIKKQRKY GAEEC
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 :
Vimentin HumanDescription:
Vimentin Human Recombinant
Vimentin, Vim, FLJ36605.
Product # :
PRO-309Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Vimentin Human Recombinant produced in E.coli cells is a single non-glycosylated protein containing 465 amino acids chain and having a molecular mass of 53.5kDa. The Vimentin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Vimentin was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Vimentin expression in human malignant glioma cells depends on cellular density, algorithms of drug delivery and chemo/radio treatment. Vimentin and detyrosinated microtubules provide structural support for the extensive microtentacles observed in detached tumor cells and a mechanism to promote successful metastatic spread. Primary colorectal carcinomas display aberrant expression of vimentin, and have activated Notch and TGFbeta signaling pathways. Vimentin is a strong arterial substrate for transglutaminases. Transglutaminase-mediated vimentin dimerization results in a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Ablation of vimentin expression inhibits migration and invasion of colon and breast cancer cell lines. Vimentin is the main intermediate filament protein in mesenchymal cells and is therefore of value in the differential diagnosis of undifferentiated neoplasms.
-
Synonyms
Vimentin, Vim, FLJ36605.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Vimentin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Vimentin 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.
-
Solubility
It is recommended to reconstitute the lyophilized Vimentin in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
STRSVSSSSY RRMFGGPGTA SRPSSSRSYV TTSTRTYSLG SALRPSTSRS LYASSPGGVY ATRSSAVRLR SSVPGVRLLQ DSVDFSLADA INTEFKNTRT NEKVELQELN DRFANYIDKV RFLEQQNKIL LAELEQLKGQ GKSRLGDLYE EEMRELRRQV DQLTNDKARV EVERDNLAED IMRLREKLQE EMLQREEAEN TLQSFRQDVD NASLARLDLE RKVESLQEEI AFLKKLHEEE IQELQAQIQE QHVQIDVDVS KPDLTAALRD VRQQYESVAA KNLQEAEEWY KSKFADLSEA ANRNNDALRQ AKQESTEYRR QVQSLTCEVD ALKGTNESLE RQMREMEENF AVEAANYQDT IGRLQDEIQN MKEEMARHLR EYQDLLNVKM ALDIEIATYR KLLEGEESRI SLPLPNFSSL NLRETNLDSL PLVDTHSKRT LLIKTVETRD GQVINETSQH HDDLE.
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 :
IFNA7 HumanDescription:
IFN-alpha 7 Human Recombinant
IFN alpha-7, IFN-alpha-7, IFN alpha-J, LeIF J, IFN alpha-J1, IFN-alpha-J1, IFNA7, IFNA-J, IFN-alphaJ.
Product # :
CYT-196Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- SDS-PAGE
Description
IFNA7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (24-189 a.a) and having a molecular mass of 22.3kDa.IFNA7 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
IFNA7 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
SDS-PAGE
More Info
-
Introduction
IFN alpha 7 (IFNA7) is a member of the alpha/beta IFN family. IFNA7 is generated by macrophages. IFN-alpha has antiviral functions. IFN promotes the production of 2 enzymes: a protein kinase and an oligoadenylate synthetase.
-
Synonyms
IFN alpha-7, IFN-alpha-7, IFN alpha-J, LeIF J, IFN alpha-J1, IFN-alpha-J1, IFNA7, IFNA-J, IFN-alphaJ.
-
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 MGSHMCDLPQ THSLRNRRAL ILLAQMGRIS PFSCLKDRHE FRFPEEEFDG HQFQKTQAIS VLHEMIQQTF NLFSTEDSSA AWEQSLLEKF STELYQQLND LEACVIQEVG VEETPLMNED FILAVRKYFQ RITLYLMEKK YSPCAWEVVR AEIMRSFSFS TNLKKGLRRK D.
-
Background
What is the molecular weight/Mw of IFNA7 HUMAN Protein?
IFNA7 HUMAN Protein has a total Mw of 22.3kDa.
What is the source or expression system of IFNA7 HUMAN Protein?
Escherichia Coli.
What is the Purity of IFNA7 HUMAN Protein?
IFNA7 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNA7 HUMAN Protein?
The biological functionality of IFNA7 HUMAN Protein will be determined in the future.
What is the amino acid sequence of IFNA7 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMCDLPQ THSLRNRRAL ILLAQMGRIS PFSCLKDRHE FRFPEEEFDG HQFQKTQAIS VLHEMIQQTF NLFSTEDSSA AWEQSLLEKF STELYQQLND LEACVIQEVG VEETPLMNED FILAVRKYFQ RITLYLMEKK YSPCAWEVVR AEIMRSFSFS TNLKKGLRRK D.
What applications can IFNA7 HUMAN Protein be used in?
IFNA7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNA7 HUMAN Protein?
The endotoxin level is minimal, IFNA7 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
INSR HumanDescription:
Insulin Receptor Human Recombinant
Insulin receptor, IR, EC 2.7.10.1, CD220, INSR, HHF5.
Product # :
CYT-777Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Insulin Receptor Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (aa 28-944 of the short isoform- HIR-A, Uniprot accession # P06213-2 which includes the whole subunit alpha and extracellular domain of subunit beta) containing a total of 927 amino acids, having a molecular mass of 105.9kDa (calculated), though it migrates at approximately 160kDa on SDS PAGE, the INSR is fused to a 2 a.a N-terminal linker, a 2 a.a C-terminal linker and fused to a 6 a.a His tag at C-Terminus.The Human INSR is purified by proprietary chromatographic techniques.
Source
HEK 293.
Formulation
INSR was filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Insulin Receptor (INSR) is a receptor tyrosine kinase which mediates the pleiotropic actions of insulin. Binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. Once the precursor signal peptide is removed, the insulin receptor precursor is post-translationally cleaved into 2 chains (alpha and beta) which are covalently linked. Insulin binding initiates phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins function as docking proteins for other signaling proteins which contain Src-homology-2 domains (SH2 domain) that specifically recognize different phosphotyrosines residues, including the p85 regulatory subunit of PI3K and SHP2.
-
Synonyms
Insulin receptor, IR, EC 2.7.10.1, CD220, INSR, HHF5.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
-
Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. INSR is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
ASHLYPGEVC PGMDIRNNLT RLHELENCSV IEGHLQILLM FKTRPEDFRD LSFPKLIMIT DYLLLFRVYG LESLKDLFPN LTVIRGSRLF FNYALVIFEM VHLKELGLYN LMNITRGSVR IEKNNELCYL ATIDWSRILD SVEDNYIVLN KDDNEECGDI CPGTAKGKTN CPATVINGQF VERCWTHSHC QKVCPTICKS HGCTAEGLCC HSECLGNCSQ PDDPTKCVAC RNFYLDGRCV ETCPPPYYHF QDWRCVNFSF CQDLHHKCKN SRRQGCHQYV IHNNKCIPEC PSGYTMNSSN LLCTPCLGPC PKVCHLLEGE KTIDSVTSAQ ELRGCTVING SLIINIRGGN NLAAELEANL GLIEEISGYL KIRRSYALVS LSFFRKLRLI RGETLEIGNY SFYALDNQNL RQLWDWSKHN LTITQGKLFF HYNPKLCLSE IHKMEEVSGT KGRQERNDIA LKTNGDQASC ENELLKFSYI RTSFDKILLR WEPYWPPDFR DLLGFMLFYK EAPYQNVTEF DGQDACGSNS WTVVDIDPPL RSNDPKSQNH PGWLMRGLKP WTQYAIFVKT LVTFSDERRT YGAKSDIIYV QTDATNPSVP LDPISVSNSS SQIILKWKPP SDPNGNITHY LVFWERQAED SELFELDYCL KGLKLPSRTW SPPFESEDSQ KHNQSEYEDS AGECCSCPKT DSQILKELEE SSFRKTFEDY LHNVVFVPRP SRKRRSLGDV GNVTVAVPTV AAFPNTSSTS VPTSPEEHRP FEKVVNKESL VISGLRHFTG YRIELQACNQ DTPEERCSVA AYVSARTMPE AKADDIVGPV THEIFENNVV HLMWQEPKEP NGLIVLYEVS YRRYGDEELH LCVSRKHFAL ERGCRLRGLS PGNYSVRIRA TSLAGNGSWT EPTYFYVTDY LDVPSNIAKK 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 :
HAVCR1 MouseDescription:
Hepatitis A Virus Cellular Receptor 1 Mouse Recombinant
Hepatitis A virus cellular receptor 1 homolog, HAVcr-1, Kidney injury molecule 1, KIM-1, T cell immunoglobulin and mucin domain-containing protein 1, TIMD-1, T cell membrane protein 1, T-cell immunoglobulin mucin receptor 1, TIM-1.
Product # :
HAV-232Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
HAVCR1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 222 amino acids (22-237 a.a.) and having a molecular mass of 24.4kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). HAVCR1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
HAVCR1 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
-
Introduction
Hepatitis A virus cellular receptor 1 (HAVCR1) is a membrane receptor for both human hepatitis A virus (HHAV) and TIMD4. HAVCR1 is a type I trans-membrane structural glycoprotein located in the renal proximal tubule epithelial cells. HAVCR1 protein may be involved in the control of asthma and allergic diseases. The reference genome represents an allele which retains a MTTVP amino acid segment that presents defense against atopy in HHAV seropositive individuals.
-
Synonyms
Hepatitis A virus cellular receptor 1 homolog, HAVcr-1, Kidney injury molecule 1, KIM-1, T cell immunoglobulin and mucin domain-containing protein 1, TIMD-1, T cell membrane protein 1, T-cell immunoglobulin mucin receptor 1, TIM-1.
-
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
YVEVKGVVGH PVTLPCTYST YRGITTTCWG RGQCPSSACQ NTLIWTNGHR VTYQKSSRYN LKGHISEGDV SLTIENSVES DSGLYCCRVE IPGWFNDQKV TFSLQVKPEI PTRPPTRPTT TRPTATGRPT TISTRSTHVP TSIRVSTSTP PTSTHTWTHK PEPTTFCPHE TTAEVTGIPS HTPTDWNGTV TSSGDTWSNH TEAIPPGKPQ KNPTKGHHHH HH.
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 :
Resistin RatDescription:
Resistin Rat Recombinant
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Product # :
CYT-1129Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Resistin Rat Recombinant produced in E.Coli is disulfide-linked homodimer consisting of 2x95 amino acid polypeptide chains and having a molecular mass of approximately 20.2kDa.Resistin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Resistin, a product of the RSTN gene, is a peptide hormone belongs to the class of cysteine-rich secreted proteins (monomeric peptide contains 11 cysteine residues) referred to as the RELM family, and is also described as ADSF (Adipose Tissue-Specific Secretory Factor) or FIZZ3 (Found in Inflammatory Zone 3). Resistin may be an important link between obesity. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppressed the ability to stimulate glucose uptake. They have also suggested that resistin was present at elevated levels in blood of obese mice, and was down regulated by fasting and by antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression. -
Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Resistin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Resistin should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Resistin in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MPSMSLCPMD EAISKKINQD FSSLLPAAMK NTVLHCWSVS SRGRLASCPE GTTVTSCSCG SGCGSWDVRE DTMCHCQCGS IDWTAARCCT LRVGS.
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 :
CD105 Human, Sf9Description:
Endoglin Human Recombinant, Sf9
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
Product # :
CYT-389Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CD105 Human Recombinant extracellular domain produced in baculovirus is a homodimeric, glycosylated, Polypeptide containing 586 amino acids and having a molecular mass of 61 kDa but as a result of glycosylation, migrates at 90 kDa under reducing conditions in SDS-PAGE. The CD105 is fused to a C-terminal His-tag (6xHis) and purified by proprietary chromatographic techniques.
Source
Sf9 Insect Cells.
Formulation
Endoglin was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.More Info
-
Introduction
Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.
The protein consists of a homodimer of 180 kDA with disulfide links. It has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Endoglin has been found to be part of the TGF-beta1 receptor complex. It thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Its expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities. -
Synonyms
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Endoglin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CD105 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.
-
Solubility
It is recommended to reconstitute the lyophilized CD-105 in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTY TTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVL SVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPI TSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLE GVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLID ANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPL ASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKE LVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNI LSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSE FLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPI PKTGTLSCTVALRPKTGS.
-
Background
What is the molecular weight/Mw of CD105 Protein?
CD105 Protein has a total Mw of 90kDa.
What is the source or expression system of CD105 Protein?
Sf9 Insect Cells.
What is the Purity of CD105 Protein?
CD105 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CD105 Protein?
Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.
What is the amino acid sequence of CD105 Protein?
MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTY TTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVL SVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPI TSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLE GVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLID ANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPL ASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKE LVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNI LSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSE FLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPI PKTGTLSCTVALRPKTGS.
What applications can CD105 Protein be used in?
CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CD105 Protein?
The endotoxin level is minimal, CD105 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 :
OX40L HumanDescription:
OX40 Ligand Human 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-1226Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
OX40L Human Recombinant is a single, glycosylated, polypeptide chain (51-183 a.a) containing a total of139 amino acids and having a molecular mass of 16.2 kDa. OX40L is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 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
Measured by its binding ability in a functional ELISA with Human OX40/TNFRSF4.
More Info
-
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.
-
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
QVSHRYPRIQ SIKVQFTEYK KEKGFILTSQ KEDEIMKVQN NSVIINCDGF YLISLKGYFS QEVNISLHYQ KDEEPLFQLK KVRSVNSLMV ASLTYKDKVY LNVTTDNTSL DDFHVNGGEL ILIHQNPGEF CVLHHHHHH.
-
Background
OX40 Ligand (OX40L), a member of the tumor necrosis factor (TNF) superfamily, plays a pivotal role in regulating immune responses and orchestrating the delicate balance between activation and tolerance. The human recombinant form of OX40L has emerged as a potent tool in immunology, offering insights into its molecular intricacies and potential applications in therapeutic interventions. This research embarks on a journey to unravel the multifaceted role of OX40L Human Recombinant, shedding light on its structural attributes, signaling pathways, and its promising avenues in immunotherapy. By delving into the properties of OX40L, scientists aim to expand our understanding of immune modulation and open new frontiers in the treatment of immune-related disorders.
Structural Insights into OX40L Human Recombinant:
OX40L, as a trimeric transmembrane protein, exhibits a unique structural configuration that governs its interactions with the OX40 receptor on T cells. The human recombinant form, engineered for controlled study, provides a window into the three-dimensional intricacies of the ligand. Understanding its structure is pivotal for deciphering how OX40L engages with its receptor and modulates immune responses.
Immunomodulatory Signaling Pathways:
OX40L binding to its cognate receptor OX40 on T cells triggers intricate signaling cascades that impact immune cell activation, proliferation, and cytokine production. The OX40-OX40L axis is a crucial regulator of T cell function, influencing both effector and regulatory T cell responses. Unraveling the specific pathways activated by OX40L Human Recombinant provides valuable insights into the modulation of immune responses in health and disease.
Applications in Immunotherapy:
The immunomodulatory properties of OX40L make it an attractive candidate for therapeutic interventions. OX40L Human Recombinant, in preclinical and clinical studies, is being explored for its potential in enhancing antitumor immune responses. By harnessing the ligand's ability to stimulate effector T cells and memory T cell formation, researchers aim to develop novel immunotherapies for cancer and other immune-related disorders.
OX40L in Autoimmune Diseases:
Conversely, OX40L's role in autoimmune diseases has spurred investigations into its inhibition as a therapeutic strategy. Blocking the OX40-OX40L interaction has shown promise in mitigating autoimmune responses, presenting a potential avenue for the development of treatments for conditions such as rheumatoid arthritis and inflammatory bowel disease.
While the potential of OX40L Human Recombinant in immunotherapy is promising, challenges persist. Fine-tuning its applications, understanding potential side effects, and optimizing dosages are critical considerations for translational success. Additionally, comprehending the context-dependent nature of OX40L signaling is essential for tailoring therapeutic strategies to specific diseases and patient profiles.
OX40L Human Recombinant stands at the forefront of immunomodulation research, offering a lens through which we can unravel the complexities of immune responses. Its structural insights, signaling pathways, and therapeutic applications position it as a key player in the evolving landscape of immunotherapy. As researchers continue to dissect the molecular nuances of OX40L, they not only expand our understanding of immune regulation but also pave the way for transformative advancements in the treatment of cancer and autoimmune diseases, shaping the future of precision medicine and immunotherapy.
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 :
SELE Human, HEKDescription:
E-Selectin Human Recombinant, HEK
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.
Product # :
PRO-1645Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
SELE Human Recombinant produced by mammalian expression system in human cells is a single polypeptide chain containing 543 amino acids (22-556). SELE is fused to an 8 amino acid His-tag at C-terminus is purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
SELE was lyophilized from a 0.2 µM filtered solution of PBS and 4% Mannitol, pH 7.5.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
E-selectin which is also called Endothelial leukocyte adhesion molecule 1, ELAM1, ELAM belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Eselectin is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. E-selectin is present in single copy in the human genome and contains 14 exons spanning about 13 kb of DNA.
-
Synonyms
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized SELE although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SELE should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized SELE in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
WSYNTSTEAMTYDEASAYCQQRYTHLVAIQNKEEIEYLNSILSYSPSYYWIGIRKVNNVW
VWVGTQKPLTEEAKNWAPGEPNNRQKDEDCVEIYIKREKDVGMWNDERCSKKKLALCYTA
ACTNTSCSGHGECVETINNYTCKCDPGFSGLKCEQIVNCTALESPEHGSLVCSHPLGNFSY
NSSCSISCDRGYLPSSMETMQCMSSGEWSAPIPACNVVECDAVTNPANGFVECFQNPGSFPW
NTTCTFDCEEGFELMGAQSLQCTSSGNWDNEKPTCKAVTCRAVRQPQNGSVRCSHSPAGEFT
FKSSCNFTCEEGFMLQGPAQVECTTQGQWTQQIPVCEAFQCTALSNPERGYMNCLPSASGSFR
YGSSCEFSCEQGFVLKGSKRLQCGPTGEWDNEKPTCEAVRCDAVHQPPKGLVRCAHSPIGEFTY
KSSCAFSCEEGFELHGSTQLECTSQGQWTEEVPSCQVVKCSSLAVPGKINMSCSGEPVFGTVCKF
ACPEGWTLNGSAARTCGATGHWSGLLPTCEAPTESNIPVDHHHHHH.
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 :
SERPINI1 HumanDescription:
Serpin Peptidase Inhibitor, Clade I Member 1 Human Recombinant
Neuroserpin, Peptidase inhibitor 12, PI-12, Serpin I1, SERPINI1, PI12.
Product # :
PRO-213Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
SERPINI1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 394 amino acids and having a total molecular mass of 44.7kDa. SERPINI1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 95.0% as determined by
(a) Analysis by HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by the dose-dependent stimulation of the proliferation of rat C6 cells which is less than 0.5µg/ml, corresponding to a specific activity of >2000IU/mg.More Info
-
Introduction
SERPINI1 (Neuroserpin) is an inhibitory serpin which is expressed primarily in the central nervous system. Even though the physiological target of SERPINI1 is still vague, amassed evidence suggest that SERPINI1 has an imperative role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis and the subsequent development of neuronal plasticity. The neuroprotective role of SERPINI1 has been demonstrated in transgenic mice lacking SERPINI1 expression. The deficiency of SERPINI1 in these mice is linked with motor neuron disease characterized by axonal degradation. In humans, defects in SERPINI1, caused by point mutations in the neuroserpin gene, trigger a hereditary disorder known as the familial encephalopathy with neuroserpin inclusion bodies (FENIB).
-
Synonyms
Neuroserpin, Peptidase inhibitor 12, PI-12, Serpin I1, SERPINI1, PI12.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized SERPINI1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SERPINI1 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized SERPINI1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
TGATFPEEAI ADLSVNMYNR LRATGEDENI LFSPLSIALA MGMMELGAQG
STQKEIRHSM GYDSLKNGEE FSFLKEFSNM VTAKESQYVM KIANSLFVQN
GFHVNEEFLQ MMKKYFNAAV NHVDFSQNVA VANYINKWVE NNTNNLVKDL
VSPRDFDAAT YLALINAVYF KGNWKSQFRP ENTRTFSFTK DDESEVQIPM
MYQQGEFYYG EFSDGSNEAG GIYQVLEIPY EGDEISMMLV LSRQEVPLAT
LEPLVKAQLV EEWANSVKKQ KVEVYLPRFT VEQEIDLKDV LKALGITEIF
IKDANLTGLS DNKEIFLSKA IHKSFLEVNE EGSEAAAVSG MIAISRMAVL
YPQVIVDHPF FFLIRNRRTG TILFMGRVMH PETMNTSGHD FEEL.
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 :
NMT1 HumanDescription:
N-Myristoyltransferase 1 Human Recombinant
N-Myristoyltransferase 1, NMT, Myristoyl-CoA:Protein N-Myristoyltransferase 1, Type I N-Myristoyltransferase, EC 2.3.1.97, Myristoyl-CoA:Protein,N- Myristoyltransferase, Glycylpeptide N-Tetradecanoyltransferase 1,Peptide N-Myristoyltransferase 1,Alternative, Short Form NMT-S, Short Form NMT-S,Long Form, NMT-L, Alternative, Long Form, NMT-L, NMT 1.
Product # :
ENZ-842Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NMT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 519 amino acids (1-496 a.a) and having a molecular mass of 59.2kDa.NMT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NMT1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4).
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Myristate, a rare 14-carbon saturated fatty acid, is co-translationally attached by an amide linkage to the N-terminal glycine residue of cellular & viral proteins with various functions. N-Myristoyltransferase 1, also known as NMT1 catalyzes the transfer of myristate from CoA to proteins. NMT1 seems to be irreversible and is essential for full expression of the biologic activities of several N-myristoylated proteins, as well as the alpha subunit of the signal-transducing guanine nucleotide-binding protein, G protein.
-
Synonyms
N-Myristoyltransferase 1, NMT, Myristoyl-CoA:Protein N-Myristoyltransferase 1, Type I N-Myristoyltransferase, EC 2.3.1.97, Myristoyl-CoA:Protein,N- Myristoyltransferase, Glycylpeptide N-Tetradecanoyltransferase 1,Peptide N-Myristoyltransferase 1,Alternative, Short Form NMT-S, Short Form NMT-S,Long Form, NMT-L, Alternative, Long Form, NMT-L, NMT 1.
-
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 MGSMADESET AVKPPAPPLP QMMEGNGNGH EHCSDCENEE DNSYNRGGLS PANDTGAKKK KKKQKKKKEK GSETDSAQDQ PVKMNSLPAE RIQEIQKAIE LFSVGQGPAK TMEEASKRSY QFWDTQPVPK LGEVVNTHGP VEPDKDNIRQ EPYTLPQGFT WDALDLGDRG VLKELYTLLN ENYVEDDDNM FRFDYSPEFL LWALRPPGWL PQWHCGVRVV SSRKLVGFIS AIPANIHIYD TEKKMVEINF LCVHKKLRSK RVAPVLIREI TRRVHLEGIF QAVYTAGVVL PKPVGTCRYW HRSLNPRKLI EVKFSHLSRN MTMQRTMKLY RLPETPKTAG LRPMETKDIP VVHQLLTRYL KQFHLTPVMS QEEVEHWFYP QENIIDTFVV ENANGEVTDF LSFYTLPSTI MNHPTHKSLK AAYSFYNVHT QTPLLDLMSD ALVLAKMKGF DVFNALDLME NKTFLEKLKF GIGDGNLQYY LYNWKCPSMG AEKVGLVLQ.
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 :
NMT2 HumanDescription:
N-Myristoyltransferase 2 Human Recombinant
Glycylpeptide N-tetradecanoyltransferase 2, Myristoyl-CoA:protein N-myristoyltransferase 2, NMT 2, Peptide N-myristoyltransferase 2, Type II N-myristoyltransferase, NMT2.
Product # :
ENZ-068Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NMT2 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 518 amino acids (1-498 a.a.) and having a molecular mass of 59.1kDa. The NMT2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NMT2 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Glycylpeptide N-tetradecan-oyltransferases 2 (NMT2) is a cytoplasmic protein which is a member of the NMT family of proteins. The proteins in the NMT family catalyze the addition of a myristoyl group to the N-terminal glycine residue of eukaryotic, fungal and viral proteins. These proteins are mostly detected in the heart, gut, kidney, liver and placenta. NMT catalyzes the reaction of N-terminal myristoylation of various signaling proteins. NMT transfers myristic acid from myristoyl coenzyme A to the amino group of a protein's N-terminal glycine residue. There are several distinct NMTs which vary in the molecular weight and /or subcellular distribution.
-
Synonyms
Glycylpeptide N-tetradecanoyltransferase 2, Myristoyl-CoA:protein N-myristoyltransferase 2, NMT 2, Peptide N-myristoyltransferase 2, Type II N-myristoyltransferase, NMT2.
-
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).Please prevent freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAEDSESAAS QQSLELDDQD TCGIDGDNEE ETEHAKGSPG GYLGAKKKKK KQKRKKEKPN SGGTKSDSAS DSQEIKIQQP SKNPSVPMQK LQDIQRAMEL LSACQGPARN IDEAAKHRYQ FWDTQPVPKL DEVITSHGAI EPDKDNVRQE PYSLPQGFMW DTLDLSDAEV LKELYTLLNE NYVEDDDNMF RFDYSPEFLL WALRPPGWLL QWHCGVRVSS NKKLVGFISA IPANIRIYDS VKKMVEINFL CVHKKLRSKR VAPVLIREIT RRVNLEGIFQ AVYTAGVVLP KPIATCRYWH RSLNPKKLVE VKFSHLSRNM TLQRTMKLYR LPDVTKTSGL RPMEPKDIKS VRELINTYLK QFHLAPVMDE EEVAHWFLPR EHIIDTFVVE SPNGKLTDFL SFYTLPSTVM HHPAHKSLKA AYSFYNIHTE TPLLDLMSDA LILAKSKGFD VFNALDLMEN KTFLEKLKFG IGDGNLQYYL YNWRCPGTDS EKVGLVLQ.
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 :
AZGP1Description:
Alpha-2-Glycoprotein 1 Zinc-Binding Human Recombinant
Zinc-alpha-2-glycoprotein, ZA2G, ZAG, Zn-alpha-2-GP, Zn-alpha-2-glycoprotein.
Product # :
PRO-2169Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
AZGP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 301 amino acids (21-298 a.a) and having a molecular mass of 34.5kDa.AZGP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AZGP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Zinc-alpha-2-glycoprotein (AZGP1) protein stimulates lipid degradation in adipocytes and causes the massive fat losses linked with various advanced cancers. AZGP1 may bind polyunsaturated fatty acids.
-
Synonyms
Zinc-alpha-2-glycoprotein, ZA2G, ZAG, Zn-alpha-2-GP, Zn-alpha-2-glycoprotein.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQENQDGR YSLTYIYTGL SKHVEDVPAF QALGSLNDLQ FFRYNSKDRK SQPMGLWRQV EGMEDWKQDS QLQKAREDIF METLKDIVEY YNDSNGSHVL QGRFGCEIEN NRSSGAFWKY YYDGKDYIEF NKEIPAWVPF DPAAQITKQK WEAEPVYVQR AKAYLEEECP ATLRKYLKYS KNILDRQDPP SVVVTSHQAP GEKKKLKCLA YDFYPGKIDV HWTRAGEVQE PELRGDVLHN GNGTYQSWVV VAVPPQDTAP YSCHVQHSSL AQPLVVPWEA S.
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 :
EPHB4 HumanDescription:
EPH Receptor B4 Human Recombinant
Tyrosine-Protein Kinase TYRO11, Hepatoma Transmembrane Kinase, TYRO11, MYK1, HTK, Ephrin Type-B Receptor, Tyrosine-Protein Kinase Receptor HTK.
Product # :
PRO-2592Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
EPHB4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (16-539a.a.) and fused to an 8 aa His Tag at C-terminus containing a total of 532 amino acids and having a molecular mass of 58.1 kDa. EPHB4 shows multiple bands between 50-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EPHB4 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
EPHB4 or Ephrin type-B receptor 4 is encoded by the EPHB4 gene in humans. The receptor and its ligands (the ephrins) take part in different developmental stages, mainly in the nervous system. EPHB4 and other Ephrin receptors are the biggest subgroup of the RTK receptors. EPHB4 binds to ephrin B2 and has a crucial part in the development of the vascular system.
-
Synonyms
Tyrosine-Protein Kinase TYRO11, Hepatoma Transmembrane Kinase, TYRO11, MYK1, HTK, Ephrin Type-B Receptor, Tyrosine-Protein Kinase Receptor HTK.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
LEETLLNTKL ETADLKWVTF PQVDGQWEEL SGLDEEQHSV RTYEVCDVQR APGQAHWLRT GWVPRRGAVH VYATLRFTML ECLSLPRAGRSCKETFTVFY YESDADTATA LTPAWMENPY IKVDTVAAEH LTRKRPGAEA TGKVNVKTLR LGPLSKAGFY LAFQDQGACM ALLSLHLFYK KCAQLTVNLT RFPETVPREL VVPVAGSCVV DAVPAPGPSP SLYCREDGQW AEQPVTGCSC APGFEAAEGN TKCRACAQGT FKPLSGEGSC QPCPANSHSN TIGSAVCQCR VGYFRARTDP RGAPCTTPPS APRSVVSRLN GSSLHLEWSA PLESGGREDL TYALRCRECR PGGSCAPCGG DLTFDPGPRD LVEPWVVVRG LRPDFTYTFE VTALNGVSSL ATGPVPFEPV NVTTDREVPP AVSDIRVTRS SPSSLSLAWA VPRAPSGAVL DYEVKYHEKG AEGPSSVRFL KTSENRAELR GLKRGASYLV QVRARSEAGY GPFGQEHHSQ TQLDESEGWR EQLAVEHHHH HH.
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 :
CXCL8 Human, HisDescription:
Interleukin-8 (1-77 a.a) Human Recombinant (CXCL8), His Tag
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
Product # :
CHM-345Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Interleukin-8 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 77 amino acids fragment (23-99) and having a total molecular mass of 13.7kDa with an amino-terminal hexahistidine tag. The IL-8 His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL8 His is supplied in 10mM Tris-HCl pH 8, 250mM NaCl and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
-
Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
-
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.
-
Background
What is the molecular weight/Mw of CXCL8 HUMAN, HIS Protein?
CXCL8 HUMAN, HIS Protein has a total Mw of 13.7kDa.
What is the source or expression system of CXCL8 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL8 HUMAN, HIS Protein?
CXCL8 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 HUMAN, HIS Protein?
The biological functionality of CXCL8 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL8 HUMAN, HIS Protein?
CXCL8 HUMAN, HIS Protein is composed from 77 amino acids.
What applications can CXCL8 HUMAN, HIS Protein be used in?
CXCL8 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL8 HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TGIF2LX HumanDescription:
TGFB-Induced Factor Homeobox 2-Like, X-Linked Human Recombinant
Homeobox protein TGIF2LX, TGF-beta-induced transcription factor 2-like protein, TGFB-induced factor 2-like protein, X-linked, TGIF-like on the X, TGIF2LX, TGIFLX, TGFB-Induced Factor Homeobox 2-Like, X-Linked.
Product # :
PRO-1902Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TGIF2LX Human Recombinant produced in E. coli is. a single polypeptide chain containing 264 amino acids (1-241) and having a molecular mass of 29.1kDa.TGIF2LX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TGIF2LX solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
TGFB-Induced Factor Homeobox 2-Like, X-Linked (TGIF2LX) belongs to the TALE/TGIF homeobox family of transcription factors and takes part in spermatogenesis. A homolog of TGIF2LX is located in the male specific region of chromosome Y, in a block of sequence which is the outcome of a large X-to-Y transposition.
-
Synonyms
Homeobox protein TGIF2LX, TGF-beta-induced transcription factor 2-like protein,
TGFB-induced factor 2-like protein, X-linked, TGIF-like on the X, TGIF2LX, TGIFLX, TGFB-Induced Factor Homeobox 2-Like, X-Linked. -
Physical Appearance
Sterile Filtered clear solution.
-
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 MGSMEAAADG PAETQSPVEK DSPAKTQSPA QDTSIMSRNN ADTGRVLALP EHKKKRKGNL PAESVKILRD WMYKHRFKAY PSEEEKQMLS EKTNLSLLQI SNWFINARRR ILPDMLQQRR NDPIIGHKTG KDAHATHLQS TEASVPAKSG PSGPDNVQSL PLWPLPKGQM SREKQPDPES APSQKLTGIA QPKKKVKVSV TSPSSPELVS PEEHADFSSF LLLVDAAVQR AAELELEKKQ EPNP.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CLTA HumanDescription:
Clathrin, Light Chain A Human Recombinant
Clathrin light chain A, Lca, CLTA.
Product # :
PRO-1144Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CLTA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 242 amino acids (1-218 a.a) and having a molecular mass of 26.2kDa (Molecular weight on SDS-PAGE will appear higher).CLTA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CLTA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Clathrin, light chain A (CLTA) is a member of the clathrin family. Clathrin, which is a large, soluble protein, is comprised of heavy and light chains. CLTA is one of 2 clathrin light chain proteins which are supposed to function as regulatory elements. CLTA is a key cytosolic coat protein in pits and vesicles originating from the plasma membrane and the trans-Golgi network. In receptor-mediated endocytosis, receptor proteins are encapsulated by Clathrin-coated vesicles.
-
Synonyms
Clathrin light chain A, Lca, CLTA.
-
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 MGSHMAELDP FGAPAGAPGG PALGNGVAGA GEEDPAAAFL AQQESEIAGI ENDEAFAILD GGAPGPQPHG EPPGGPDAVD GVMNGEYYQE SNGPTDSYAA ISQVDRLQSE PESIRKWREE QMERLEALDA NSRKQEAEWK EKAIKELEEW YARQDEQLQK
TKANNRAAEE AFVNDIDESS PGTEWERVAR LCDFNPKSSK QAKDVSRMRS VLISLKQAPL VH.
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 :
RLN2 HumanDescription:
Relaxin-2 Human Recombinant
Prorelaxin H2, RLN2, H2, RLXH2, H2-RLX, bA12D24.1.1, bA12D24.1.2.
Product # :
PRO-1327Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
RLN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids (25-185 a.a) and having a molecular mass of 20.7kDa.RLN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RLN2 protein solution (1mg/ml) containing 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
-
Introduction
Prorelaxin H2 (RLN2) is a member of a family which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. It may also have other roles in boosting sperm motility, regulating blood pressure, controlling heart rate and releasing vasopressin. RLN2 is a peptide hormone linked to several therapeutically relevant physiological effects, including regulation of collagen metabolism and multiple vascular control pathways. The active form of the RLN2 protein consists of an A chain and a B chain linked by disulfide bonds.
-
Synonyms
Prorelaxin H2, RLN2, H2, RLXH2, H2-RLX, bA12D24.1.1, bA12D24.1.2.
-
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 MGSDSWMEEV IKLCGRELVR AQIAICGMST WSKRSLSQED APQTPRPVAE IVPSFINKDT ETINMMSEFV ANLPQELKLT LSEMQPALPQ LQQHVPVLKD SSLLFEEFKK LIRNRQSEAA DSSPSELKYL GLDTHSRKKR QLYSALANKC CHVGCTKRSL ARFC.
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 :
IpamorelinDescription:
Ipamorelin
Ipamorelin
Product # :
HOR-024Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
Ipamorelin Synthetic is a single, non-glycosylated polypeptide chain containing 4 amino acids, having a molecular mass of 711.85 Dalton and a Molecular formula of C38H49N9O5.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
-
Introduction
Ipamorelin is a peptide selective agonist of the ghrelin/growth hormone secretagogue receptor and a growth hormone secretagogue. Ipamorelin is a pentapeptide that was derived from GHRP1. Ipamorelin significantly increases plasma growth hormone levels in both animals and humans. Like pralmorelin and GHRP-6, ipamorelin does not affect prolactin, FSH, LH or TSH levels. However, unlike GHRP2 and GHRP6, but as growth hormone-releasing hormone (GHRH), ipamorelin does not stimulate the secretion of adrenocorticotropic hormone (ACTH) or cortisol, and is highly selective for inducing the secretion only of GH.
-
Synonyms
Ipamorelin
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Ipamorelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Ipamorelin 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.
-
Solubility
It is recommended to reconstitute the lyophilized Ipamorelin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
Aib-His-D-2-Nal-D-Phe-Lys-NH2.
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 :
IFNA1 HumanDescription:
IFN-Alpha 1 Human Recombinant
IFNA1, IFN-alpha 1, IFN -a.
Product # :
CYT-291Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- SDS-PAGE
Description
IFNA1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 167 amino acids (24-189) and having a molecular mass of 19.5 kDa. The IFN-alpha 1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1mg/ml in phosphate-buffered saline (PBS), pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
-
Introduction
IFNs are cytokines that are widely known to induce potent anti-viral activity. IFN-a exerts a variety of other biological effects, including antitumor and immunomodulatory activities and are increasingly used clinically to treat a range of malignancies, myelodysplasias and autoimmune diseases.
-
Synonyms
IFNA1, IFN-alpha 1, IFN -a.
-
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
MCDLPETHSL DNRRTLMLLA QMSRISPSSC LMDRHDFGFP QEEFDGNQFQ KAPAISVLHE LIQQIFNLFT TKDSSAAWDE DLLDKFCTEL YQQLNDLEAC VMQEERVGET PLMNVDSILA VKKYFRRITL YLTEKKYSPC AWEVVRAEIM RSLSLSTNLQ ERLRRKE.
-
Background
What is the molecular weight/Mw of IFNA1 HUMAN Protein?
IFNA1 HUMAN Protein has a total Mw of 19.5kDa.
What is the source or expression system of IFNA1 HUMAN Protein?
Escherichia Coli.
What is the Purity of IFNA1 HUMAN Protein?
IFNA1 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNA1 HUMAN Protein?
The biological functionality of IFNA1 HUMAN Protein will be determined in the future.
What is the amino acid sequence of IFNA1 HUMAN Protein?
MCDLPETHSL DNRRTLMLLA QMSRISPSSC LMDRHDFGFP QEEFDGNQFQ KAPAISVLHE LIQQIFNLFT TKDSSAAWDE DLLDKFCTEL YQQLNDLEAC VMQEERVGET PLMNVDSILA VKKYFRRITL YLTEKKYSPC AWEVVRAEIM RSLSLSTNLQ ERLRRKE.
What applications can IFNA1 HUMAN Protein be used in?
IFNA1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNA1 HUMAN Protein?
The endotoxin level is minimal, IFNA1 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.