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1000 results found for “visfatin”
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Name :
TEF HumanDescription:
Thyrotrophic Embryonic Factor Human Recombinant
Thyrotroph embryonic factor, TEF, Thyrotroph embryonic factor isoform 1.FBG2, FBS2, FBX6, Fbx6b, F-box only protein 6, F-box protein that recognizes sugar chains 2, F-box/G-domain protein 2, FBXO6.
Product # :
PRO-1523Price :
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Description
TEF Human Recombinant produced in E. coli is a single polypeptide chain containing 326 amino acids (1-303) and having a molecular mass of 35.6kDa.TEF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TEF solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Thyrotroph embryonic factor (TEF) is a nuclear transcription factor which is a part of the bZIP (basic region/leucine zipper) family and PAR subfamily. TEF binds DNA as either a homodimer or heterodimer, and is known to transactivate the TSH beta promoter. TEF accumulates according to a robust circadian rhythm and is also inhibits cell growth by down-regulating beta chain expression of cytokine receptors.
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Synonyms
Thyrotroph embryonic factor, TEF, Thyrotroph embryonic factor isoform 1.FBG2, FBS2, FBX6, Fbx6b, F-box only protein 6, F-box protein that recognizes sugar chains 2, F-box/G-domain protein 2, FBXO6.
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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 MGSMSDAGGG KKPPVDPQAG PGPGPGRAAG ERGLSGSFPL VLKKLMENPP REARLDKEKG KEKLEEDEAA AASTMAVSAS LMPPIWDKTI PYDGESFHLE YMDLDEFLLE NGIPASPTHL AHNLLLPVAE LEGKESASSS TASPPSSSTA IFQPSETVSS
TESSLEKERE TPSPIDPNCV EVDVNFNPDP ADLVLSSVPG GELFNPRKHK FAEEDLKPQP MIKKAKKVFV PDEQKDEKYW TRRKKNNVAA KRSRDARRLK ENQITIRAAF LEKENTALRT EVAELRKEVG KCKTIVSKYE TKYGPL.
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 :
SYT1 HumanDescription:
Synaptotagmin I Human Recombinant
Synaptotagmin-1, Synaptotagmin I, SytI, p65, SYT1, SVP65, SYT.
Product # :
PRO-239Price :
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Description
SYT1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 256 amino acids (136-382 a.a) and having a molecular mass of 29.5kDa.SYT1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SYT1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 100mM NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Synaptotagmin-1(SYT1) is a member of the synaptotagmin family, which contains two C2 domains. The synaptotagmins are integral membrane proteins of synaptic vesicles assumed to function as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. SYT1 is the principal regulator responsible for allowing the human brain to release neurotransmitters. SYT1 may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. SYT1 binds acidic phospholipids with a specificity which entails the presence of both an acidic head group and a diacyl backbone. SYT1 can also bind to at least 3 additional proteins in a Ca2+-independent manner; these being neurexins, syntaxin and AP2.
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Synonyms
Synaptotagmin-1, Synaptotagmin I, SytI, p65, SYT1, SVP65, SYT.
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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
MEPKEEEKLG KLQYSLDYDF QNNQLLVGII QAAELPALDM GGTSDPYVKV FLLPDKKKKF ETKVHRKTLN PVFNEQFTFK VPYSELGGKT LVMAVYDFDR FSKHDIIGEF KVPMNTVDFG HVTEEWRDLQ SAEKEEQEKL GDICFSLRYV PTAGKLTVVI LEAKNLKKMD VGGLSDPYVK IHLMQNGKRL KKKKTTIKKN TLNPYYNESF SFEVPFEQIQ KVQVVVTVLD YDKIGKNDAI GKVFVGYNLE HHHHHH.
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 :
CRYAB AntibodyDescription:
Crystallin Alpha B, Mouse Anti Human
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
Product # :
ANT-306Price :
Quantity :
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Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
Citations
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Introduction
Alpha crystallins are composed of two gene products; alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20). They act as molecular chaperones and hold them in in large soluble aggregates. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional function of -crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-B is expressed widely in many tissues and organs and occurs in many neurological diseases.
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Synonyms
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
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Physical Appearance
Sterile Filtered colorless solution.
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Immunogen
Anti-human CRYAB mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CRYAB amino acids 1-175 purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chains and κ light chain.
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Clone
P2E8AT.
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Applications
CRYAB antibody has been tested by ELISA and 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 dilution range for Western blot analysis is 1:500 ~ 2,000. Recommended starting dilution is 1:1,000.
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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
CRYAB antibody was purified from mouse ascitic fluids by protein-G 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.
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Name :
CX3CL1 Human, Sf9Description:
Fractalkine (CX3CL1) Human Recombinant, Sf9
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
Product # :
CHM-042Price :
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Description
Fractalkine Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 323 amino acids (25-339aa) and having a molecular mass of 34.3kDa.Fractalkine is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The Fractalkine solution (1 mg/ml) contains 10% Glycerol and Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
SDS-PAGE
Citations
More Info
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Introduction
Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.
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Synonyms
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
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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
QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD
AMQHLDRQAA ALTRNGGTFE KQIGEVKPRT TPAAGGMDES VVLEPEATGE SSSLEPTPSS
QEAQRALGTS PELPTGVTGS SGTRLPPTPK AQDGGPVGTE LFRVPPVSTA ATWQSSAPHQ
PGPSLWAEAK TSEAPSTQDP STQASTASSP APEENAPSEG QRVWGQGQSP RPENSLEREE
MGPVPAHTDA FQDWGPGSMA HVSVVPVSSE GTPSREPVAS GSWTPKAEEP IHATMDPQRL GVLITPVPDA QAATRLEHHH HHH -
Background
What is the molecular weight/Mw of CX3CL1 HUMAN, SF9 Protein?
CX3CL1 HUMAN, SF9 Protein has a total Mw of 34.3kDa.
What is the source or expression system of CX3CL1 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.
What is the Purity of CX3CL1 HUMAN, SF9 Protein?
CX3CL1 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CX3CL1 HUMAN, SF9 Protein?
The biological functionality of CX3CL1 HUMAN, SF9 Protein will be determined in the future.
What is the amino acid sequence of CX3CL1 HUMAN, SF9 Protein?
QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD
AMQHLDRQAA ALTRNGGTFE KQIGEVKPRT TPAAGGMDES VVLEPEATGE SSSLEPTPSS
QEAQRALGTS PELPTGVTGS SGTRLPPTPK AQDGGPVGTE LFRVPPVSTA ATWQSSAPHQ
PGPSLWAEAK TSEAPSTQDP STQASTASSP APEENAPSEG QRVWGQGQSP RPENSLEREE
MGPVPAHTDA FQDWGPGSMA HVSVVPVSSE GTPSREPVAS GSWTPKAEEP IHATMDPQRL GVLITPVPDA QAATRLEHHH HHH
What applications can CX3CL1 HUMAN, SF9 Protein be used in?
CX3CL1 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CX3CL1 HUMAN, SF9 Protein?
The endotoxin level is minimal, CX3CL1 HUMAN, SF9 Protein was purified using conventional chromatography techniques.
Who supplies recombinant CX3CL1 HUMAN, 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 CX3CL1 HUMAN, 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 :
MFAP3 HumanDescription:
Microfibrillar-associated Protein 3 Human Recombinant
Microfibril-associated glycoprotein 3, MFAP3.
Product # :
PRO-1949Price :
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Description
MFAP3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 152 amino acids (19-147) and having a molecular mass of 16.7 kDa.MFAP3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MFAP3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Microfibrillar-associated Protein 3 (MFAP3) contains 1 Ig-like C2-type (immunoglobulin-like) domain, and belongs to lncRNA RNA class. The MFAP3 protein is a component of the elastin-associated microfibrils. Among MFAP3 related pathways are degradation of the extracellular matrix and elastic fiber formation. An significant paralog of the MFAP3 gene is MFAP3L.
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Synonyms
Microfibril-associated glycoprotein 3, MFAP3.
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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 MGSAFVLEDV DFDQMVSLEA NRSSYNASFP SSFELSASSH SDDDVIIAKE GTSVSIECLL TASHYEDVHW HNSKGQQLDG RSRGGKWLVS DNFLNITNVA FDDRGLYTCF VTSPIRASYS VTLRVIFTSG DM.
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 :
ACOT11 HumanDescription:
Acyl-CoA Thioesterase 11 Human Recombinant
Acyl-CoA Thioesterase 11, StAR-Related Lipid Transfer (START) Domain Containing 14, Thioesterase, Adipose Associated, Acyl-CoA Thioester Hydrolase 11, Adipose-Associated Thioesterase, Brown Fat-Inducible Thioesterase, Thioesterase Superfamily Member 1, START Domain Containing 14, Acyl-Coenzyme A Thioesterase 11, STARD14, THEM1, THEA, BFIT, BFIT1, BFIT2, KIAA0707, EC 3.1.2.1.
Product # :
ENZ-756Price :
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Description
ACOT11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain topological domain containing 268 amino acids (19-250 a.a) and having a molecular mass of 29.9kDa. ACOT11 is fused to a 36 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
ACOT11 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ACOT11 belongs to the acyl-CoA thioesterase family which catalyses the transformation of activated fatty acids to the equivalent non-esterified fatty acid and coenzyme A. Expression of a mouse homolog in brown adipose tissue is induced by low temperatures and inhibited by high temperatures. Obesity-resistant mice demonstrated High levels of expression compared with obesity-prone mice, indicating BFIT takes part in acyl-CoA thioesterase 11 in obesity. BFIT has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates.
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Synonyms
Acyl-CoA Thioesterase 11, StAR-Related Lipid Transfer (START) Domain Containing 14, Thioesterase, Adipose Associated, Acyl-CoA Thioester Hydrolase 11, Adipose-Associated Thioesterase, Brown Fat-Inducible Thioesterase, Thioesterase Superfamily Member 1, START Domain Containing 14, Acyl-Coenzyme A Thioesterase 11, STARD14, THEM1, THEA, BFIT, BFIT1, BFIT2, KIAA0707, EC 3.1.2.1.
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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 KDRWGSNRTS RKSALRAGND SAMADGEGYR NPTEVQMSQL VLPCHTNQRG ELSVGQLLKW IDTTACLSAE RHAGCPCVTA SMDDIYFEHT ISVGQVVNIK AKVNRAFNSS MEVGIQVASE DLCSEKQWNV CKALATFVAR REITKVKLKQ ITPRTEEEKM EHSVAAERRR MRLVYADTIK DLLANCAIQG DLESRDCSRM VPAEKTRVES VELVLPPHAN HQGNTFGGQI MAWMENVA
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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Description:
Hepatoma-Derived Growth Factor (32-285 a.a) Human Recombinant
Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF, DFNB39.
Product # :
CYT-294Price :
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Description
HGF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids (32-285 a.a.) and having a molecular mass of 29.8kDa. HGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HGF protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80% as determined by SDS-PAGE.
SDS-PAGE
Citations
More Info
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Introduction
Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.
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Synonyms
Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF, DFNB39.
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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
MQRKRRNTIH EFKKSAKTTL IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SYRGKDLQEN YCRNPRGEEG GPWCFTSNPE VRYEVCDIPQ CSEVECMTCN GESYRGLMDH TESGKICQRW DHQTPHRHKF LPERYPDKGF DDNYCRNPDG QPRPWCYTLD PHTRWEYCAI KTCET.
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Background
What is the molecular weight/Mw of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein has a total Mw of 29.8kDa.
What is the source or expression system of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
Escherichia Coli.
What is the Purity of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein is >80% pure as determined by SDS-PAGE.
What is the Biological Activity of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
What is the molecular weight/Mw of HGF (32-285) HUMAN Protein? HGF (32-285) HUMAN Protein has a total Mw of 29.8kDa. What is the source or expression system of HGF (32-285) HUMAN Protein? Escherichia Coli. What is the Purity of HGF (32-285) HUMAN Protein? HGF (32-285) HUMAN Protein is >80% pure as determined by SDS-PAGE. What is the Biological Activity of HGF (32-285) HUMAN Protein? The biological functionality of HGF (32-285) HUMAN Protein will be determined in the future. What is the amino acid sequence of HGF (32-285) HUMAN Protein? MQRKRRNTIH EFKKSAKTTL IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SYRGKDLQEN YCRNPRGEEG GPWCFTSNPE VRYEVCDIPQ CSEVECMTCN GESYRGLMDH TESGKICQRW DHQTPHRHKF LPERYPDKGF DDNYCRNPDG QPRPWCYTLD PHTRWEYCAI KTCET. What applications can HGF (32-285) HUMAN Protein be used in? HGF (32-285) HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow. What is the endotoxin level for HGF (32-285) HUMAN Protein? The endotoxin level is minimal, HGF (32-285) HUMAN Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
MQRKRRNTIH EFKKSAKTTL IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SYRGKDLQEN YCRNPRGEEG GPWCFTSNPE VRYEVCDIPQ CSEVECMTCN GESYRGLMDH TESGKICQRW DHQTPHRHKF LPERYPDKGF DDNYCRNPDG QPRPWCYTLD PHTRWEYCAI KTCET.
What applications can HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein be used in?
HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for HEPATOCYTE GROWTH FACTOR (32-285) HUMAN Protein?
The endotoxin level is minimal, HEPATOCYTE GROWTH FACTOR (32-285) 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 :
ANXA13 HumanDescription:
Annexin A13 Human Recombinant
Annexin A13, Annexin XIII, Annexin-13, Intestine-specific annexin, ISA, ANXA13, ANX13, MGC150460.
Product # :
PRO-197Price :
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Description
ANXA13 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 336 amino acids (1-316 a.a.) and having a molecular mass of 37.5kDa. The ANXA13 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ANXA13 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol, 0.1M NaCl and 1mM EDTA.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Annexin A13 (ANXA13) belongs to the annexin protein family, whose members play a role in cytoskeletal interactions, phospholipase inhibition, regulation of cellular growth, and intracellular signal transduction pathways. ANXA13 is believed to be the original originator of the 12 members of vertebrate annexins. ANXA13 expression is decidedly tissue-specific, being expressed only in intestinal and kidney epithelial cells. This expression is linked with a highly differentiated intracellular transport function.
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Synonyms
Annexin A13, Annexin XIII, Annexin-13, Intestine-specific annexin, ISA, ANXA13, ANX13, MGC150460.
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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 MGNRHAKASS PQGFDVDRDA KKLNKACKGM GTNEAAIIEI LSGRTSDERQ QIKQKYKATY GKELEEVLKS ELSGNFEKTA LALLDRPSEY AARQLQKAMK GLGTDESVLI EVLCTRTNKE IIAIKEAYQR LFDRSLESDV KGDTSGNLKK ILVSLLQANR NEGDDVDKDL AGQDAKDLYD AGEGRWGTDE LAFNEVLAKR SYKQLRATFQ AYQILIGKDI EEAIEEETSG DLQKAYLTLV RCAQDCEDYF AERLYKSMKG AGTDEETLIR IVVTRAEVDL QGIKAKFQEK YQKSLSDMVR SDTSGDFRKL LVALLH.
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 :
ANXA7 HumanDescription:
Annexin A7 Human Recombinant
Annexin A7, Annexin-7, Annexin VII, Synexin, ANXA7, ANX7, SNX.
Product # :
PRO-449Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ANXA7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 490 amino acids (1-466 a.a.) and having a molecular mass of 52.9kDa.ANXA7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ANXA7 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 150mM NaCl, 1mM DTT and 40% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Annexin VII is a member of the annexin family of calcium-dependent phospholipid binding proteins. Annexin VII has molecular weight of approximately 51 kDa with a unique, highly hydrophobic N-terminal domain of 167 amino acids and a conserved C-terminal region of 299 amino acids. The latter domain is composed of alternating hydrophobic and hydrophilic segments. Structural analysis of the protein suggests that Annexin VII is a membrane binding protein with diverse properties including voltage-sensitive calcium channel activity, ion selectivity and membrane fusion.
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Synonyms
Annexin A7, Annexin-7, Annexin VII, Synexin, ANXA7, ANX7, SNX.
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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 MGSHMSYPGY PPTGYPPFPG YPPAGQESSF PPSGQYPYPS GFPPMGGGAY PQVPSSGYPG AGGYPAPGGY PAPGGYPGAP QPGGAPSYPG VPPGQGFGVP PGGAGFSGYP QPPSQSYGGG PAQVPLPGGF PGGQMPSQYP GGQPTYPSQP ATVTQVTQGT IRPAANFDAI RDAEILRKAM KGFGTDEQAI VDVVANRSND QRQKIKAAFK TSYGKDLIKD LKSELSGNME ELILALFMPP TYYDAWSLRK AMQGAGTQER VLIEILCTRT NQEIREIVRC YQSEFGRDLE KDIRSDTSGH FERLLVSMCQ GNRDENQSIN HQMAQEDAQR LYQAGEGRLG TDESCFNMIL ATRSFPQLRA TMEAYSRMAN RDLLSSVSRE FSGYVESGLK TILQCALNRP AFFAERLYYA MKGAGTDDST LVRIVVTRSE IDLVQIKQMF AQMYQKTLGT MIAGDTSGDY RRLLLAIVGQ
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 :
SFTPD HumanDescription:
Surfactant Protein D Human Recombinant
Surfactant Protein D, SFTP4, Surfactant Pulmonary-Associated Protein D, Lung Surfactant Protein D, Collectin-7, COLEC7, PSP-D, SP-D, Surfactant-Associated Protein Pulmonary 4, Pulmonary Surfactant-Associated Protein D, Pulmonary Surfactant Apoprotein, Collectin 7, PSPD, SFTPD.
Product # :
PRO-2000Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SFTPD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids (224-375 a.a) and having a molecular mass of 18.9kDa.SFTPD is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SFTPD protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Surfactant pulmonary-associated protein D (SFTPD) belongs to the collectin family of C-type lectins, which is synthesized in many tissues including respiratory epithelial cells in the lung, and contains one C-type lectin domain and one collagen-like domain. SFTPD has humoral molecules of the innate immune system, and is deemed a functional candidate in chronic periodontitis. Moreover, SFTPD is involved in the development of acute and chronic inflammation of the lung. A number of human lung diseases are characterized by decreased levels of bronchoalveolar SFTPD. SFTPD contributes to the lungs defense against inhaled microorganisms, organic antigens and toxins. SFTPD interacts with complexes such as bacterial lipopolysaccharides, oligosaccharides and fatty acids and modulates leukocyte action in immune response. In addition, SFTPD participates in the extracellular reorganization or turnover of pulmonary surfactant. SFTPD binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties.
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Synonyms
Surfactant Protein D, SFTP4, Surfactant Pulmonary-Associated Protein D, Lung Surfactant Protein D, Collectin-7, COLEC7, PSP-D, SP-D, Surfactant-Associated Protein Pulmonary 4, Pulmonary Surfactant-Associated Protein D, Pulmonary Surfactant Apoprotein, Collectin 7, PSPD, SFTPD.
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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 MGSVASLRQQ VEALQGQVQH LQAAFSQYKK VELFPNGQSV GEKIFKTAGF VKPFTEAQLL CTQAGGQLAS PRSAAENAAL QQLVVAKNEA AFLSMTDSKT EGKFTYPTGE SLVYSNWAPG EPNDDGGSED CVEIFTNGKW NDRACGEKRL VVCEF.
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 :
EIF3I HumanDescription:
Eukaryotic Translation Initiation Factor 3I Human Recombinant
Eukaryotic Translation Initiation Factor 3, Subunit I, EIF3S2, Eukaryotic Translation Initiation Factor 3, Subunit 2 Beta, 36kDa, Eukaryotic Translation Initiation Factor 3 Subunit 2, TRIP-1, eIF-3-beta, EIF3 P36, TGF-Beta Receptor-Interacting Protein 1, PRO2242, eIF3-beta, eIF3-p36, Eukaryotic Translation Initiation Factor 3 Subunit I, Eukaryotic Translation Initiation Factor 3, Subunit 2 (Beta, 36kD), Predicted Protein Of HQ2242, TGFbeta Receptor-Interacting Protein 1, eIF3i.
Product # :
PRO-1740Price :
Quantity :
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Shipped with Ice Packs
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Description
EIF3I Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 348 amino acids (1-325aa) and having a molecular mass of 38.9kDa.EIF3I is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
APOBEC4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Eukaryotic translation initiation factor 3, subunit I (EIF3I) is part of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is essential for numerous steps in the initiation of protein synthesis. The eIF-3 complex links with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2: GTP: methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also essential for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. Among the diseases associated with EIF3I are clonorchiasis, and tonsillitis.
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Synonyms
Eukaryotic Translation Initiation Factor 3, Subunit I, EIF3S2, Eukaryotic Translation Initiation Factor 3, Subunit 2 Beta, 36kDa, Eukaryotic Translation Initiation Factor 3 Subunit 2, TRIP-1, eIF-3-beta, EIF3 P36, TGF-Beta Receptor-Interacting Protein 1, PRO2242, eIF3-beta, eIF3-p36, Eukaryotic Translation Initiation Factor 3 Subunit I, Eukaryotic Translation Initiation Factor 3, Subunit 2 (Beta, 36kD), Predicted Protein Of HQ2242, TGFbeta Receptor-Interacting Protein 1, eIF3i.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMKPILLQ GHERSITQIK YNREGDLLFT VAKDPIVNVW YSVNGERLGT YMGHTGAVWC VDADWDTKHV LTGSADNSCR LWDCETGKQL ALLKTNSAVR TCGFDFGGNI IMFSTDKQMG YQCFVSFFDL RDPSQIDNNE PYMKIPCNDS KITSAVWGPL GECIIAGHES GELNQYSAKS GEVLVNVKEH SRQINDIQLS RDMTMFVTAS KDNTAKLFDS TTLEHQKTFR TERPVNSAAL SPNYDHVVLG GGQEAMDVTT TSTRIGKFEA RFFHLAFEEE FGRVKGHFGP INSVAFHPDG KSYSSGGEDG YVRIHYFDPQ YFEFEFEA
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 :
ElcatoninDescription:
Elcatonin
Product # :
HOR-302Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Elcatonin Synthetic is a single, non-glycosylated polypeptide chain containing 31 amino acids, having a molecular mass of 3363.2 Dalton and a Molecular formula of C148H244N42O47.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 93.3% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Biological Activity (based on net peptide) was found to be 6695.2 IU/mg.Citations
More Info
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Introduction
Elcatonin is a Calcitonin derivative which is transformed from eel´s calcitonin by changing the S-S bond into the stable C-N bond. It inhibits the absorption and autolysis of bones, thus leads to blood calcium descending. In addition, it inhibits the bone salts dissolving and transferring and promotes the excretion of calcium and phosphorus in urine. Meanwhile, it inhibits renal tubules reabsorbing calcium, phosphorus and sodium and keeps blood calcium at normal level. It is mainly used for remitting or eliminating the pain caused by Osteoporosis.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Elcatonin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Elcatonin 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 Elcatonin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
Ser-Asn-Leu-Ser-Thr-Asu-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Val-Gly-Ala-Gly-Thr-Pro-NH2.
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Background
What is the molecular weight/Mw of ELCATONIN Protein?
ELCATONIN Protein has a total Mw of 3.36kDa.
What is the Purity of ELCATONIN Protein?
ELCATONIN Protein is > 93.3% pure as determined by SDS-PAGE.
What is the Biological Activity of ELCATONIN Protein?
Biological Activity (based on net peptide) was found to be 6695.2 IU/mg.
What is the amino acid sequence of ELCATONIN Protein?
Ser-Asn-Leu-Ser-Thr-Asu-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Val-Gly-Ala-Gly-Thr-Pro-NH2.
What applications can ELCATONIN Protein be used in?
ELCATONIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ELCATONIN Protein?
The endotoxin level is minimal, ELCATONIN Protein was purified using conventional chromatography techniques.
Who supplies ELCATONIN 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 ELCATONIN?
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 :
Osteocrin HumanDescription:
Osteocrin Human Recombinant
Osteocrin, Musclin, OSTN.
Product # :
PRO-420Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The recombinant Human Osteocrin is produced with N-terminal fusion of His Tag. The Human Osteocrin His-Tagged Fusion Protein is 13.6 kDa containing 106 amino acid residues of the human Osteocrin and 16 additional amino acid residues – His Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer, pH 4.0.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Osteocrin is a recently identified secreted protein expression of which was only detected in bone, peaking just after birth and decreasing markedly with age. A 1280-bp mRNA encodes osteocrin producing a mature protein of 103 amino acids with a molecular mass of 11.4 kDa. In primary osteoblastic cell cultures osteocrin expression coincided with matrix formation then decreased in very mature cultures. Treatment of cultures with 1,25-dihydroxyvitamin D3 resulted in a rapid dose- dependent down-regulation of osteocrin expression, suggesting direct regulation. Chronic treatment of primary cultures with osteocrin-conditioned media inhibited mineralization and reduced osteocalcin and alkaline phosphatase expression. These results suggest that osteocrin represents a novel, unique vitamin D-regulated bone-specific protein that appears to act as a soluble osteoblast regulator.
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Synonyms
Osteocrin, Musclin, OSTN.
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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 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited. Product 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
MRGSHHHHHH GMASHMVDVT TTEAFDSGVI DVQSTPTVRE EKSATDLTAK LLLLDELVSL ENDVIETKKK RSFSGFGSPL DRLSAGSVDH KGKQRKVVDH PKRRFGIPMD RIGRNRLSNS RG.
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 :
TAC3 HumanDescription:
Tachykinin-3 Human Recombinant
Tachykinin-3, ZNEUROK1, Neurokinin-B, NKB, Neuromedin-K, TAC3, NKNB, PRO1155.
Product # :
PRO-716Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TAC3 Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (17-121 a.a.) and having a molecular mass of 13.8kDa.The TAC3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TAC3 solution contains 20mM Tris-HCl buffer (pH 8.0) and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Tachykinin-3 belongs to the substance P-related tachykinin family. Tachykinins are active peptides that stimulate neurons, induce behavioral responses, are effective vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. TAC3 and its receptor are essential switches of regulator of human puberty, regulated by the brain through the release of the GnRH which starts a chain of processes which eventually lead to the production of sex hormones.
During pregnancy, the expression of TAC3 is restricted to the outer syncytiotrophoblast of the placenta, significant concentrations of TAC3 can be identified in plasma as early as week 9, and plasma concentrations of TAC3 are grossly elevated in pregnancy-induced hypertension and pre-eclampsia. Higher Tachykinin-3 concentrations in normotensive pregnant women may be caused by the advanced gestational age and/or the result of a negative interaction of other vasoactive substances. TAC3 has a role in the continuance of high placental blood flow in normal pregnancy. -
Synonyms
Tachykinin-3, ZNEUROK1, Neurokinin-B, NKB, Neuromedin-K, TAC3, NKNB, PRO1155.
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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 QSFGAVCKEP QEEVVPGGGR SKRDPDLYQL LQRLFKSHSS LEGLLKALSQ ASTDPKESTS PEKRDMHDFF VGLMGKRSVQ PDSPTDVNQE NVPSFGILKY PPRAE.
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 :
IRF3 HumanDescription:
IFN Regulatory Factor-3 Human Recombinant
IRF-3, IRF3, IFN Regulatory Factor 3.
Product # :
CYT-292Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IRF-3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids (1-112) and having a molecular mass of 13 kDa.The IRF3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1mg/ml in phosphate-buffered saline (PBS), pH 7.4.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
-
Introduction
Members of the IFN regulatory factor (IRF) family regulate gene expression critical to immune response, hemopoiesis, and proliferation. IRF-3 is a member of the IRF family, and is distinct from other family members. Its transcriptional activity is regulated solely by posttranslational modifications. It plays a crucial role in activation of innate immunity and inflammation in response to viral infection. IRF-3 mediates IFN-stimulated response element (isre) promoter activation. Functions as a molecular switch for antiviral activity. Dsrna generated during the course of an viral infection leads to IRF3 phosphorylation on the c-terminal serine/threonine cluster. This induces a conformational change, leading to its dimerization, nuclear localization and association with creb binding protein (crebbp) to form dsrna-activated factor 1 (draf1), a complex which activates the transcription of genes under the control of isre. The complex binds to the ie and prdiii regions on the ifn-alpha and ifn-beta promoters respectively. IRF-3 does not have any transcription activation domains.
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Synonyms
IRF-3, IRF3, IFN Regulatory Factor 3.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Liquid IRF3 although stable at 10°C for 1 week, should be stored 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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Amino Acid Sequence
MGTPKPRILP WLVSQLDLGQ LEGVAWVNKS RTRFRIPWKH GLRQDAQQED FGIFQAWAEA TGAYVPGRDK PDLPTWKRNF RSALNRKEGL RLAEDRSKDP HDPHKIYEFV NS.
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Background
What is the molecular weight/Mw of IRF3 HUMAN Protein?
IRF3 HUMAN Protein has a total Mw of 13kDa.
What is the source or expression system of IRF3 HUMAN Protein?
Escherichia Coli.
What is the Purity of IRF3 HUMAN Protein?
IRF3 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IRF3 HUMAN Protein?
The biological functionality of IRF3 HUMAN Protein will be determined in the future.
What is the amino acid sequence of IRF3 HUMAN Protein?
MGTPKPRILP WLVSQLDLGQ LEGVAWVNKS RTRFRIPWKH GLRQDAQQED FGIFQAWAEA TGAYVPGRDK PDLPTWKRNF RSALNRKEGL RLAEDRSKDP HDPHKIYEFV NS.
What applications can IRF3 HUMAN Protein be used in?
IRF3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IRF3 HUMAN Protein?
The endotoxin level is minimal, IRF3 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 :
Pleiotrophin HumanDescription:
Pleiotrophin Human Recombinant
PTN, Heparin Affin Regulatory Protein, HARP, Heparin-binding growth factor-8, HBGF-8, Osteoblast-Specific Factor-1, OSF-1, Heparin-binding growth-associated molecule, HB-GAM, HBNF-1 Heparin-binding brain mitogen, Heparin-binding neurite outgrowth-promoting factor 1, HBBM, NEGF1.
Product # :
CYT-749Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Pleiotrophin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 136 amino acids and having a molecular mass of 15.3kDa.The Pleiotrophin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Pleiotrophin protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.sds-page
Citations
More Info
-
Introduction
Pleiotrophin (Osteoblast-Specific Factor-1, OSF-1) contains 136 amino acid residues. The sequence is very rich in cationic amino acids (24% of the residues); lysine cluster sequences are found in the N-terminal and C-terminal ends of the structure.
The OSF-1 gene was shown by Northern blotting analysis to be expressed in mouse calvarial osteoblast-enriched cells and in mouse brain tissues, but not in thymus, spleen, kidney, liver, lung, testis or heart. Pleiotrophin has the ability to promote adhesion, migration, expansion, and differentiation of human osteoprogenitor cells. In addition to certain types of cancer, the embryonic growth and differentiation factor pleiotrophin is found also in adults in inflammatory diseases. In osteoarthritis, pleiotrophin is especially expressed in early stages, and its concentrations in the synovial fluid could serve as a marker for the progress of the disease. Pleitrophin might be involved in cartilage repair in osteoarthritis, in particular, in earlier stages. -
Synonyms
PTN, Heparin Affin Regulatory Protein, HARP, Heparin-binding growth factor-8, HBGF-8, Osteoblast-Specific Factor-1, OSF-1, Heparin-binding growth-associated molecule, HB-GAM, HBNF-1 Heparin-binding brain mitogen, Heparin-binding neurite outgrowth-promoting factor 1, HBBM, NEGF1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Pleiotrophin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pleiotrophin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Pleiotrophin 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
GKKEKPEKKV KKSDCGEWQW SVCVPTSGDC GLGTREGTRT GAECKQTMKT QRCKIPCNWK KQFGAECKYQ FQAWGECDLN TALKTRTGSL KRALHNAECQ KTVTISKPCG KLTKPKPQAE SKKKKKEGKK QEKMLD.
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 :
KRT20 Human, HisDescription:
Cytokeratin 20 Human Recombinant, His Tag
Keratin, type I cytoskeletal 20, CD20, CK-20, CK20, K20, KRT21, Keratin, Cytokeratin-20, Keratin-20, Protein IT, KRT20.
Product # :
PRO-1358Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KRT20 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids (1-424 a.a) and having a molecular mass of 50.9kDa. KRT20 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KRT20 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Recombinant Human Cytokeratin 20 His Tag (KRT20) belongs to the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins is comprised of acidic proteins that are organized in pairs of heterotypic keratin chains. KRT20 is a main cellular protein of mature enterocytes and goblet cells and is specifically expressed in the gastric and intestinal mucosa.
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Synonyms
Keratin, type I cytoskeletal 20, CD20, CK-20, CK20, K20, KRT21, Keratin, Cytokeratin-20, Keratin-20, Protein IT, KRT20.
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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 MGSMDFSRRS FHRSLSSSLQ APVVSTVGMQ RLGTTPSVYG GAGGRGIRIS NSRHTVNYGS DLTGGGDLFV GNEKMAMQNL NDRLASYLEK VRTLEQSNSK LEVQIKQWYE TNAPRAGRDY SAYYRQIEEL RSQIKDAQLQ NARCVLQIDN AKLAAEDFRL KYETERGIRL TVEADLQGLN KVFDDLTLHK TDLEIQIEEL NKDLALLKKE HQEEVDGLHK HLGNTVNVEV DAAPGLNLGV IMNEMRQKYE VMAQKNLQEA KEQFERQTAV LQQQVTVNTE ELKGTEVQLT ELRRTSQSLE IELQSHLSMK ESLEHTLEET KARYSSQLAN LQSLLSSLEA QLMQIRSNME RQNNEYHILL DIKTRLEQEI ATYRRLLEGE DVKTTEYQLS TLEERDIKKT RKIKTVVQEV VDGKVVSSEV KEVEENI.
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 :
LGALS10 HumanDescription:
Charcot-Leyden Crystal Protein Human Recombinant
Eosinophil lysophospholipase, Charcot-Leyden crystal protein, CLC, Galectin-10, Gal-10, Lysolecithin acylhydrolase, GAL10, LGALS10, LGALS10A.
Product # :
PRO-744Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LGALS10 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 162 amino acids (1-142 a.a.) and having a molecular mass of 18.6kDa.LGALS10 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Galectin-10 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Eosinophil lysophospholipase (CLC) acts on biological membranes to regulate the multifunctional lysophospholipids. CLC is a lysophospholipase expressed in eosinophils and basophils. CLC hydrolyzes lysophosphatidylcholine to glycerophosphocholine and a free fatty acid. The CLC protein may possess carbohydrate or IgE-binding activities. CLC is both structurally and functionally related to the galectin family of beta-galactoside binding proteins. CLC may be linked with inflammation and some myeloid leukemias.
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Synonyms
Eosinophil lysophospholipase, Charcot-Leyden crystal protein, CLC, Galectin-10, Gal-10, Lysolecithin acylhydrolase, GAL10, LGALS10, LGALS10A.
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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 MSLLPVPYTE AASLSTGSTV TIKGRPLACF LNEPYLQVDF HTEMKEESDI VFHFQVCFGR RVVMNSREYG AWKQQVESKN MPFQDGQEFE LSISVLPDKY QVMVNGQSSY TFDHRIKPEA VKMVQVWRDI SLTKFNVSYL KR.
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 :
CLCF1 Human, HisDescription:
Neurotrophin-1 Human Recombinant, His Tag
Cardiotrophin-like cytokine factor 1, B-cell-stimulating factor 3, BSF-3, Novel neurotrophin-1, NNT-1, CLCF1, BSF3, CLC, NNT1, NR6, CISS2.
Product # :
CYT-071Price :
Quantity :
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Shipped with Ice Packs
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Description
CLCF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (28-225 a.a) and having a molecular mass of 24.6kDa.CLCF1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CLCF1 protein solution (1mg/ml) containing 20mM sodium citrate (pH 3.5), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
sds-page
Citations
More Info
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Introduction
Cardiotrophin-like cytokine factor 1 (CLCF1) is a member of the interleukin 6 family of cytokines, which are involved in cell signaling via phosphorylation of gp130. CLCF1 has a sequence of 225 amino acids with a 27 aa signal peptide, having a molecular mass of 22kDa in the mature form, and the maximum homology to cardiotrophin-1 and ciliary neurotrophic factor. CLCF1 is actively secreted from cells by forming a complex with soluble type I CRLF1 or soluble CNTFR. Defects in the CLCF1 gene cause cold-induced sweating syndrome 2 (CISS2). The CISS2 syndrome is typified by profuse sweating after exposure to cold as well as congenital physical abnormalities of the head and spine.
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Synonyms
Cardiotrophin-like cytokine factor 1, B-cell-stimulating factor 3, BSF-3, Novel neurotrophin-1, NNT-1, CLCF1, BSF3, CLC, NNT1, NR6, CISS2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.
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Background
Cardiotrophin-Like Cytokine Factor 1 Human Recombinant: A Significant Player in Neuronal Development and Immune Regulation
Cardiotrophin-like cytokine factor 1 (CLCF1) has emerged as a crucial player in neuronal development and immune regulation. As a heterodimeric neurotropic cytokine, CLCF1 in complex with cytokine-like factor-1 (CLF-1) has demonstrated vital roles in neuronal development. Studies show that mice lacking this heterodimer exhibit reduced motor neurons and die shortly after birth due to suckling defects. In humans, mutations in the genes encoding for CLCF1 and CLF-1 manifest as Sohar-Crisponi or cold-induced sweating syndrome, with individuals at high risk of early death1.
CLCF1 also exhibits a significant role in the regulation of hematopoiesis, particularly skewing towards myeloid cell differentiation. It has been demonstrated that in mice, CLCF1 promotes B-cell expansion, enhances humoral responses, and triggers autoimmunity. Further, CLCF1 administration resulted in an increase in circulating myeloid cells, along with augmented hematopoietic progenitor cells in the bone marrow. These findings underscore CLCF1's crucial role in modulating the immune system, particularly in the context of bonemarrow transplants and recovery following sub-lethal irradiation2.
Interestingly, CLCF1 is a member of the IL-6 family of cytokines, known for their significant roles in immune regulation and stem cell biology. Like other family members, CLCF1 is secreted as a composite cytokine with CRLF1 and signals through the heterodimerization of the signaling chains LIFRβ and gp130. This suggests overlapping functions with leukemia inhibitor factor (LIF), another IL-6 family member. Expression of CLCF1 is documented in lymph nodes, spleen, and circulating lymphocytes, further establishing its role in immune modulation. However, the comprehensive implications of CLCF1 in immune regulation and hematopoiesis remain an active area of investigation3.
In summary, Cardiotrophin-like cytokine factor 1 human recombinant represents a promising area of research with potential therapeutic implications in neurodevelopmental disorders and immune regulation.
What is the molecular weight/Mw of CLCF Protein?
CLCF Protein has a total Mw of 24.6kDa.
What is the source or expression system of CLCF Protein?
Escherichia Coli.
What is the Purity of CLCF Protein?
CLCF Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CLCF Protein?
The biological functionality of CLCF Protein will be determined in the future.
What is the amino acid sequence of CLCF Protein?
MGSSHHHHHH SSGLVPRGSH MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.
What applications can CLCF Protein be used in?
CLCF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CLCF Protein?
The endotoxin level is minimal, CLCF Protein was purified using conventional chromatography techniqu
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CNTF HumanDescription:
Ciliary-Neurotrophic Factor Human Recombinant
HCNTF, CNTF, Ciliary Neurotrophic Factor.
Product # :
CYT-272Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Ciliary Neurotrophic Factor Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and having a molecular mass of 22706 Dalton. The CNTF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 5mM sodium Phosphate buffer pH=7.5 and 5mM sodium chloride.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.Citations
More Info
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Introduction
CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. -
Synonyms
HCNTF, CNTF, Ciliary Neurotrophic Factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Ciliary Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CNTF 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 HCNTF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Phe-Thr-Glu.
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Background
Exploring the Potential of Human Recombinant Ciliary-Neurotrophic Factor: Implications and Applications
Abstract:
Ciliary-Neurotrophic Factor (CNTF) holds remarkable promise in neurobiology and therapeutic development due to its neuroprotective and regenerative properties. This paper delves into the significance of Human Recombinant CNTF, its production methodologies, and its potential applications in treating neurodegenerative disorders. The review sheds light on the therapeutic potential of CNTF and its role in advancing neuroregeneration research.
Introduction:
CNTF, a neurotrophic cytokine, is known for its pivotal role in neuronal survival and growth. The availability of Human Recombinant CNTF allows researchers to investigate its therapeutic potential and explore avenues for developing novel treatments for neurodegenerative diseases. CNTF's ability to support neuronal health and promote regeneration makes it a promising candidate for medical interventions.
Mechanisms of Action:
CNTF interacts with specific receptor complexes, activating various downstream signaling pathways, including Janus kinase (JAK) and Signal Transducer and Activator of Transcription (STAT) pathways. These pathways contribute to cell survival, differentiation, and axonal growth, forming the foundation for CNTF's neuroprotective effects.
Production Methods:
Human Recombinant CNTF is produced by introducing the CNTF gene into suitable expression systems, often employing bacterial or mammalian cells. Ensuring proper post-translational modifications is essential for maintaining the protein's biological activity and therapeutic potential.
Therapeutic Applications:
CNTF's neuroprotective and regenerative effects offer potential therapeutic applications in neurodegenerative disorders, such as amyotrophic lateral sclerosis (ALS), retinal degeneration, and Parkinson's disease. It holds promise for preserving and restoring neuronal function, thereby improving the quality of life for affected individuals.
Challenges and Future Directions:
While Human Recombinant CNTF shows great potential, challenges include precise dosing, delivery methods, and potential side effects. Further research is needed to optimize CNTF-based therapies and assess their long-term safety and efficacy in clinical settings.
Conclusion:
Human Recombinant Ciliary-Neurotrophic Factor emerges as a critical tool in advancing our understanding of neuroprotection and neuroregeneration. Its potential in treating neurodegenerative disorders highlights the ongoing quest for innovative therapeutic approaches that harness the body's inherent ability to heal and regenerate.
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 22kDa.
What is the source or expression system of CNTF Protein?
Escherichia Coli.
What is the Purity of CNTF Protein?
CNTF Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTF Protein?
The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.
What is the amino acid sequence of CNTF Protein?
CNTF Protein is composed from 199 amino acids.
What applications can CNTF Protein be used in?
CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTF Protein?
The endotoxin level is minimal, CNTF Protein was purified using conventional chromatography techniques.
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Protein content
CNTF quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.28 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 CNTF Recombinant 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.
- View Data Sheet
Name :
S100A10 HumanDescription:
S100 Calcium Binding Protein A10 Human Recombinant
Protein S100-A10, S100 calcium-binding protein A10, Calpactin-1 light chain, Calpactin I light chain, p10 protein, p11, Cellular ligand of annexin II, S100A10, ANX2LG, CAL1L, CLP11, 42C, p10, GP11, ANX2L, Ca[1], MGC111133.
Product # :
PRO-384Price :
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Description
S100A10 Human Recombinant also called Calpactin light chain is expressed in E. coli having a molecular weight of 15.3kDa fused to an amino terminal hexahistidine tag.
Source
Escherichia Coli.
Formulation
S100-A10 is supplied in 1xPBS and 50% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
2 bands on Western blot at 15.3 and 30.6 kDa, respectively representing monomeric and dimeric form.Citations
More Info
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Introduction
S100A10 is a member of the S100 family of proteins contains two EF-hand calcium-binding motifs and is thought to be involved in the regulation of a number of cellular processes including cell cycle progression and differentiation. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. S100A10 may function in exocytosis and endocytosis.
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Synonyms
Protein S100-A10, S100 calcium-binding protein A10, Calpactin-1 light chain, Calpactin I light chain, p10 protein, p11, Cellular ligand of annexin II, S100A10, ANX2LG, CAL1L, CLP11, 42C, p10, GP11, ANX2L, Ca[1], MGC111133.
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Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Applications
S100A10 can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
The biological activity of this product has not yet been tested.
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 :
CSTF1 Human, sf9Description:
Cleavage Stimulation Factor 1 Human Recombinant, sf9
Cleavage Stimulation Factor Subunit 1, Cleavage Stimulation Factor, 3 Pre-RNA, Subunit 1, 50kD, Cleavage Stimulation Factor 50 KDa Subunit, CF-1 50 KDa Subunit, CSTF 50 KDa Subunit, CstF-50, Cleavage Stimulation Factor, 3 Pre-RNA, Subunit 1, 50kDa, Cleavage Stimulation Factor, 3 Pre-RNA, Subunit 1, CstFp50.
Product # :
PRO-2436Price :
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Description
CSTF1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 437 amino acids (1-431a.a.) and having a molecular mass of 49.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CSTF1 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CSTF1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4), 1mM DTT and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Cleavage stimulation factor subunit 1 (CSTF1) is involved in the polyadenylation and 3'end cleavage of pre-mRNAs. The CSTF1 gene encodes one of three subunits which merge to produce cleavage stimulation factor (CSTF). Like the mammalian G protein beta subunits, CSTF1 contains transducin-like repeats. CSTF1 is one of the numerous factors necessary for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. CSTF1 is responsible for the interaction of CSTF with other factors to create a stable complex on the pre-mRNA.
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Synonyms
Cleavage Stimulation Factor Subunit 1, Cleavage Stimulation Factor, 3 Pre-RNA, Subunit 1, 50kD, Cleavage Stimulation Factor 50 KDa Subunit, CF-1 50 KDa Subunit, CSTF 50 KDa Subunit, CstF-50, Cleavage Stimulation Factor, 3 Pre-RNA, Subunit 1, 50kDa, Cleavage Stimulation Factor, 3 Pre-RNA, Subunit 1, CstFp50.
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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
MYRTKVGLKD RQQLYKLIIS QLLYDGYISI ANGLINEIKP QSVCAPSEQL LHLIKLGMEN DDTAVQYAIG RSDTVAPGTG IDLEFDADVQ TMSPEASEYE TCYVTSHKGP CRVATYSRDG QLIATGSADA SIKILDTERM LAKSAMPIEV MMNETAQQNM ENHPVIRTLY DHVDEVTCLA FHPTEQILAS GSRDYTLKLF DYSKPSAKRA FKYIQEAEML RSISFHPSGD FILVGTQHPT LRLYDINTFQ CFVSCNPQDQ HTDAICSVNY NSSANMYVTG SKDGCIKLWD GVSNRCITTF EKAHDGAEVC SAIFSKNSKY ILSSGKDSVA KLWEISTGRT LVRYTGAGLS GRQVHRTQAV FNHTEDYVLL PDERTISLCC WDSRTAERRN LLSLGHNNIV RCIVHSPTNP GFMTCSDDFR ARFWYRRSTT DHHHHHH.
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 :
CNTFR Human, Sf9Description:
Ciliary Neurotrophic Factor Receptor Human Recombinant, Sf9
Ciliary Neurotrophic Factor Receptor, CNTF Receptor Subunit Alpha, CNTFR-Alpha, Ciliary Neurotrophic Factor Receptor Subunit Alpha.
Product # :
CYT-1087Price :
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Description
CTNFR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 329 amino acids (23-342a.a.) and having a molecular mass of 36.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CTNFR is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CTNFR protein solution (1mg/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
Ciliary Neurotrophic Factor Receptor (CNTFR) is a member of the type I cytokine receptor family and binds to CNTF. The alpha subunit provides the receptor specificity. Sole nucleotide polymorphisms in CNTFR has been associated with variations in muscle strength, in addition to early onset of eating disorders.
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Synonyms
Ciliary Neurotrophic Factor Receptor, CNTF Receptor Subunit Alpha, CNTFR-Alpha, Ciliary Neurotrophic Factor Receptor Subunit Alpha.
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Physical Appearance
Sterile Filtered colorless clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. 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
ADPQRHSPQE APHVQYERLG SDVTLPCGTA NWDAAVTWRV NGTDLAPDLL NGSQLVLHGL ELGHSGLYAC FHRDSWHLRH QVLLHVGLPPREPVLSCRSN TYPKGFYCSW HLPTPTYIPN TFNVTVLHGS KIMVCEKDPA LKNRCHIRYM HLFSTIKYKV SISVSNALGH NATAITFDEF TIVKPDPPEN VVARPVPSNP RRLEVTWQTP STWPDPESFP LKFFLRYRPL ILDQWQHVEL SDGTAHTITD AYAGKEYIIQ VAAKDNEIGTWSDWSVAAHA TPWTEEPRHL TTEAQAAETT TSTTSSLAPP PTTKICDPGE LGSHHHHHH.
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Background
What is the molecular weight/Mw of CNTFR Protein?
CNTFR Protein has a total Mw of 36.9kDa.
What is the source or expression system of CNTFR Protein?
Sf9, Baculovirus cells.
What is the Purity of CNTFR Protein?
CNTFR Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTFR Protein?
The biological functionality of CNTFR Protein will be determined in the future.
What is the amino acid sequence of CNTFR Protein?
ADPQRHSPQE APHVQYERLG SDVTLPCGTA NWDAAVTWRV NGTDLAPDLL NGSQLVLHGL ELGHSGLYAC FHRDSWHLRH QVLLHVGLPPREPVLSCRSN TYPKGFYCSW HLPTPTYIPN TFNVTVLHGS KIMVCEKDPA LKNRCHIRYM HLFSTIKYKV SISVSNALGH NATAITFDEF TIVKPDPPEN VVARPVPSNP RRLEVTWQTP STWPDPESFP LKFFLRYRPL ILDQWQHVEL SDGTAHTITD AYAGKEYIIQ VAAKDNEIGTWSDWSVAAHA TPWTEEPRHL TTEAQAAETT TSTTSSLAPP PTTKICDPGE LGSHHHHHH.
What applications can CNTFR Protein be used in?
CNTFR Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTFR Protein?
The endotoxin level is minimal, CNTFR 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 :
CXCL12 Human beta, HisDescription:
Stromal Cell-Derived Factor-1 beta Human Recombinant (CXCL12), His Tag
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.
Product # :
CHM-249Price :
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Description
SDF-1 beta Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 93 amino acids (22-93 a.a.) and having a molecular mass of 10.8 KDa. The SDF-1b is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SDF-1 beta His Tag protein contains 20mM Tris-HCl buffer pH-8 and 10% glycerol.
Purity
Greater than 90% as determined by Analysis by SDS-PAGE.
Citations
More Info
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Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor. The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively. -
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.
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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 MKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKR FKM.
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Background
What is the molecular weight/Mw of CXCL12 HUMAN BETA, HIS Protein?
CXCL12 HUMAN BETA, HIS Protein has a total Mw of 10.8kDa.
What is the source or expression system of CXCL12 HUMAN BETA, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL12 HUMAN BETA, HIS Protein?
CXCL12 HUMAN BETA, HIS Protein is > 90% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL12 HUMAN BETA, HIS Protein?
The biological functionality of CXCL12 HUMAN BETA, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL12 HUMAN BETA, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKR FKM.
What applications can CXCL12 HUMAN BETA, HIS Protein be used in?
CXCL12 HUMAN BETA, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL12 HUMAN BETA, HIS Protein?
The endotoxin level is minimal, CXCL12 HUMAN BETA, HIS Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL12 HUMAN BETA, HIS 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 CXCL12 HUMAN BETA, HIS?
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.