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1000 results found for “igfbp”
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Name :
FABP1 HumanDescription:
Fatty Acid Binding Protein-1 Human Recombinant
Fatty acid-binding protein 1 liver, L-FABP, FABPL, FABP-1, FABP1, Z-protein.
Product # :
PRO-1593Price :
Quantity :
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Shipped at Room temp
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Description
FABP1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a total molecular mass of 14.2kDa (calculated).
Source
Escherichia Coli.
Formulation
Filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20mM TRIS and 50mM NaCl, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
FABP1 (Fatty acid binding protein1) encodes the fatty acid binding protein found in liver. FABP1 is composed of ten antiparallel beta strands that form a barrel with a bigger binding pocket than the other FABPs allowing it to accommodate two fatty acid. This protein binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm; it may be involved in intracellular lipid transport and metabolism.
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Synonyms
Fatty acid-binding protein 1 liver, L-FABP, FABPL, FABP-1, FABP1, Z-protein.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. FABP1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MSFSGKYQLQ SQENFEAFMK AIGLPEELIQ KGKDIKGVSE IVQNGKHFKF TITAGSKVIQ NEFTVGEECE LETMTGEKVK TVVQLEGDNK LVTTFKNIKS VTELNGDIIT NTMTLGDIVF KRISKRI.
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 :
GADD45B HumanDescription:
Growth Arrest and DNA-Damage-Inducible Beta Human Recombinant
MYD118, GADD45BETA, GADD45B, Growth arrest and DNA-damage-inducible protein GADD45 beta, Myeloid differentiation primary response protein MyD118, Negative growth regulatory protein MyD118, DKFZp566B133.
Product # :
PRO-563Price :
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Shipped with Ice Packs
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Description
GADD45B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 160 amino acids and having a molecular mass of 17.8 kDa.
Source
Escherichia Coli.
Formulation
The GADD45B protein solution contains 20mM Tris-HCl pH-7.5 and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GADD45B is part of the nuclear proteins to interact with various proteins whose transcript levels are raised after stressful growth arrest conditions and treatment with DNA-damaging agents. GADD45B reacts to environmental stresses by mediating activation of the p38/JNK pathway which is mediated through their protein binding and activating MTK1/MEKK4 kinase, which is an upstream activator of both p38 and JNK MAPKs. GADD45B is involved in the regulation of growth and apoptosis. GADD45b takes part during chondrocyte terminal differentiation and mediates MMP-13 gene expression. GADD45 in B cells is induced by CD40 via a mechanism that involves NF-kappa B and that induction suppresses Fas-mediated killing. GADD45b is down-regulated in most cases of hepatocellular carcinoma (HCC), and is a molecular marker in the diagnosis of HCC and as a possible therapeutic target.
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Synonyms
MYD118, GADD45BETA, GADD45B, Growth arrest and DNA-damage-inducible protein GADD45 beta, Myeloid differentiation primary response protein MyD118, Negative growth regulatory protein MyD118, DKFZp566B133.
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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
MTLEELVACD NAAQKMQTVT AAVEELLVAA QRQDRLTVGV YESAKLMNVD PDSVVLCLLA IDEEEEDDIA LQIHFTLIQS FCCDNDINIV
RVSGMQRLAQ LLGEPAETQG TTEARDLHCL LVTNPHTDAW KSHGLVEVAS YCEESRGNNQ WVPYISLQER.
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 :
PPIF HumanDescription:
Cyclophilin-F Human Recombinant
Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.
Product # :
ENZ-385Price :
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Shipped with Ice Packs
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Description
PPIF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 198 amino acids (30-207) and having a molecular mass of 21 kDa. The PPIF is fused to a 20 amino acid His tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PPIF solution containing 20mM Tris-HCl pH-7.5, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 250 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.Citations
More Info
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Introduction
PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.
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Synonyms
Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.
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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 CSKGSGDPSS SSSSGNPLVY LDVDANGKPL GRVVLELKAD VVPKTAENFR ALCTGEKGFG YKGSTFHRVI PSFMCQAGDF TNHNGTGGKS IYGSRFPDEN FTLKHVGPGV LSMANAGPNT NGSQFFICTI KTDWLDGKHV VFGHVKEGMD VVKKIESFGS KSGRTSKKIV ITDCGQLS.
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 :
CEBP Gamma HumanDescription:
CCAAT/enhancer binding protein C/EBP Gamma Recombinant Human
CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-1.
Product # :
PRO-434Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CEBP-g Recombinant Human His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 146 (aa 39-147) and having a molecular mass of 16.5 kDa. The DNA binding domain of CEBP-g was purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein contains 20mM Tris-HCl pH7.5, 0.1M NaCl and 5mM b-Mercaptoethanol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CCAAT/enhancer binding protein(C/EBP) g is a family of transcription factors all contain a highly conserved, basic-leucine zipper domain at the C-terminus that is involved in dimerization and DNA binding. C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP family consist of several related proteins, C/EBP a,b,g,d, that form homodimers and/or form heterodimers with each other. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein; a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. C/EBP g may cooperate with Fos to bind PRE- enhancer elements.
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Synonyms
CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMPGG GGKAVAPSKQ SKKSSPMDRN SDEYRQRRER NNMAVKKSRL KSKQKAQDTL QRVNQLKEEN ERLEAKIKLL TKELSVLKDL FLEHAHNLAD NVQSISTENT TADGDN.
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 :
NPPA HumanDescription:
Natriuretic Peptide A Human Recombinant
Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.
Product # :
CYT-1028Price :
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Shipped at Room temp
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Description
NPPA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 26-123) containing 106 amino acids including an 8 a.a N-terminal His tag. The total molecular mass is 11.7kDa (calculated).
Source
Escherichia Coli.
Formulation
NPPA filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer, 50 mM NaCl and 5% w/v trehalosa, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Natriuretic Peptide A (NPPA) is a part of the natriuretic peptide family and is involved in cardiovascular homeostasis through regulation of natriuresis, diuresis, and vasodilation. NPPA is synthesized as a great precursor which releases a peptide from the N-terminus with similarity to vasoactive peptide, cardiodilatin, and another peptide from the C-terminus with natriuretic-diuretic activity. In female pregnancy, NPPA is promoting trophoblast invasion and spiral artery remodeling in uterus.
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Synonyms
Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. NPPA is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHNP MYNAVSNADL MDFKNLLDHL EEKMPLEDEV VPPQVLSEPN EEAGAALSPL PEVPPWTGEV SPAQRDGGAL GRGPWDSSDR SALLKSKLRA LLTAPR.
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 :
IL6 Mouse, Sf9Description:
Interleukin-6 Mouse Recombinant, Sf9
Interleukin-6, IL-6, B-cell hybridoma growth factor, Interleukin HP-1.
Product # :
CYT-904Price :
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Shipped with Ice Packs
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Description
Interleukin-6 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 193 amino acids (25-211a.a.) and having a molecular mass of 22.5kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). IL6 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL 6 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using M-NFS-60 mouse B cell. The ED50 for this effect is less or equal to 0.1 ng/ml.
SDS-PAGE
Citations
More Info
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Introduction
Il-6 is a cytokine with a wide variety of biological functions: it plays an essential role in the final differentiation of b-cells into ig-secreting cells, it induces myeloma and plasmacytoma growth, it induces nerve cells differentiation, in hepatocytes it induces acute phase reactants.
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Synonyms
Interleukin-6, IL-6, B-cell hybridoma growth factor, Interleukin HP-1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
FPTSQVRRGD FTEDTTPNRP VYTTSQVGGL ITHVLWEIVE MRKELCNGNS DCMNNDDALA ENNLKLPEIQ RNDGCYQTGY NQEICLLKIS SGLLEYHSYL EYMKNNLKDN KKDKARVLQR DTETLIHIFN QEVKDLHKIV LPTPISNALL TDKLESQKEW LRTKTIQFIL KSLEEFLKVT LRSTRQTHHH HHH.
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Background
Research Paper on Interleukin-6 Mouse Recombinant, Sf9
Abstract:
Exploring Interleukin-6 Mouse Recombinant, Sf9, a fascinating research topic! This paper provides an extensive description of Interleukin-6 (IL-6) Mouse Recombinant expressed in Sf9 insect cells. We delve into the molecular properties of IL-6, its significance in immune responses and inflammation, and its synonyms, including DIF, TNFA, and TNFSF2. Join us as we uncover the potential applications of IL-6 research using this novel recombinant mouse protein.
Introduction:
Introducing Interleukin-6 Mouse Recombinant, Sf9. This paper sheds light on the production and characteristics of IL-6 expressed in Sf9 insect cells. As researchers, we are intrigued by the versatility and applications of this recombinant protein in immunological studies.
An Extensive Description of Interleukin-6 Mouse Recombinant:
We present a comprehensive overview of Interleukin-6 Mouse Recombinant, focusing on its structure and functions. This recombinant protein enables us to explore IL-6's role in various cellular processes, making it a valuable tool for investigating immune regulation.
Significance in Immune Responses:
Marvel at IL-6's critical role in orchestrating immune responses! As a key cytokine, IL-6 plays a central role in immune cell activation and the regulation of inflammatory processes. Its pleiotropic effects contribute to maintaining homeostasis in the immune system.
Interactions and Synonyms:
Learn about the synonyms associated with IL-6, such as DIF, TNFA, and TNFSF2. Understanding these synonyms enhances our understanding of the interconnectedness of cytokine signaling. The complex interactions between IL-6 and other molecules further enrich our knowledge of immune responses.
Potential Applications in Immunological Research:
Explore the wide range of applications of Interleukin-6 Mouse Recombinant in immunological studies. From cell-based assays to therapeutic developments, this recombinant protein offers novel avenues for advancing immunology research. It serves as a valuable tool in deciphering the intricate immune system functions.
Novel Production Method using Sf9 Insect Cells:
Discover the innovative use of Sf9 insect cells for producing Interleukin-6. This expression system provides a scalable and efficient approach for obtaining large quantities of functional IL-6. The use of Sf9 cells opens up possibilities for large-scale protein production and downstream applications.
Conclusion:
Concluding our exploration of Interleukin-6 Mouse Recombinant, Sf9, we recognize its significance in immunological research. The extensive description of this recombinant protein broadens our understanding of IL-6 biology and its potential applications in various fields. As researchers, we are excited about the potential discoveries that lie ahead with the help of this valuable tool.
What is the molecular weight/Mw of IL6 MOUSE, SF9 Protein?
IL6 MOUSE, SF9 Protein has a total Mw of 22.5kDa.
What is the source or expression system of IL6 MOUSE, SF9 Protein?
Sf9, Baculovirus cells.
What is the Purity of IL6 MOUSE, SF9 Protein?
IL6 MOUSE, SF9 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IL6 MOUSE, SF9 Protein?
Measured in a cell proliferation assay using M-NFS-60 mouse B cell. The ED50 for this effect is less or equal to 0.1 ng/ml.
What is the amino acid sequence of IL6 MOUSE, SF9 Protein?
FPTSQVRRGD FTEDTTPNRP VYTTSQVGGL ITHVLWEIVE MRKELCNGNS DCMNNDDALA ENNLKLPEIQ RNDGCYQTGY NQEICLLKIS SGLLEYHSYL EYMKNNLKDN KKDKARVLQR DTETLIHIFN QEVKDLHKIV LPTPISNALL TDKLESQKEW LRTKTIQFIL KSLEEFLKVT LRSTRQTHHH HHH.
What applications can IL6 MOUSE, SF9 Protein be used in?
IL6 MOUSE, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL6 MOUSE, SF9 Protein?
The endotoxin level is minimal, IL6 MOUSE, SF9 Protein was purified using conventional chromatography techniques.
Who supplies recombinant IL6 MOUSE, SF9 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of IL6 MOUSE, SF9?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
AAGAB HumanDescription:
Alpha & Gamma-Adaptin Binding Protein Human Recombinant
P34, Alpha- and gamma-adaptin-binding protein p34.
Product # :
PRO-1479Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AAGAB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-315 a.a.) and having a molecular mass of 36.7kDa.AAGAB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AAGAB protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Alpha & Gamma-Adaptin Binding Protein (AAGAB), which is also known as P34, takes part in membrane traffic and interacts with AP1G1 and AP2A1.AAGAB is highly expressed in skin and keratinocytes, with the highest levels in adrenal gland, rectum and thymus.
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Synonyms
P34, Alpha- and gamma-adaptin-binding protein p34.
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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 MAAGVPCALV TSCSSVFSGD QLVQHILGTE DLIVEVTSND AVRFYPWTID NKYYSADINL CVVPNKFLVT AEIAESVQAF VVYFDSTQKS GLDSVSSWLP LAKAWLPEVM ILVCDRVSED GINRQKAQEW CIKHGFELVE LSPEELPEED DDFPESTGVK RIVQALNANV WSNVVMKNDR NQGFSLLNSL TGTNHSIGSA DPCHPEQPHL PAADSTESLS DHRGGASNTT DAQVDSIVDP MLDLDIQELA SLTTGGGDVE NFERLFSKLK EMKDKAATLP HEQRKVHAEK VAKAFWMAIG GDRDEIEGLS SDEEH.
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 :
CCL15 68 a.a HumanDescription:
Macrophage Inflammatory Protein-5 (68 a.a) Human Recombinant (CCL15)
Small inducible cytokine A15 precursor, CCL15, Macrophage inflammatory protein 5, MIP-5, MIP5, Chemokine CC-2, HCC-2, NCC-3, MIP- 1 delta, Leukotactin-1, LKN-1, Mrp-2b, C-C motif chemokine 15.
Product # :
CHM-011Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Macrophage Inflammatory Protein-5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a molecular mass of 7.4kDa. The MIP5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIP5 was lyophilized from a 0.2µm filtered concentrated solution containing PBS, pH-7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to chemoattract THP-1 human acute monocytic leukemia cells. The ED50 for this effect is typically 2-4ng/ml.Citations
More Info
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Introduction
CCL15, a new human CC chemokine, was isolated from a human fetal spleen cDNA library. CCL15 cDNA encodes a predicted 113 amino acid (aa) protein containing a putative signal peptide of 21 amino acids that is cleaved to generate a 92 aa residue mature protein. Within the CC family members, human CCL15 shares 45%, 44%, 35%, and 30% aa homology with mouse C10, human MPIF-1, human HCC-1, and mouse MIP-1?, respectively. The gene for MIP-5 is found on chromosome 17 where the genes for most of the human CC chemokines are located. Human CCL15 is expressed in T and B lymphocytes, NK cells, monocytes and monocyte-derived dendritic cells. Human MIP-5 is chemotactic for T cells and monocytes and has been shown to induce calcium flux in human CCR-1-transfected cells.
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Synonyms
Small inducible cytokine A15 precursor, CCL15, Macrophage inflammatory protein 5, MIP-5, MIP5, Chemokine CC-2, HCC-2, NCC-3, MIP- 1 delta, Leukotactin-1, LKN-1, Mrp-2b, C-C motif chemokine 15.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIP-5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL15 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 MIP5 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
SFHFAADCCT SYISQSIPCS LMKSYFETSS ECSKPGVIFL TKKGRQVCAK PSGPGVQDCM KKLKPYSI.
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Background
What is the molecular weight/Mw of CCL15 68 A.A HUMAN Protein?
CCL15 68 A.A HUMAN Protein has a total Mw of 7.4kDa.
What is the source or expression system of CCL15 68 A.A HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL15 68 A.A HUMAN Protein?
CCL15 68 A.A HUMAN Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL15 68 A.A HUMAN Protein?
Measured by its ability to chemoattract THP-1 human acute monocytic leukemia cells. The ED50 for this effect is typically 2-4ng/ml.
What is the amino acid sequence of CCL15 68 A.A HUMAN Protein?
SFHFAADCCT SYISQSIPCS LMKSYFETSS ECSKPGVIFL TKKGRQVCAK PSGPGVQDCM KKLKPYSI.
What applications can CCL15 68 A.A HUMAN Protein be used in?
CCL15 68 A.A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL15 68 A.A HUMAN Protein?
The endotoxin level is minimal, CCL15 68 A.A HUMAN Protein was purified using conventional chromatography techniques.Who supplies recombinant CCL15 68 A.A HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CCL15 68 A.A HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CINP HumanDescription:
Cyclin-Dependent Kinase 2 Interacting Protein Human Recombinant
Cyclin-dependent kinase 2 interacting protein, CDK2-interacting protein, MGC849.
Product # :
PKA-269Price :
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Shipped with Ice Packs
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Description
CINP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212) and having a molecular mass of 26.4 kDa.The CINP is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CINP protein (1mg/ml) is supplied in 20mM Tris-HCL, pH-8, 0.1M NaCl, 1mM DTT and 20% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CINP is a member of the CINP family. CINP cooperates with the components of the replication complex and 2 kinases, CDK2 and CDC7, to provide a working and physical link between CDK2 and CDC7 throughout the firing of the origins of replication.
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Synonyms
Cyclin-dependent kinase 2 interacting protein, CDK2-interacting protein, MGC849.
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Physical Appearance
CINP is supplied as a 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 MEAKTLGTVT PRKPVLSVSA RKIKDNAADW HNLILKWETL NDAGFTTANN IANLKISLLN KDKIELDSSS PASKENEEKV CLEYNEELEK LCEELQATLD GLTKIQVKME KLSSTTKGIC ELENYHYGEE SKRPPLFHTW PTTHFYEVSH KLLEMYRKEL LLKRTVAKEL AHTGDPDLTL SYLSMWLHQP YVESDSRLHL ESMLLETGHR AL
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 :
NXPH1 Human, Sf9Description:
Neurexophilin 1 Human Recombinant, Sf9
NXPH1, Nbla00697, NPH1 , Neurexophilin-1, Neurexophilin 1.
Product # :
PRO-2418Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NXPH1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 259 amino acids (22-271) and having a molecular mass of 29.7kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).NXPH1 is fused to 9 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
NXPH1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Neurexophilin 1 (NXPH1) is a part of the neurexophilin family which encodes a secreted protein with a variable N terminal domain, an extremely conserved, N-glycosylated central domain, a short linker region, and a cysteine-rich Cterminal domain. NXPH1 shapes a very tight complex with alpha neurexins, a group of proteins which promote adhesion among dendrites and axons.
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Synonyms
NXPH1, Nbla00697, NPH1 , Neurexophilin-1, Neurexophilin 1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPANLTNGG KSELLKSGSS KSTLKHIWTE SSKDLSISRL LSQTFRGKEN DTDLDLRYDT PEPYSEQDLW DWLRNSTDLQ EPRPRAKRRP IVKTGKFKKM FGWGDFHSNI KTVKLNLLIT GKIVDHGNGT FSVYFRHNST GQGNVSVSLV PPTKIVEFDL AQQTVIDAKD SKSFNCRIEY EKVDKATKNT LCNYDPSKTC YQEQTQSHVS WLCSKPFKVI CIYISFYSTD YKLVQKVCPD YNYHSDTPYF PSGHHHHHH.
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 :
IL36G 152 a.a. HumanDescription:
Interleukin-36 Gamma (152 a.a) Human Recombinant
Interleukin 36 gamma, IL1F9, interleukin 1 family member 9, Interleukin-1 epsilon, IL-1RP2, IL-1H1, IL1E, interleukin 1-related protein 2, Interleukin-1 homolog 1.
Product # :
CYT-161Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL36G (152 a.a.) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 152 amino acids and having a molecular mass of 17.0kDa.The IL36G (152 a.a.) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4, containing 5% trehalose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Fully biologically active when compared to standard. The ED50 as measured by its ability to induce IL-8 secretion in human preadipocytes is less than 15ng/ml, corresponding to a Specific Activity of 67,000 IU/mg.Citations
More Info
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Introduction
IL-36gamma belongs to the IL-1 family which includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36 Ra (IL-1F5), IL-36a (IL-1F6), IL-36b (IL-1F8), IL-37 (IL-1F7) and IL-1F10. ). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. IL-36g is an 18-22 kDa, 169aa intracellular and secreted protein which holds no signal sequence, no prosegment and no potential N-linked glycosylation sites. Human IL-36g shares 58%- 69% aa sequence homology with mouse, rat, bovine and equine IL-36g, and 23 - 57% aa sequence homology with other family members. The IL-36g receptor is a mixture of IL-1 Rrp2, mostly located in epithelia and keratinocytes, and the extensively expressed IL-1 RAcP. All IL-36 (a, b and g) activate N F-?B and MAPK pathways in an IL-1 Rrp2 dependent reaction. Additionally, IL-36g induces production of inflammatory cytokines and chemokines like CXCL8/IL-8.
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Synonyms
Interleukin 36 gamma, IL1F9, interleukin 1 family member 9, Interleukin-1 epsilon, IL-1RP2, IL-1H1, IL1E, interleukin 1-related protein 2, Interleukin-1 homolog 1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL36g Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL36g 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 IL36g in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SMCKPITGTI NDLNQQVWTL QGQNLVAVPR SDSVTPVTVA VITCKYPEAL EQGRGDPIYL GIQNPEMCLY CEKVGEQPTL QLKEQKIMDL YGQPEPVKPF LFYRAKTGRT STLESVAFPD WFIASSKRDQ PIILTSELGK SYNTAFELNI ND
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 :
EGF (1-51), HumanDescription:
Epidermal Growth Factor (1-51 a.a.)Human Recombinant
Urogastrone, URG, EGF.
Product # :
CYT-1115Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Epidermal Growth Factor (1-51 a.a.) Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 6.0kDa. The EGF is purified by proprietary chromatographic techniques.
Source
Saccharomyces cerevisiae
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 is determined by a cell proliferation assay using murine Balb/c 3T3 cells and is < than 0.1 ng/ml, corresponding to a specific activity of > 1.0 × 107 IU/mg.
Citations
More Info
-
Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of several epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
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Synonyms
Urogastrone, URG, EGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Epidermal Growth Factor 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 Epidermal Growth 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
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.
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Background
Exploring the Potential of Epidermal Growth Factor (1-51 a.a.) Human Recombinant: Novel Insights and Therapeutic Prospects
Abstract:
Epidermal Growth Factor (EGF) stands as a pivotal cytokine orchestrating essential cellular processes. This concise research paper delves into the unique realm of Epidermal Growth Factor (1-51 a.a.) Human Recombinant, unveiling its intricate molecular dynamics, signaling cascades, and therapeutic promise. Employing cutting-edge methodologies encompassing in vitro assays and animal models, this study elucidates the multifaceted cellular responses sparked by this truncated EGF variant, paving the way for potential clinical applications.
Introduction:
The truncated form of EGF, spanning amino acids 1 to 51 (a.a.), carries distinct attributes that set it apart from the full-length counterpart. This paper centers on exploring the intriguing dimensions of Epidermal Growth Factor (1-51 a.a.) Human Recombinant, offering new insights into its interactions and potential utility.
Molecular Insights and Signaling Dynamics:
At the heart of its function lies the interplay between EGF (1-51 a.a.) and the epidermal growth factor receptor (EGFR). High-resolution structural analyses unveil the nuances of their binding interface, initiating a cascade of phosphorylation events that trigger canonical and non-canonical signaling pathways. The MAPK pathway and the PI3K/Akt pathway, intricately modulated by EGF (1-51 a.a.), propel cellular processes like proliferation, migration, and evasion of apoptosis.
In Vitro Profiling and Cellular Responses:
In dissecting the cellular responses, diverse in vitro assays have been employed. These encompass cell viability assays, wound healing assays, and intricate fluorescence resonance energy transfer (FRET) studies. These assays converge to illuminate the dynamic orchestration of EGF-induced cellular behaviors, showcasing its role in promoting cellular migration, division, and wound closure.
In Vivo Implications and Therapeutic Horizons:
Translating these insights into tangible therapeutic possibilities, in vivo studies present a compelling narrative. In animal models, EGF (1-51 a.a.) emerges as a potent player in cutaneous wound healing, fostering accelerated tissue regeneration. Moreover, its potential extends to oncology, as it not only influences tumor microenvironments but also demonstrates anti-apoptotic effects, hinting at its role in tailored cancer interventions.
Future Prospects and Challenges:
While these discoveries hold immense promise, challenges persist. The intricate network of signaling events demands further scrutiny, considering potential cross-talk and off-target effects. Refining delivery mechanisms and dosing regimens is essential for realizing the clinical potential of EGF (1-51 a.a.).
Conclusion:
In a synthesis of complex molecular insights and tangible therapeutic potential, Epidermal Growth Factor (1-51 a.a.) Human Recombinant emerges as a captivating subject. Its truncated structure and distinctive signaling cascades paint a canvas of cellular orchestration. As research advances, harnessing its therapeutic benefits could usher in novel interventions for wound healing and cancer therapy.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6kDa.
What is the source or expression system of EGF Protein?
Saccharomyces cerevisiae
What is the Purity of EGF Protein?
EGF Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF Protein?
The ED50 is determined by a cell proliferation assay using murine Balb/c 3T3 cells and is < than 0.1 ng/ml, corresponding to a specific activity of > 1.0 × 107 IU/mg.
What is the amino acid sequence of EGF Protein?
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.
What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, 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.
- View Data Sheet
Name :
IL17RA HumanDescription:
Interleukin-17 Receptor Alpha Human Recombinant
Interleukin 17 Receptor A, IL-17 Receptor A, IL-17RA, CDw217, IL17R, Interleukin-17 Receptor A, Interleukin 17 Receptor, CD217 Antigen, HIL-17R, CANDF5, CD217, IMD51.
Product # :
CYT-1023Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IL17RA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 527 amino acids (33-320) and having a molecular mass of 60.4kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). IL17RA is fused to a 239 amino acids hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL17RA protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Interleukin-17 receptor A isoform 1 (IL17RA) is a cytokine receptor which binds interleukin 17. IL17RA is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL17RA is a type 1 membrane glycoprotein which binds with low affinity to interleukin 17A. The IL17RA protein and Interleukin 17A has a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis.
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Synonyms
Interleukin 17 Receptor A, IL-17 Receptor A, IL-17RA, CDw217, IL17R, Interleukin-17 Receptor A, Interleukin 17 Receptor, CD217 Antigen, HIL-17R, CANDF5, CD217, IMD51.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
LRLLDHRALV CSQPGLNCTV KNSTCLDDSW IHPRNLTPSS PKDLQIQLHF AHTQQGDLFP VAHIEWTLQT DASILYLEGA ELSVLQLNTN ERLCVRFEFL SKLRHHHRRW RFTFSHFVVD PDQEYEVTVH HLPKPIPDGD PNHQSKNFLV PDCEHARMKV TTPCMSSGSL WDPNITVETL EAHQLRVSFT LWNESTHYQI LLTSFPHMEN HSCFEHMHHI PAPRPEEFHQ RSNVTLTLRN LKGCCRHQVQ IQPFFSSCLN DCLRHSATVS CPEMPDTPEP IPDYMPLWVE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.
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 :
NT 3 HumanDescription:
Neurotrophin-3 Human Recombinant
Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.
Product # :
CYT-257Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Neurotrophin-3 Human Recombinant produced in E.Coli is a non-glycosylated and non-covalently linked homodimer, containing 2x120 amino acid chains, having a total Mw of 27.5 kDa. The NT-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from 0.1% TFA.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependent proliferation of neuroblastoma cell line expressing BR6 is 3.49 ng/ml.
Citations
More Info
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Introduction
NT3 a member of the neurotrophin family, that controls survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NTF3-deficient mice generated by gene targeting display severe movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse.
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Synonyms
Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NGF-2 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 Neurotrophin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MYAEHKSHRGE YSVCDSESLW VTDKSSAIDI RGHQVTVLGE IKTGNSPVKQ YFYETRCKEA RPVKNGCRGI DDKHWNSQCK TSQTYVRALT SENNKLVGWR WIRIDTSCVC ALSRKIGRT.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 2.165 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of NT-3 as a Reference Standard.
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 :
LGALS8 Human, HisDescription:
Galectin-8 Human Recombinant, His Tag
Gal-8, PCTA1, Po66-CBP, Prostate carcinoma tumor antigen 1.
Product # :
CYT-727Price :
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Shipped with Ice Packs
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Description
LGALS8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 337 amino acids (1-317 a.a.) and having a molecular mass of 37.9 kDa. The LGALS8 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Galectin-8 His tag 0.5mg/ml protein solution contains 20mM Tris-HCl pH-8, 0.1M NaCl, 10% glycerol & 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 for this effect is 5–10ug/ml. Measured by its ability to agglutinate human red blood cells corresponding to a specific activity of 100-200IU/mg.SDS-PAGE
Citations
More Info
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Introduction
LGALS8 is a prostate-specific antigen that is solely overexpressed in malignant tumors and thus is a supplementary specific identifier of malignancies. LGALS8 is part of the galectin gene family which facilitates both cell-cell and cell matrix interactions in a method parallel to the selectin subgroup of C-type lectins.
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Synonyms
Gal-8, PCTA1, Po66-CBP, Prostate carcinoma tumor antigen 1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MMLSLNNLQN IIYNPVIPFV GTIPDQLDPG TLIVIRGHVP SDADRFQVDL QNGSSMKPRA DVAFHFNPRF
KRAGCIVCNT LINEKWGREE ITYDTPFKRE KSFEIVIMVL KDKFQVAVNG KHTLLYGHRI GPEKIDTLGI YGKVNIHSIG FSFSSDLQST
QASSLELTEI SRENVPKSGT PQLRLPFAAR LNTPMGPGRT VVVKGEVNAN AKSFNVDLLA GKSKDIALHL NPRLNIKAFV RNSFLQESWG
EEERNITSFP FSPGMYFEMI IYCDVREFKV AVNGVHSLEY KHRFKELSSI DTLEINGDIH LLEVRSW. -
Background
What is the molecular weight/Mw of LGALS8 HUMAN, HIS Protein?
LGALS8 HUMAN, HIS Protein has a total Mw of 37.9kDa.
What is the source or expression system of LGALS8 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of LGALS8 HUMAN, HIS Protein?
LGALS8 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS8 HUMAN, HIS Protein?
The ED50 for this effect is 5–10ug/ml. Measured by its ability to agglutinate human red blood cells corresponding to a specific activity of 100-200IU/mg.What is the amino acid
sequence of LGALS8 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MMLSLNNLQN IIYNPVIPFV GTIPDQLDPG TLIVIRGHVP SDADRFQVDL QNGSSMKPRA DVAFHFNPRF
KRAGCIVCNT LINEKWGREE ITYDTPFKRE KSFEIVIMVL KDKFQVAVNG KHTLLYGHRI GPEKIDTLGI YGKVNIHSIG FSFSSDLQST
QASSLELTEI SRENVPKSGT PQLRLPFAAR LNTPMGPGRT VVVKGEVNAN AKSFNVDLLA GKSKDIALHL NPRLNIKAFV RNSFLQESWG
EEERNITSFP FSPGMYFEMI IYCDVREFKV AVNGVHSLEY KHRFKELSSI DTLEINGDIH LLEVRSW.
What applications can LGALS8 HUMAN, HIS Protein be used in?
LGALS8 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS8 HUMAN, HIS Protein?
The endotoxin level is minimal, LGALS8 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 :
IL5RA HumanDescription:
Interleukin-5 Receptor Alpha Human Recombinant
Interleukin 5 Receptor Subunit Alpha, Interleukin 5 Receptor, Alpha, IL-5 Receptor Subunit Alpha, IL-5R Subunit Alpha, CD125 Antigen, CDw125, IL5R, Interleukin-5 Receptor Subunit Alpha, Interleukin-5 Receptor Alpha Chain, Interleukin 5 Receptor Type 3, IL-5R-Alpha, HSIL5R3, IL-5RA, CD125, Interleukin-5 receptor subunit alpha, IL-5 receptor subunit alpha, IL-5R subunit alpha, IL-5R-alpha, IL-5RA.
Product # :
cyt-1067Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IL5RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 331 amino acids (21-342a.a.) and having a molecular mass of 37.8kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IL5RA is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL5RA protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Interleukin-5 receptor subunit alpha (Il5ra) regulates the development and function of eosinophils. The Il5ra protein is a therapeutic target for hypereosinophilic diseases including allergic inflammations and asthma. Oct2 enhances antibody-secreting cell differentiation via regulation of Il5ra chain expression on activated B cells.
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Synonyms
Interleukin 5 Receptor Subunit Alpha, Interleukin 5 Receptor, Alpha, IL-5 Receptor Subunit Alpha, IL-5R Subunit Alpha, CD125 Antigen, CDw125, IL5R, Interleukin-5 Receptor Subunit Alpha, Interleukin-5 Receptor Alpha Chain, Interleukin 5 Receptor Type 3, IL-5R-Alpha, HSIL5R3, IL-5RA, CD125, Interleukin-5 receptor subunit alpha, IL-5 receptor subunit alpha, IL-5R subunit alpha, IL-5R-alpha, IL-5RA.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPDLLPDEK ISLLPPVNFT IKVTGLAQVL LQWKPNPDQE QRNVNLEYQV KINAPKEDDY ETRITESKCV TILHKGFSAS VRTILQNDHS LLASSWASAE LHAPPGSPGT SIVNLTCTTN TTEDNYSRLR SYQVSLHCTW LVGTDAPEDT QYFLYYRYGS WTEECQEYSK DTLGRNIACW FPRTFILSKG RDWLAVLVNG SSKHSAIRPF DQLFALHAID QINPPLNVTA EIEGTRLSIQ WEKPVSAFPI HCFDYEVKIH NTRNGYLQIE KLMTNAFISI IDDLSKYDVQ VRAAVSSMCR EAGLWSEWSQ PIYVGNDEHK PLREWHHHHH H.
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Background
What is the molecular weight/Mw of IL 5 RA HUMAN Protein?
IL 5 RA HUMAN Protein has a total Mw of 37.8kDa.
What is the source or expression system of IL 5 RA HUMAN Protein?
Sf9, Baculovirus cells.
What is the Purity of IL 5 RA HUMAN Protein?
IL 5 RA HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IL 5 RA HUMAN Protein?
The biological functionality of IL 5 RA HUMAN Protein will be determined in the future.
What is the amino acid sequence of IL 5 RA HUMAN Protein?
ADPDLLPDEK ISLLPPVNFT IKVTGLAQVL LQWKPNPDQE QRNVNLEYQV KINAPKEDDY ETRITESKCV TILHKGFSAS VRTILQNDHS LLASSWASAE LHAPPGSPGT SIVNLTCTTN TTEDNYSRLR SYQVSLHCTW LVGTDAPEDT QYFLYYRYGS WTEECQEYSK DTLGRNIACW FPRTFILSKG RDWLAVLVNG SSKHSAIRPF DQLFALHAID QINPPLNVTA EIEGTRLSIQ WEKPVSAFPI HCFDYEVKIH NTRNGYLQIE KLMTNAFISI IDDLSKYDVQ VRAAVSSMCR EAGLWSEWSQ PIYVGNDEHK PLREWHHHHH H.
What applications can IL 5 RA HUMAN Protein be used in?
IL 5 RA HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL 5 RA HUMAN Protein?
The endotoxin level is minimal, IL 5 RA HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant IL 5 RA HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of IL 5 RA HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL 18 Mouse, HisDescription:
Interleukin-18 Mouse Recombinant, His Tag
Interferon-gamma-inducing factor, IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin, Il18.
Product # :
CYT-634Price :
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Description
Interleukin-18 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 178 amino acids (36-192 a.a.) and having a molecular mass of 20.4 kDa. The Mouse IL-18 is fused to a 20 amino acids His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Mouse IL-18 protein solution contains 20mM Tris-HCl pH-8 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
IL-18 is a proinflammatory cytokine. This cytokine can induce the IFN-gamma production of T cells. The combination of this cytokine and IL12 has been shown to inhibit IL4 dependent IgE and IgG1 production, and enhance IgG2a production of B cells. IL-18 binding protein (IL18BP) can specifically interact with this cytokine, and thus negatively regulate its biological activity.
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Synonyms
Interferon-gamma-inducing factor, IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin, Il18.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MNFGRLHCTT AVIRNINDQV LFVDKRQPVF EDMTDIDQSA SEPQTRLIIY MYKDSEVRGL AVTLSVKDSK MSTLSCKNKI ISFEEMDPPE NIDDIQSDLI FFQKRVPGHN KMEFESSLYE GHFLACQKED DAFKLILKKK DENGDKSVMF TLTNLHQS.
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 :
IL 33 Rat, HisDescription:
Interleukin-33 Rat Recombinant, His Tag
Interleukin-33, IL-33.
Product # :
CYT-906Price :
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Description
IL 33 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids (109-264 a.a) and having a molecular mass of 19.8kDa. IL 33 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL 33 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
nterleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.
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Synonyms
Interleukin-33, IL-33.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSIQGTSL LTESCALSTY NDQSVSFVLE NGCYVINVED CGKNQEKDKV LLRYYESSFP AQSGDGVDGK KLMVNMSPIK DTDIWLNAND KDYSVELQKG DVSPPDQAFF VLHKKSSDFV SFECKNLPGT YIGVKDNQLA LVEENDESCN NIMFKLSKM.
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 :
FOLR1 Human, Sf9Description:
Folate Receptor 1 Human Recombinant, sf9
Folate Receptor 1, Ovarian Tumor-Associated Antigen MOv18, Adult Folate-Binding Protein, Folate Receptor 1 (Adult), Folate Receptor Adult, Folate Receptor Alpha, KB Cells FBP, FR-Alpha, FOLR, FBP, Folate Binding Protein, FOLR1.
Product # :
PRO-2389Price :
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Description
FOLR1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 218 amino acids (26-234a.a.) and having a molecular mass of 25.6kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).FOLR1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
FOLR1 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.
Citations
More Info
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Introduction
Folate Receptor 1, also known as FOLR1, is a part of the folate receptor family whose members bind folic acid. FOLR1 binds to folate and reduced folic acid derivatives and facilitates transfer of 5-methyltetrahydrofolate and folate analogs into the cells. FOLR1 is either attaches to membranes through a glycosyl-phosphatidylinositol linkage or exists in a soluble form. FOLR1 is also needed for embryonic development and normal cell proliferation.
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Synonyms
Folate Receptor 1, Ovarian Tumor-Associated Antigen MOv18, Adult Folate-Binding Protein, Folate Receptor 1 (Adult), Folate Receptor Adult, Folate Receptor Alpha, KB Cells FBP, FR-Alpha, FOLR, FBP, Folate Binding Protein, FOLR1.
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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
ADLIAWARTE LLNVCMNAKH HKEKPGPEDK LHEQCRPWRK NACCSTNTSQ EAHKDVSYLY RFNWNHCGEM APACKRHFIQ DTCLYECSPN LGPWIQQVDQ SWRKERVLNV PLCKEDCEQW WEDCRTSYTC KSNWHKGWNW TSGFNKCAVG AACQPFHFYF PTPTVLCNEI WTHSYKVSNY SRGSGRCIQM WFDPAQGNPN EEVARFYAAA MSHHHHHH.
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 :
NKp46 HumanDescription:
Natural Cytotoxicity Receptor NKp46 Human Recombinant
Natural cytotoxicity triggering receptor 1, Natural killer cell p46-related protein, hNKp46, NK-p46, NKp46, NK cell-activating receptor, Lymphocyte antigen 94 homolog, CD335 antigen, NCR1, LY94, NCRNKp46, CD335.
Product # :
PRO-432Price :
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Description
NKp46 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 235 amino acids (22-255) and having a molecular mass of 26.6kDa. NKp46 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NKp46 (1mg/ml) contains phosphate buffered saline (pH7.4) & 1mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
A natural cytotoxicity receptor (NCR) NKp46 has been shown to represent a novel NK cell-specific molecule involved in human NK cell activation. The natural cytotoxicity receptors (NCRs) are a recently characterized family of Ig-like activation receptors that appear to be major triggering receptors in tumor cell recognition. The three known NCRs include NKp46 and NKp30, which are expressed on circulating NKcells, and NKp44, which is expressed only on activating NK cells. NKp46 has been implicated in NK cell-mediated lysis of several autologous tumor cells, pathogen-infected cell lines and mononuclear phagocytes infected with an intracellular bacterium. The Lysis of tumor cells by NK-cells involves recognition by NKp46 of heparan sulfate moieties of membrane heparan sulfate proteoglycans. Furthermore, NKp46 is a surface receptor involved in NK-cell cell death by apoptosis. NKp46 has two extracellular Ig-like domains followed by a ~40 residue stalk region, a type I transmembrane domain, and a short cytoplasmic tail. The extracellular Ig-like domain of NKp46 (22-255aa) is purified by FPLC gel-filtration chromatography, after refolding of the isolated inclusion bodies in a redox buffer. In addition, engagement of the antigen with the monoclonal antibody stimulates intracellular calcium levels and the synthesis of cytokines. CD59 is an NKp46 coreceptor (by physical association) together they activate cytotoxicity of human NK-cells, their engagement results in tyrosine phosphorylation of CD3-zeta chains associated with NKp46. Reduced cell surface expression of NKp46 and other NK-cell receptors is linked to the impaired NK-cell cytolytic function in viremic HIV-1 infection.
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Synonyms
Natural cytotoxicity triggering receptor 1, Natural killer cell p46-related protein, hNKp46, NK-p46, NKp46, NK cell-activating receptor, Lymphocyte antigen 94 homolog, CD335 antigen, NCR1, LY94, NCRNKp46, CD335.
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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
MQQQTLPKPF IWAEPHFMVP KEKQVTICCQ GNYGAVEYQL HFEGSLFAVD RPKPPERINKVKFYIPDMNS RMAGQYSCIY RVGELWSEPS NLLDLVVTEM YDTPTLSVHP GPEVISGEEV TFYCRLDTAT SMFLLLKEGR SSHVQRGYGK VQAEFPLGPV TTAHRGTYRX FGSYNNHAWSFPSEPVKLLV TGDIENTSLA PEDPTFSADT WGTYLLTTET GLQKDHALWD HTAQN.
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 :
SGTA HumanDescription:
Small Glutamine-Rich Tetratricopeptide Repeat-Containing Protein Alpha Human Recombinant
alphaSGT, hSGT, SGT, Vpu-binding protein, UBP, Small glutamine-rich tetratricopeptide repeat-containing protein alpha, Alpha-SGT, SGT1.
Product # :
PRO-807Price :
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Description
SGTA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 321 amino acids (1-313 a.a.) and having a molecular mass of 35.1 kDa. SGTA protein is fused to a 8 amino acid His-Tag at C-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
SGTA Human solution containing 20mM Trsi HCL pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SGTA is a ubiquitously expressed protein that contains three TPR protein-protein interaction duplicates. SGTA takes part as a component of the androgen receptor (AR)-chaperone-cochaperone complex, functions as a cochaperone and participates in androgen signaling. SGTA binds directly to HSC70 and HSP70 and mediates their ATPase activity. SGTA gene encodes a protein that is able to interact with the chief nonstructural protein of parvovirus H-1 and 70-kDa heat shock cognate. In addition, SGTA interacts with Vpu and Gag from HIV-1, SARS-CoV accessory protein 7a, DNAJC5 and DNAJC5B. Since this transcript is expressed universally in several tissues, SGTA serves a housekeeping function. While being involved in apoptosis and androgen signaling, SGTA is a possible molecule for polycystic ovary syndrome, a disorder characterized by androgen excess, obesity and menstrual disturbances.
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Synonyms
alphaSGT, hSGT, SGT, Vpu-binding protein, UBP, Small glutamine-rich tetratricopeptide repeat-containing protein alpha, Alpha-SGT, SGT1.
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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
MDNKKRLAYA IIQFLHDQLR HGGLSSDAQE SLEVAIQCLE TAFGVTVEDS DLALPQTLPE IFEAAATGKE MPQDLRSPAR TPPSEEDSAE AERLKTEGNE QMKVENFEAA VHFYGKAIEL NPANAVYFCN RAAAYSKLGN YAGAVQDCER AICIDPAYSK AYGRMGLALS SLNKHVEAVA YYKKALELDP DNETYKSNLK IAELKLREAP SPTGGVGSFD IAGLLNNPGF MSMASNLMNN PQIQQLMSGM ISGGNNPLGT PGTSPSQNDL ASLIQAGQQF AQQMQQQNPE LIEQLRSQIR SRTPSASNDD QQELEHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Insulin HumanDescription:
Insulin Human Recombinant
Product # :
CYT-270Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Insulin Human Recombinant produced in E.Coli is a two chain, non-glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 5807 Dalton. Insulin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 98.0% as determined by RP-HPLC analysis.
Biological Activity
The Biological Activity was determined to be 28 units/mg.Citations
More Info
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Introduction
Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Insulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Insulin 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 Insulin in sterile 0.005N HCl not more than 1 mg/ml.
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 :
ATP1B1 Human, Sf9Description:
ATPase Transporting Beta 1 Human Recombinant, Sf9
Sodium/potassium-transporting ATPase subunit beta-1, ATPase, Na+/K+ transporting, beta 1 polypeptide, ATP1B, ATPBS, Sodium/potassium-dependent ATPase subunit beta-1, ATP1B1, ATPaseTransporting Beta 1.
Product # :
PRO-2385Price :
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Description
ATP1B1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 250 amino acids (63-303 a.a.) and having a molecular mass of 29kDa (Molecular size on SDS-PAGE will appear at approximately 28-40 kDa).ATP1B1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ATP1B1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ATPase Transporting Beta 1 (ATP1B1) is a part of the family of Na+/K+ and H+/K+ ATPases beta chain proteins, and the subfamily of Na+/K+ -ATPases. Na+/K+ -ATPase is an essential membrane protein accountable for establishing and maintaining the electrochemical gradients of Na and K ions over the plasma membrane. These gradients are vital for osmoregulation, for sodium-coupled transport of a range of organic and inorganic molecules, and for electrical excitability of muscle and nerve. ATP1B1is combined of 2 subunits, a large catalytic subunit (alpha) and a smaller glycoprotein subunit (beta). The beta subunit regulates the number of sodium pumps transported to the plasma membrane through assembly of alpha/beta heterodimers. ATP1B1 is a beta 1 subunit.
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Synonyms
Sodium/potassium-transporting ATPase subunit beta-1, ATPase, Na+/K+ transporting, beta 1 polypeptide, ATP1B, ATPBS, Sodium/potassium-dependent ATPase subunit beta-1, ATP1B1, ATPaseTransporting Beta 1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPEFKPTYQ DRVAPPGLTQ IPQIQKTEIS FRPNDPKSYE AYVLNIVRFL EKYKDSAQRD DMIFEDCGDV PSEPKERGDF NHERGERKVC RFKLEWLGNC SGLNDETYGY KEGKPCIIIK LNRVLGFKPK PPKNESLETY PVMKYNPNVL PVQCTGKRDE DKDKVGNVEY FGLGNSPGFP LQYYPYYGKL LQPKYLQPLL AVQFTNLTMD TEIRIECKAY GENIGYSEKD RFQGRFDVKI EVKSHHHHHH.
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 :
TNFRSF10A Human FcDescription:
TRAIL Receptor-1 Human Recombinant Fc
Tumor Necrosis Factor Receptor Superfamily Member 10a, TRAILR1, APO2, DR4, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261, TNFRSF10A.
Product # :
CYT-877Price :
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Shipping Method :
Shipped at Room temp
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Description
TRAIL R1 Fc Human Recombinant (24-240) produced in E.Coli is a non-glycosylated, disulfide-linked homodimer containing two polypeptide chains of 217 amino acids each and having a molecular mass of 41kDa [including tag] each chain. TRAILR1 is fused to a 236 amino acid Fc tag at C-terminal and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in PBS.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured by its ability to inhibit Trail-mediated cytotoxicity in mouse L-929 cells, is less than 1.25ng/ml.Citations
More Info
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Introduction
Human TNFRSF10A is a type 1 transmembrane protein in the TNF R superfamily. TNFRSF10A is not expressed in rodents. The trimeric ligand Trail binds TNFRSF10A and induces apoptosis, and recombinant, soluble forms of the receptor inhibit Trail-induced apoptosis. TNFRSF10A is expressed generally in damaged, infected, and malignant cells. TNFRSF10A functions in immune surveillance, inducing apoptosis in cancer cells but not normal cells.
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Synonyms
Tumor Necrosis Factor Receptor Superfamily Member 10a, TRAILR1, APO2, DR4, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261, TNFRSF10A.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TNFRSF10A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TRAIL-R1 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 TNFRSF10A in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ASGTEAAAAT PSKVWGSSAG RIEPRGGGRG ALPTSMGQHG PSARARAGRA PGPRPAREAS PRLRVHKTFK FVVVGVLLQV VPSSAATIKL HDQSIGTQQW EHSPLGELCP PGSHRSERPG ACNRCTEGVG YTNASNNLFA CLPCTACKSD EEERSPCTTT RNTACQCKPG TFRNDNSAEM CRKCSTGCPR GMVKVKDCTP WSDIECVHKE SGNGHNIEGR MDPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK.
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.