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1000 results found for “mortality factor”
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Name :
FIBP HumanDescription:
FGF-1 Intracellular-Binding Protein Human Recombinant
FGFIBP, FIBP-1, Acidic fibroblast growth factor intracellular-binding protein, aFGF intracellular-binding protein, FGF-1 intracellular-binding protein, FIBP.
Product # :
CYT-758Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
FIBP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 387amino acids (1-364) and having a molecular mass of 44.3kDa. The FIBP is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
FIBP protein (0.5mg/ml) is supplied in 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
FGF-1 Intracellular-Binding Protein (FIBP) which is a member of Fibroblast growth factors (FGFs) binds to internalized FGF-1 and is thought to be involved in mitogenic function of FGF-1. FGF activity effects development, adult tissue homeostasis, angiogenesis and cancer progression. FIBP localizes to the nucleus and is greatly expressed in heart, skeletal muscle and pancreas and at lower levels in brain, placenta, liver and kidney.
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Synonyms
FGFIBP, FIBP-1, Acidic fibroblast growth factor intracellular-binding protein, aFGF intracellular-binding protein, FGF-1 intracellular-binding protein, FIBP.
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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 MGSMTSELDI FVGNTTLIDE DVYRLWLDGY SVTDAVALRV RSGILEQTGA TAAVLQSDTM DHYRTFHMLE RLLHAPPKLL HQLIFQIPPS RQALLIERYY AFDEAFVREV LGKKLSKGTK KDLDDISTKT GITLKSCRRQ FDNFKRVFKV VEEMRGSLVD NIQQHFLLSD RLARDYAAIV FFANNRFETG KKKLQYLSFG DFAFCAELMI QNWTLGAVGE APTDPDSQMD DMDMDLDKEF LQDLKELKVL VADKDLLDLH KSLVCTALRG KLGVFSEMEA NFKNLSRGLV NVAAKLTHNK DVRDLFVDLV EKFVEPCRSD HWPLSDVRFF LNQYSASVHS LDGFRHQALW DRYMGTLRGC LLRLYHD.
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Background
What is the molecular weight/Mw of FIBP Protein?
FIBP Protein has a total Mw of 44.3kkDa.
What is the source or expression system of FIBP Protein?
Escherichia Coli.
What is the Purity of FIBP Protein?
FIBP Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FIBP Protein?
The biological functionality of FIBP Protein will be determined in the future.
What is the amino acid sequence of FIBP Protein?
MGSSHHHHHH SSGLVPRGSH MGSMTSELDI FVGNTTLIDE DVYRLWLDGY SVTDAVALRV RSGILEQTGA TAAVLQSDTM DHYRTFHMLE RLLHAPPKLL HQLIFQIPPS RQALLIERYY AFDEAFVREV LGKKLSKGTK KDLDDISTKT GITLKSCRRQ FDNFKRVFKV VEEMRGSLVD NIQQHFLLSD RLARDYAAIV FFANNRFETG KKKLQYLSFG DFAFCAELMI QNWTLGAVGE APTDPDSQMD DMDMDLDKEF LQDLKELKVL VADKDLLDLH KSLVCTALRG KLGVFSEMEA NFKNLSRGLV NVAAKLTHNK DVRDLFVDLV EKFVEPCRSD HWPLSDVRFF LNQYSASVHS LDGFRHQALW DRYMGTLRGC LLRLYHD.
What applications can FIBP Protein be used in?
FIBP Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FIBP Protein?
The endotoxin level is minimal, FIBP 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.
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Name :
Leptin tA RatDescription:
Leptin Antagonist Triple Mutant Rat Recombinant
Product # :
CYT-355Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Antagonist Triple Mutant Rat Recombinant is a singly non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Rat Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (0.85mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
ProSpec’s Leptin Antagonist Triple Mutant Rat Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin-Antagonist Triple Mutant Rat Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP-tA mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Rat Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.21 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MAFF HumanDescription:
V-maf Musculoaponeurotic Fibrosarcoma Oncogene F Human Recombinant
hMafF, U-MAF, Transcription factor MafF, U-Maf, V-maf musculoaponeurotic fibrosarcoma oncogene homolog F, MAFF.
Product # :
PRO-1565Price :
Quantity :
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Shipped with Ice Packs
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Description
MAFF Human Recombinant produced in E. coli is a single polypeptide chain containing 187 amino acids (1-164) and having a molecular mass of 20.1kDa. MAFF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MAFF solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
V-maf Musculoaponeurotic Fibrosarcoma Oncogene F (MAFF) which is expressed in the term myometrium and kidney is a basic leucine zipper (bZIP) transcription factor which lacks a transactivation domain. MAFF is known to bind the US-2 DNA element and probably heterodimerizes along with other leucine zipper-containing proteins to enhance expression of the OTR gene throughout pregnancy period. MAFF also forms homodimers, and since it lacks a transactivation domain, the homodimer operates as a repressor of transcription.
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Synonyms
hMafF, U-MAF, Transcription factor MafF, U-Maf, V-maf musculoaponeurotic fibrosarcoma oncogene homolog F, MAFF.
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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 MGSMSVDPLS SKALKIKREL SENTPHLSDE ALMGLSVREL NRHLRGLSAE EVTRLKQRRR TLKNRGYAAS CRVKRVCQKE ELQKQKSELE REVDKLAREN AAMRLELDAL RGKCEALQGF ARSVAAARGP ATLVAPASVI TIVKSTPGSG SGPAHGPDPA HGPASCS.
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 :
IFN tau OvineDescription:
IFN-Tau Ovine Recombinant
IFN-tau1, Trophoblast protein 1, TP-1, Trophoblastin, Antiluteolysin, Trophoblast antiluteolytic protein, IFN-tau, IFN tau-1.
Product # :
CYT-377Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IFN-Tau Ovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 19914.7 Dalton.The IFN-Tau is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from (1mg/ml) solution containing PBS pH-7.4.
Purity
Greater than 95.0% as determined by both:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 10,000,000IU/mg.More Info
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Introduction
IFN-tau is also known as TP-1 (trophoblast protein-1) is a new class of type I IFN that is secreted by the trophoblast and is the signal for maternal recognition of pregnancy in sheep. IFN- tau has potent immunosuppressive and antiviral activities similar to other type I IFN but is less cytotoxic than IFN-alpha and IFN-beta. The current investigation concerns the effect of recombinant ovine IFN- tau (rOIFN- tau) on the modulation of MHC class I and II expression on cloned mouse cerebrovascular endothelial (CVE) cells.
IFN-tau induced tyrosine phosphorylation of Stat1 and upregulated the expression of MHC class I on CVE. One proposed action by which type I IFN reduces the relapse rate in MS is via interference with IFN-?-induced MHC class II expression. IFN- tau was shown to downregulate IFN-?-induced MHC class II expression on CVE and, hence, may be of potential therapeutic value in downregulating inflammation in the central nervous system (CNS). IFN- tau did not upregulate the expression of MHC class II on CVE. IFN- tau also inhibited the replication of Theiler's virus in CVE. -
Synonyms
IFN-tau1, Trophoblast protein 1, TP-1, Trophoblastin, Antiluteolysin, Trophoblast antiluteolytic protein, IFN-tau, IFN tau-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IFN-Tau although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Tau 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 IFN Tau in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Cys-Tyr-Leu-Ser-Arg.
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Background
What is the molecular weight/Mw of IFN TAU OVINE Protein?
IFN TAU OVINE Protein has a total Mw of 19.9kDa.
What is the source or expression system of IFN TAU OVINE Protein?
Escherichia Coli.
What is the Purity of IFN TAU OVINE Protein?
IFN TAU OVINE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFN TAU OVINE Protein?
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 10,000,000IU/mg.
What is the amino acid sequence of IFN TAU OVINE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Cys-Tyr-Leu-Ser-Arg.
What applications can IFN TAU OVINE Protein be used in?
IFN TAU OVINE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFN TAU OVINE Protein?
The endotoxin level is minimal, IFN TAU OVINE 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.
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Name :
ADI1 HumanDescription:
Acireductone Dioxygenase 1 Human Recombinant
APL1, ARD, FLJ10913, HMFT1638, MTCBP-1, SIPL, 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase, Acireductone dioxygenase, Fe-ARD, Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1, Submergence-induced protein-like factor.
Product # :
ENZ-700Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ADI1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (1-179 a.a.) and having a molecular mass of 25.6kDa. ADI1 is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ADI1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Acireductone dioxygenase 1 (ADI1) is a part of the acireductone dioxygenase family of metal-binding enzymes, which are involved in methionine salvage. ADI1 regulates mRNA processing in the nucleus, and carries out different functions depending on its localization. Related pseudogenes have been defined on chromosomes 8 and 20. ADI1 down-regulates cell migration arbitrated by MMP14.
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Synonyms
APL1, ARD, FLJ10913, HMFT1638, MTCBP-1, SIPL, 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase, Acireductone dioxygenase, Fe-ARD, Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1, Submergence-induced protein-like factor.
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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 KDRWGSSMVL AWYMDDAPGD PRQPHRPDPG RPVGLEQLRR LGVLYWKLDA DKYENDPELE KIRRERNYSW MDIITICKDK LPNYEEKIKM FYEEHLHLDD EIRYILDGSG YFDVRDKEDQ WIRIFMEKGD MVTLPAGIYH RFTVDEKNYT KAMRLFVGEP VWTAYNRPAD HFEARGQYVK FLAQTA.
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 :
TNIP1 HumanDescription:
TNFAIP3 Interacting Protein 1 Human Recombinant
TNFAIP3-interacting protein 1, HIV-1 Nef-interacting protein, Nef-associated factor 1, Naf1, Nip40-1, Virion-associated nuclear shuttling protein, VAN, hVAN, TNIP1, KIAA0113, NAF1, ABIN-1.
Product # :
PRO-005Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TNIP1 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 458 amino acids (94-530 a.a.) and having a molecular mass of 51.8kDa. The TNIP1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TNIP1 solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH7.5), 20% glycerol, 5mM DTT and 200mM NaCl.
Purity
Greater than 75.0% as determined by SDS-PAGE.
More Info
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Introduction
TNFAIP3-interacting protein 1 (TNIP1) interacts with zinc finger protein A20/TNFAIP3 and inhibits TNF-induced NF-kappa-B-dependent gene expression by interfering with a RIP- or TRAF2-mediated transactivation signal. Furthermore, TNIP1 interacts with HIV-1 matrix protein and is packaged into virions and its overexpression can inhibit viral replication. TNIP1 can regulate matrix nuclear localization, both nuclear import of Preintegration complex (PIC) and export of GAG polyprotein and viral genomic RNA during virion production.
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Synonyms
TNFAIP3-interacting protein 1, HIV-1 Nef-interacting protein, Nef-associated factor 1, Naf1, Nip40-1, Virion-associated nuclear shuttling protein, VAN, hVAN, TNIP1, KIAA0113, NAF1, ABIN-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 MSNVTASPTA PACPSDKPAP VQKPPSSGTS SEFEVVTPEE QNSPESSSHA NAMALGPLPR EDGNLMLHLQ RLETTLSVCA EEPDHGQLFT HLGRMALEFN RLASKVHKNE QRTSILQTLC EQLRKENEAL KAKLDKGLEQ RDQAAERLRE ENLELKKLLM SNGNKEGASG RPGSPKMEGT GKKAVAGQQQ ASVTAGKVPE VVALGAAEKK VKMLEQQRSE LLEVNKQWDQ HFRSMKQQYE QKITELRQKL ADLQKQVTDL EAEREQKQRD FDRKLLLAKS KIEMEETDKE QLTAEAKELR QKVKYLQDQL SPLTRQREYQ EKEIQRLNKA LEEALSIQTP PSSPPTAFGS PEGAGALLRK QELVTQNELL KQQVKIFEED FQRERSDRER MNEEKEELKK QVEKLQAQVT LSNAQLKAFK DEEKAREALR QQKRKAKA.
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 :
CXCL7 HumanDescription:
Neutrophil Activating Protein-2 Human Recombinant (CXCL7)
Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.
Product # :
CHM-274Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Neutrophil Activating Protein-2 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 70 amino acids and having a molecular mass of 7609 Dalton. The NAP-2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CXCL7 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.
Purity
Greater than 97% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined by the ability of NAP2 to chemoattract human neurotrophils using a concentration of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
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Introduction
Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.
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Synonyms
Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NAP-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL7should 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 Neutrophil Activating Protein-2in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Glu-Leu-Arg-Cys.
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Background
What is the molecular weight/Mw of CXCL7 HUMAN Protein?
CXCL7 HUMAN Protein has a total Mw of 7.6kDa.
What is the source or expression system of CXCL7 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL7 HUMAN Protein?
CXCL7 HUMAN Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL7 HUMAN Protein?
The specific activity as determined by the ability of NAP2 to chemoattract human neurotrophils using a concentration of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CXCL7 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Glu-Leu-Arg-Cys.
What applications can CXCL7 HUMAN Protein be used in?
CXCL7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL7 HUMAN Protein?
The endotoxin level is minimal, CXCL7 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.
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Name :
Leptin qA Human, PEGDescription:
Leptin Quadruple Antagonist Pegylated Human Recombinant
Product # :
CYT-1251Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Pegylated Quadruple Antagonist Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and an additional Ala at N-terminus acids. The Human Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Human Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Human Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Human Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated human leptin antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated human leptin antagonist), resulting mainly from increased food intake. The in vivo activity of human pegylated super leptin antagonist was compared to that of human pegylated leptin antagonist is 9-27 fold higher.
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Human Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of Human pegylated leptin antagonist and filter sterilization Human pegylated leptin antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Human Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin is a~16 kDa protein which is encoded by the obese gene. Leptin is a hormone which participates in regulating body weight, reproductive function and metabolism. leptin is expressed predominantly by adipocytes, which supports the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GH CarpDescription:
Growth Hormone Carp Recombinant
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
Product # :
CYT-297Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Growth Hormone Carp Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 188 amino acids & having a molecular mass of 21,408 Dalton. Growth Hormone Carp is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GH Carp was lyophilized from a concentrated (1mg/ml) solution with 0.3% NaHCO3 adjusted to pH 8.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Carp GH is biologically active in rat 3T3 F442A preadipocytes, though its activity is 15-fold lower compared to bovine GH, but it is equally potent in vivo in promoting carp growth (Fine et al.1993). Furthermore, carp GH forms 1:2 complex with the extra cellular domain of ovine growth hormone receptor.More Info
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Introduction
Growth-Hormone is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
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Synonyms
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Growth Hormone Carp recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Growth Hormone Carp 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 Growth Hormone Carp recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and found to be Ser-Asp-Asn-Gln-Arg.
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 :
LGALS3 MouseDescription:
Galectin-3 Mouse Recombinant
CBP35, GAL3, GALBP, GALIG, LGALS2, MAC2, Galectin-3, Lectin, galactose binding, soluble 3, Lectin, galactose binding, soluble 3, isoform CRA_a, Lectin, galactose binding, soluble 3, isoform CRA_d, Lgals3.
Product # :
CYT-188Price :
Quantity :
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- sds-page
Description
LGALS3 Mouse Recombinant produced in E. coli is a single polypeptide chain containing 287 amino acids (1-264) and having a molecular mass of 29.8 kDa. LGALS3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The LGALS3 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol, 1mM DTT and 2mM EDTA.
Purity
Greater than 95% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Galectin-3 mediates with the alpha-3, beta-1 integrin the stimulation by cspg4 of endothelial cells migration. Galectin-3 plays an necessary part during the acquisition of vasculogenic mimicry and angiogenic properties associated with melanoma progression. LGALS3 overexpression is highly expressed in early stages of papillary carcinoma, and its expression intensity declines during tumor progression. Serum levels of LGALS3 are high in patients with thyroid malignancy but there is considerable overlap in serum LGALS3 concentrations between those with benign and malignant nodular thyroid disease. LGLAS3 takes part as an immune regulator to inhibit T-cell immune responses and promote tumor growth, as a result providing a new mechanism for tumor immune tolerance.
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Synonyms
CBP35, GAL3, GALBP, GALIG, LGALS2, MAC2, Galectin-3, Lectin, galactose binding, soluble 3, Lectin, galactose binding, soluble 3, isoform CRA_a, Lectin, galactose binding, soluble 3, isoform CRA_d, Lgals3.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMADSFSL NDALAGSGNP NPQGYPGAWG NQPGAGGYPG AAYPGAYPGQ APPGAYPGQA PPGAYPGQAP PSAYPGPTAP GAYPGPTAPG AYPGSTAPGA FPGQPGAPGA YPSAPGGYPA AGPYGVPAGP LTVPYDLPLP GGVMPRMLIT IMGTVKPNAN RIVLDFRRGN DVAFHFNPRF NENNRRVIVC NTKQDNNWGK EERQSAFPFE SGKPFKIQVL VEADHFKVAV NDAHLLQYNH RMKNLREISQ LGISGDITLT SANHAMI.
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Background
What is the molecular weight/Mw of LGALS3 Protein?
LGALS3 Protein has a total Mw of 29.8kDa.
What is the source or expression system of LGALS3 Protein?
Escherichia Coli.
What is the Purity of LGALS3 Protein?
LGALS3 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS3 Protein?
The biological functionality of LGALS3 Protein will be determined in the future.
What is the amino acid sequence of LGALS3 Protein?
MGSSHHHHHH SSGLVPRGSH MGSMADSFSL NDALAGSGNP NPQGYPGAWG NQPGAGGYPG AAYPGAYPGQ APPGAYPGQA PPGAYPGQAP PSAYPGPTAP GAYPGPTAPG AYPGSTAPGA FPGQPGAPGA YPSAPGGYPA AGPYGVPAGP LTVPYDLPLP GGVMPRMLIT IMGTVKPNAN RIVLDFRRGN DVAFHFNPRF NENNRRVIVC NTKQDNNWGK EERQSAFPFE SGKPFKIQVL VEADHFKVAV NDAHLLQYNH RMKNLREISQ LGISGDITLT SANHAMI.
What applications can LGALS3 Protein be used in?
LGALS3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS3 Protein?
The endotoxin level is minimal, LGALS3 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 :
MAPK1 Human, ActiveDescription:
Mitogen-Activated Protein Kinase 1 Human Recombinant, Active
Mitogen-activated protein kinase 1, EC 2.7.11.24, Extracellular signal-regulated kinase 2, ERK-2, Mitogen-activated protein kinase 2, MAP kinase 2, MAPK 2, p42-MAPK, ERT1, ERK, p38, p40, p41, ERK2, MAPK2, PRKM1, PRKM2, P42MAPK, p41mapk.
Product # :
PKA-214Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MAPK1 Human Recombinant is a non-glycosylated full length chain containing amino acids Met1-Ser360 and having a calculated molecular mass of 41,762 Dalton. MAPK1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MAPK1 protein solution is supplied in 50mM HEPES pH 7.5, 100mM NaCl, 5mM DTT and 20% glycerol.
Purity
The purity is greater than 95%.
More Info
-
Introduction
Mitogen-activated protein kinase 1 (MAPK1) is also known as "extracellular signal-regulated kinase 2" (ERK2). Two similar (85% sequence identity) protein kinases were originally called ERK1 and ERK2. They were found during a search for protein kinases that are rapidly phosphorylated after activation of cell surface tyrosine kinasessuch as the epidermal growth factor receptor. Phosphorylation of ERKs leads to the activation of their kinase activity.
The molecular events linking cell surface receptors to activation of ERKs are complex. It was found that RasGTP-binding proteins are involved in the activation of ERKs. Another protein kinase, Raf-1, was shown to phosphorylate a "MAPK kinase", thus qualifying as a "MAPK kinase kinase". The MAPK kinase was named "MAPK/ERK kinase" (MEK).
Receptor-linked tyrosine kinases, Ras, Raf, MEK and MAPK could be fitted into a signaling cascade linking an extracellular signal to MAPK activation.
Transgenic gene knockoutmice lacking MAPK1 have major defects in early development. -
Synonyms
Mitogen-activated protein kinase 1, EC 2.7.11.24, Extracellular signal-regulated kinase 2, ERK-2, Mitogen-activated protein kinase 2, MAP kinase 2, MAPK 2, p42-MAPK, ERT1, ERK, p38, p40, p41, ERK2, MAPK2, PRKM1, PRKM2, P42MAPK, p41mapk.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store vial at -20°C to -80°C.Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
maaaaaagag pemvrgqvfd vgprytnlsy igegaygmvc saydnvnkvr vaikkispfe hqtycqrtlr eikillrfrh eniigindii raptieqmkd vyivqdlmet dlykllktqh lsndhicyfl yqilrglkyi hsanvlhrdl kpsnlllntt cdlkicdfgl arvadpdhdh tgflteyvat rwyrapeiml nskgytksid iwsvgcilae mlsnrpifpg khyldqlnhi lgilgspsqe dlnciinlka rnyllslphk nkvpwnrlfp nadskaldll dkmltfnphk rieveqalah pyleqyydps depiaeapfk fdmelddlpk eklkelifee tarfqpgyrs.
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Specific Activity
386 pmol/µgxmin ATP-KM: 1.7µM
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 :
NRBF2 HumanDescription:
Nuclear Receptor Binding Factor 2 Human Recombinant
Nuclear receptor binding factor 2, COPR1, COPR2, NRBF-2, Nuclear receptor-binding factor 2, Comodulator of PPAR and RXR, NRBF2, COPR.
Product # :
PRO-1692Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NRBF2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 266 amino acids (45-287) and having a molecular mass of 29.9 kDa.NRBF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NRBF2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Nuclear receptor binding factor 2 (NRBF2) which works as transcriptional activator, modulates transcriptional activation by target nuclear receptors.
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Synonyms
Nuclear receptor binding factor 2, COPR1, COPR2, NRBF-2, Nuclear receptor-binding factor 2, Comodulator of PPAR and RXR, NRBF2, COPR.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMKLTQSE QAHLSLELQR DSHMKQLLLI QERWKRAQRE ERLKAQQNTD KDAAAHLQTS HKPSAEDAEG QSPLSQKYSP STEKCLPEIQ GIFDRDPDTL LYLLQQKSEP AEPCIGSKAP KDDKTIIEEQ ATKIADLKRH VEFLVAENER LRKENKQLKA EKARLLKGPI EKELDVDADF VETSELWSLP PHAETATASS TWQKFAANTG KAKDIPIPNL PPLDFPSPEL PLMELSEDIL KGFMNN.
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 :
POU2AF1 HumanDescription:
POU class 2 associating factor 1 Human Recombinant
POU domain class 2 associating factor 1, BOB-1, OCA-B, B-cell-specific coactivator OBF-1, OCT-binding factor 1.
Product # :
PRO-880Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
POU2AF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 276 amino acids (1-256) and having a molecular mass of 29.6 kDa.The POU2AF1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
POU2AF1 protein (0.5mg/ml) is supplied in 20mM Tris-HCL, pH-8 and 20% Glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
POU2AF1 is a lymphocyte specific transcription coactivator protein. POU2AF1 cooperates only with the Oct1/2 proteins using sub domains in the POU domain of the Oct1/2 proteins, increasing their transcriptional efficiency. Even though POU2AF1 have no basic ability to bind DNA, it links firmly with the octomer motif in the presence of Oct1 and Oct2. POU2AF1 is expressed at maximum levels in spleen and peripheral blood leukocytes.
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Synonyms
POU domain class 2 associating factor 1, BOB-1, OCA-B, B-cell-specific coactivator OBF-1, OCT-binding factor 1.
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Physical Appearance
POU2AF1 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 MLWQKPTAPE QAPAPARPYQ GVRVKEPVKE LLRRKRGHAS SGAAPAPTAV VLPHQPLATY TTVGPSCLDM EGSVSAVTEE AALCAGWLSQ PTPATLQPLA PWTPYTEYVP HEAVSCPYSA DMYVQPVCPS YTVVGPSSVL TYASPPLITN VTTRSSATPA VGPPLEGPEH QAPLTYFPWP QPLSTLPTST LQYQPPAPAL PGPQFVQLPI SIPEPVLQDM EDPRRAASSL TIDKLLLEEE DSDAYALNHT LSVEGF
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 :
MMAB HumanDescription:
Methylmalonic Aciduria Type B Human Recombinant
CBIB, Cob(I)alamin adenosyltransferase, EC 2.5.1.17.
Product # :
ENZ-248Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MMAB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 239 amino acids (33-250 a.a.) and having a molecular mass of 26.3 kDa. The MMAB is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MMAB 1mg/ml protein solution contains 20mM Tris pH-7.5 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
MMAB protein catalyzes the last step in the conversion of vitamin B(12) into adenosylcobalamin (AdoCbl), a vitamin B12 containing coenzyme for methylmalonyl-CoA mutase(MCM). Decreased MMAB activity leads to the inherited disorder vitamin B12 dependent methylmalonic aciduria linked to the cblB complementation group.
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Synonyms
CBIB, Cob(I)alamin adenosyltransferase, EC 2.5.1.17.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
MMAB Human although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQSRGPQGVE DGDRPQPSSK TPRIPKIYTK TGDKGFSSTF TGERRPKDDQ VFEAVGTTDE LSSAIGFALE LVTEKGHTFA EELQKIQCTL QDVGSALATP CSSAREAHLK YTTFKAGPIL ELEQWIDKYT SQLPPLTAFI LPSGGKISSA LHFCRAVCRR AERRVVPLVQ MGETDANVAK FLNRLSDYLF TLARYAAMKE GNQEKIYKKN DPSAESEGL.
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 :
NDUFS5 HumanDescription:
Histidine NADH Dehydrogenase Fe-S Protein 5 Human Recombinant
CI-15k, CI15K, NADH dehydrogenase [ubiquinone] iron-sulfur protein 5, Complex I-15 kDa, NADH-ubiquinone oxidoreductase 15 kDa subunit, CI-15 kDa, NDUFS5.
Product # :
ENZ-771Price :
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Description
NDUFS5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 129 amino acids (1-106a.a) and having a molecular mass of 14.9kDa. NDUFS5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NDUFS5 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Histidine NADH Dehydrogenase Fe-S Protein 5 (NDUFS5) belongs to the NADH dehydrogenase (ubiquinone) iron-sulfur protein family. NDUFS5 is a subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which doesn’t take part in catalysis. Complex I is transferring the electrons from NADH to the respiratory chain.
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Synonyms
CI-15k, CI15K, NADH dehydrogenase [ubiquinone] iron-sulfur protein 5, Complex I-15 kDa, NADH-ubiquinone oxidoreductase 15 kDa subunit, CI-15 kDa, NDUFS5.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPFLDIQ KRFGLNIDRW LTIQSGEQPY KMAGRCHAFE KEWIECAHGI GYTRAEKECK IEYDDFVECL LRQKTMRRAG TIRKQRDKLI KEGKYTPPPH HIGKGEPRP.
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 :
POFUT1 HumanDescription:
Protein O-Fucosyltransferase 1 Human Recombinant
FUT12, O-Fuc-T, O-FucT-1, O-FUT, GDP-fucose protein O-fucosyltransferase 1, Peptide-O-fucosyltraferase 1,KIAA0180.
Product # :
ENZ-679Price :
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Shipped with Ice Packs
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Description
POFUT1 Human Recombinant produced in E. coli is a single polypeptide chain containing 385 amino acids (27-388) and having a molecular mass of 43.7 kDa. POFUT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The POFUT1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
GDP-fucose protein O-fucosyltransferase 1 (POUFUT1), belongs to the glycosyltransferase O-Fuc family. POUFUT1 encodes a member of the glycosyltransferase O-Fuc family and Expressed mainly in pancreas, kidney, lung, heart, brain, liver, placenta and skeletal muscle.POUFUT1 adds O-fucose through an O-glycosidic linkage to Preserve serine or threonine residues in the epidermal growth factor-like repeats of a number of cell surface and emitted proteins. POUFUT1 is involved in ligand-induced receptor signaling. Alternative splicing of this gene results in 2 transcript variants encoding different isoforms.POFUT1 participates in Notch signaling, as Notch ligands can use as POFUT1 substrates.
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Synonyms
FUT12, O-Fuc-T, O-FucT-1, O-FUT, GDP-fucose protein O-fucosyltransferase 1, Peptide-O-fucosyltraferase 1,KIAA0180.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSGSWDPAG YLLYCPCMGR FGNQADHFLG SLAFAKLLNR TLAVPPWIEY QHHKPPFTNL HVSYQKYFKL EPLQAYHRVI SLEDFMEKLA PTHWPPEKRV AYCFEVAAQR SPDKKTCPMK EGNPFGPFWD QFHVSFNKSE LFTGISFSAS YREQWSQRFS PKEHPVLALP GAPAQFPVLE EHRPLQKYMV WSDEMVKTGE AQIHAHLVRP YVGIHLRIGS DWKNACAMLK DGTAGSHFMA SPQCVGYSRS TAAPLTMTMC LPDLKEIQRA VKLWVRSLDA QSVYVATDSE SYVPELQQLF KGKVKVVSLK PEVAQVDLYI LGQADHFIGN CVSSFTAFVK RERDLQGRPS SFFGMDRPPK LRDEF.
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 :
LGALS1 MouseDescription:
Galectin-1 Mouse Recombinant
Galectin-1, Gal-1, 14 kDa lectin, Beta-galactoside-binding lectin L-14-I, Galaptin, Lactose-binding lectin 1, Lectin galactoside-binding soluble 1, S-Lac lectin 1, Lgals1, Gbp, L14, Galbp, L-14.5, Lect14, AA410090.
Product # :
CYT-186Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- SDS-PAGE
Description
LGALS1 mouse Recombinant produced E. coli is a single polypeptide chain containing 159 amino acids (1-135) and having a molecular mass of 17kDa.LGALS1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LGALS1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
The galectins are a family of beta-galactoside-binding proteins implicated in modulating cell-cell and cell-matrix interactions. Galectin-1 is an autocrine negative growth factor that regulates cell proliferation. Galectin-1 regulates cell apoptosis and cell differentiation. Galectin-1 binds CD45, CD3 and CD4 & inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of lyn kinase. Galectin-1 and its ligands are one of the master regulators of immune responses as T-cell homeostasis and survival, T-cell immune disorders, inflammation and allergies as well as host–pathogen interactions. Galectin-1 expression or overexpression in tumors and/or the tissue surrounding them must be considered as a sign of the malignant tumor progression that is often related to the long-range dissemination of tumoral cells (metastasis), to their dissemination into the surrounding normal tissue, and to tumor immune-escape. Galectin-1 in its oxidized form plays a number of important roles in the regeneration of the central nervous system after injury. The targeted overexpression (or delivery) of Galectin-1 should be considered as a method of choice for the treatment of some kinds of inflammation-related diseases, neurodegenerative pathologies and muscular dystrophies. In contrast, the targeted inhibition of Galectin-1 expression is what should be developed for therapeutic applications against cancer progression. Galectin-1 is thus a promising molecular target for the development of new and original therapeutic tools. There is 88% homology between the human and mouse galectin-1.
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Synonyms
Galectin-1, Gal-1, 14 kDa lectin, Beta-galactoside-binding lectin L-14-I, Galaptin, Lactose-binding lectin 1, Lectin galactoside-binding soluble 1, S-Lac lectin 1, Lgals1, Gbp, L14, Galbp, L-14.5, Lect14, AA410090.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMACGLV ASNLNLKPGE CLKVRGEVAS DAKSFVLNLG KDSNNLCLHF NPRFNAHGDA NTIVCNTKED GTWGTEHREP AFPFQPGSIT EVCITFDQAD LTIKLPDGHE FKFPNRLNME AINYMAADGD FKIKCVAFE.
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Background
What is the molecular weight/Mw of LGALS1 MOUSE Protein?
LGALS1 MOUSE Protein has a total Mw of 17kDa.
What is the source or expression system of LGALS1 MOUSE Protein?
Escherichia Coli.
What is the Purity of LGALS1 MOUSE Protein?
LGALS1 MOUSE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS1 MOUSE Protein?
The biological functionality of LGALS1 MOUSE Protein will be determined in the future.
What is the amino acid sequence of LGALS1 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMACGLV ASNLNLKPGE CLKVRGEVAS DAKSFVLNLG KDSNNLCLHF NPRFNAHGDA NTIVCNTKED GTWGTEHREP AFPFQPGSIT EVCITFDQAD LTIKLPDGHE FKFPNRLNME AINYMAADGD FKIKCVAFE.
What applications can LGALS1 MOUSE Protein be used in?
LGALS1 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS1 MOUSE Protein?
The endotoxin level is minimal, LGALS1 MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
LGALS3 HumanDescription:
Galectin-3 Human Recombinant
Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.
Product # :
CYT-606Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
LGALS3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 250 amino acids and having a molecular mass of 26.2kDa. The LGALS3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Galectin-3 protein was lyophilized from a sterile 0.2 micron filtered aqueous solution containing 10 mM sodium phosphate and 50mM sodium chloride, pH 7.5.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
Galectin-3 mediates with the alpha-3, beta-1 integrin the stimulation by cspg4 of endothelial cells migration. Galectin-3 plays an necessary part during the acquisition of vasculogenic mimicry and angiogenic properties associated with melanoma progression. LGALS3 overexpression is highly expressed in early stages of papillary carcinoma, and its expression intensity declines during tumor progression. Serum levels of LGALS3 are high in patients with thyroid malignancy but there is considerable overlap in serum LGALS3 concentrations between those with benign and malignant nodular thyroid disease. LGLAS3 takes part as an immune regulator to inhibit T-cell immune responses and promote tumor growth, as a result providing a new mechanism for tumor immune tolerance.
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Synonyms
Galectin-3, GAL3, MAC2, CBP35, GALB, GALIG, LGALS2, LGALS3, Galactose-specific lectin 3, Mac-2 antigen, IgE-binding protein, 35 kDa lectin, Carbohydrate-binding protein 35, CBP 35, Laminin-binding protein, Lectin L-29, L-31, Galactoside-binding protein, GALBP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Galectin-3 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Galectin-3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized LGALS3 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
MADNFSLHDAL SGSGNPNPQG WPGAWGNQPA GAGGYPGASY PGAYPGQAPP GAYPGQAPPG AYPGAPGAYP GAPAPGVYPG PPSGPGAYPS SGQPSATGAY PATGPYGAPA GPLIVPYNLP LPGGVVPRML ITILGTVKPN ANRIALDFQR GNDVAFHFNP RFNENNRRVI VCNTKLDNNW GREERQSVFP FESGKPFKIQ VLVEPDHFKV AVNDAHLLQY NHRVKKLNEI SKLGISGDID LTSASYTMI.
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Background
What is the molecular weight/Mw of LGALS3 HUMAN Protein?
LGALS3 HUMAN Protein has a total Mw of 26.2kDa.
What is the source or expression system of LGALS3 HUMAN Protein?
Escherichia Coli.
What is the Purity of LGALS3 HUMAN Protein?
LGALS3 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS3 HUMAN Protein?
The biological functionality of LGALS3 HUMAN Protein will be determined in the future.
What is the amino acid sequence of LGALS3 HUMAN Protein?
MADNFSLHDAL SGSGNPNPQG WPGAWGNQPA GAGGYPGASY PGAYPGQAPP GAYPGQAPPG AYPGAPGAYP GAPAPGVYPG PPSGPGAYPS SGQPSATGAY PATGPYGAPA GPLIVPYNLP LPGGVVPRML ITILGTVKPN ANRIALDFQR GNDVAFHFNP RFNENNRRVI VCNTKLDNNW GREERQSVFP FESGKPFKIQ VLVEPDHFKV AVNDAHLLQY NHRVKKLNEI SKLGISGDID LTSASYTMI.
What applications can LGALS3 HUMAN Protein be used in?
LGALS3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS3 HUMAN Protein?
The endotoxin level is minimal, LGALS3 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 :
Activin-A RatDescription:
Activin-A Rat Recombinant
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-147Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Active form Activin-A Rat Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.
Source
E.Coli.
Formulation
Rat Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.02% TFA.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/mlMore Info
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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
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Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A 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
Rat INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 26.2 kDa.
What is the source or expression system of Activin A Protein?
Ecoli
What is the Purity of Activin A Protein?
Activin A Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000units/mg.
What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACTIVIN A Protein?
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
What applications can ACTIVIN A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
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 :
EGFR Human Sf9Description:
Epidermal Growth Factor Receptor Sf9 Human Recombinant
Epidermal growth factor receptor, EC 2.7.10.1, Receptor tyrosine-protein kinase ErbB-1, ERBB, mENA, ERBB1, EGFR.
Product # :
PKA-344Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
The EGFR contains the extracellular domain of the human EGFR (25-647 a.a.) excluding the signal peptide which is cleaved by the insect cells having an approximate Mw of 85kDa. The EGFR is fused to a C-terminal Strep-tag and purified by proprietary chromatographic techniques.
Source
Sf9 Insect Cells.
Formulation
ErbB1 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1x PBS pH-7.4.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-a , betacellulin, epiregulin, HBEGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.
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Synonyms
Epidermal growth factor receptor, EC 2.7.10.1, Receptor tyrosine-protein kinase ErbB-1, ERBB, mENA, ERBB1, EGFR.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EGFR although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGFR 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 EGFR in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
LEEKKV CQGTSNKLTQ LGTFEDHFLS LQRMFNNCEV VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP LENLQIIRGN MYYENSYALA VLSNYDANKT GLKELPMRNL QEILHGAVRF SNNPALCNVE SIQWRDIVSS DFLSNMSMDF QNHLGSCQKC DPSCPNGSCW GAGEENCQKL TKIICAQQCS GRCRGKSPSD CCHNQCAAGC TGPRESDCLV CRKFRDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV VTDHGSCVRA CGADSYEMEE DGVRKCKKCE GPCRKVCNGI GIGEFKDSLS INATNIKHFK NCTSISGDLH ILPVAFRGDS FTHTPPLDPQ ELDILKTVKE ITGFLLIQAW PENRTDLHAF ENLEIIRGRT KQHGQFSLAV VSLNITSLGL RSLKEISDGD VIISGNKNLC YANTINWKKL FGTSGQKTKI ISNRGENSCK ATGQVCHALC SPEGCWGPEP RDCVSCRNVS RGRECVDKCK LLEGEPREFV ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGVM GENNTLVWKY ADAGHVCHLC HPNCTYGCTG PGLEGCPTNG PKIPSIAASW SHPQFEK.
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 :
EAF1 HumanDescription:
ELL Associated Factor 1 Human Recombinant
ELL-associated factor 1, EAF1.
Product # :
PRO-1855Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
EAF1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 110 amino acids (182-268) and having a molecular mass of 11.3kDa. EAF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EAF1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
ELL Associated Factor 1 (EAF1) is a part of the EAF family and is expressed mainly in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, prostate, testis, small intestine and colon. EAF1 plays a role as a transcriptional transactivator of ELL and ELL2 elongation activities.
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Synonyms
ELL-associated factor 1, EAF1.
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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 MGSDIIEQMS SSSGSSSSDS ESSSGSDDDS SSSGGEDNGP ASPPQPSHQQ PYNSRPAVAN GTSRPQGSNQ LMNTLRNDLQ LSESGSDSDD.
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-6 PAT1F10AT AntibodyDescription:
Interleukin-6 Clone PAT1F10AT, Mouse Anti Human
IFN-b2, B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2, Interferon beta-2, Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.
Product # :
ANT-540Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
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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
IFN-b2, B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2, Interferon beta-2, Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human IL-6, clone PAT1F10AT mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human IL-6 protein 30-212 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and k light chain.
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Clone
PAT1F10AT.
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Applications
The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
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Background
Research Paper on Interleukin-6 Clone PAT1F10AT, Mouse Anti-Human
Abstract:
Interleukin-6 (IL-6) Clone PAT1F10AT, a Mouse Anti-Human monoclonal antibody, plays a pivotal role in deciphering the complexities of immune modulation. This research paper provides an insightful exploration of its molecular attributes and its profound implications in immunological research. We examine its interactions, functions, and synonyms, including DIF, TNFA, and TNFSF2, shedding light on its significance in understanding immune responses.
Introduction:
IL-6 Clone PAT1F10AT, a Mouse Anti-Human antibody, has emerged as a cornerstone in immunology research. This paper delves into its unique characteristics and its critical role in unraveling immune mechanisms.
Molecular Precision and Specificity:
The exceptional affinity and specificity of IL-6 Clone PAT1F10AT for human IL-6 distinguish it as an invaluable tool for immunodetection and functional studies. Its targeted binding facilitates accurate identification of IL-6 in various experimental contexts.
Unveiling Immune Dynamics:
IL-6 is a central player in immune orchestration, and IL-6 Clone PAT1F10AT offers a window into its world. By investigating its involvement in immune responses, inflammation, and signaling pathways, researchers gain insights into immune regulation.
Synonyms and Interactions:
Understanding IL-6 synonyms, such as DIF, TNFA, and TNFSF2, underscores its intricate web of interactions. IL-6 Clone PAT1F10AT's ability to decipher these connections enhances our understanding of cytokine-mediated immune modulation.
Disease Implications and Therapeutic Avenues:
With its relevance in diseases like autoimmune disorders and inflammatory conditions, IL-6 Clone PAT1F10AT assumes significance in disease-focused investigations. It enables researchers to dissect disease mechanisms and evaluate potential therapeutic interventions.
Clinical Utility and Diagnostic Precision:
IL-6 Clone PAT1F10AT's utility transcends research settings, finding application in clinical diagnostics. Its role in immunoassays facilitates accurate disease diagnosis and monitoring, contributing to improved patient management.
Conclusion:
In the realm of immunology, IL-6 Clone PAT1F10AT stands as a potent ally in unraveling immune intricacies. Its molecular precision, diverse functions, and potential therapeutic implications make it a cornerstone in advancing our understanding of immune responses and diseases.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
IL-6 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL 7 MouseDescription:
Interleukin-7 Mouse Recombinant
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
Product # :
CYT-372Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
Interleukin-7 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 129 amino acids and having a molecular mass of 14.9kDa.
Source
Escherichia Coli.
Formulation
Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 1×PBS, pH7.4 and 2% trehalose.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50was determined by the dose-dependent stimulation of the proliferation of murine 2E8 cells is less than 0.2 ng/ml, corresponding to a specific activity of >5.0×106 IU/mg.More Info
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Introduction
Interleukin-7 is a potent lymphoid cell growth factor produced primarily by stromal cells. IL-7 has been shown to support the proliferation and differentiation of pre B- and early T cells as well as displaying a biological effect on cells of NK and myeloid lineages.
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Synonyms
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 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 Interleukin 7 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
ECHIKDKEGK AYESVLMISI DELDKMTGTD SNCPNNEPNF FRKHVCDDTK EAAFLNRAAR KLKQFLKMNI SEEFNVHLLT VSQGTQTLVN CTSKEEKNVK EQKKNDACFL KRLLREIKTC WNKILKGSI.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin qA HumanDescription:
Leptin Antagonist Quadruple Mutant Human Recombinant
Product # :
CYT-353Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
Leptin Quadruple Mutant Human Recombinant is a single polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a Mw of 16 kDa, Human Leptin was mutated, resulting in L39A/D40A/F41A/I42A.Leptin Antagonist Quadruple Mutant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
ProSpec’s Leptin Quadruple Antagonist Mutant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transected with the long form of human Leptin receptor. It also inhibits various Leptin effects in several in vitro bioassays.More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Quadruple Mutant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.89 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.