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1000 results found for “Tissue Factor Pathway Inhibitor”
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Name :
ANGPTL3 (17-460) HumanDescription:
Angiopoietin-like Protein 3 (17-460 a.a.) Human Recombinant
Angiopoietin Like 3, Angiopoietin 5, ANGPT5, ANG-5, Angiopoietin-Related Protein 3 , Angiopoietin-Like Protein 3, Angiopoietin-Like 3, Angiopoietin-5, FHBL2, ANL3.
Product # :
CYT-986Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ANGPTL3 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 453 amino acids (17-460 a.a.) and having a molecular mass of 52.9kDa (Migrates at 25-70kDa on SDS-PAGE under reducing conditions). ANGPTL3 is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ANGPTL3 protein solution (0.25mg/ml) contains Buffered Saline (pH 7.4),30% glycerol And 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
Citations
More Info
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Introduction
ANGPTL3 and ANGPTL4 are angiopoietin-like proteins secreted and expressed mainly by the liver, their role being the regulation of triglyceride metabolism by inhibiting the lipolysis of triglyceride-rich lipoproteins. During different nutritional states (feeding/fasting) the levels of the circulating triglycerides are regulated by Angptl3 and Angptl4 through differential inhibition of Lipoprotein lipase (LPL) as shown by the experimental data. The molecular structure of ANGPTL3 is similar to that of the angiopoietins (vascular endothelial growth factors). Deletion mutants of human Angiopoietin 5 were used in order to demonstrate that the N-terminal domain (fragment 17-207) and not the C-terminal fibrinogen-like domain (fragment 207-460) increased the plasma triglyceride levels in mice.
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Synonyms
Angiopoietin Like 3, Angiopoietin 5, ANGPT5, ANG-5, Angiopoietin-Related Protein 3 , Angiopoietin-Like Protein 3, Angiopoietin-Like 3, Angiopoietin-5, FHBL2, ANL3.
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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
ADPSRIDQDN SSFDSLSPEP KSRFAMLDDV KILANGLLQL GHGLKDFVHK TKGQINDIFQ KLNIFDQSFY DLSLQTSEIK EEEKELRRTT YKLQVKNEEV KNMSLELNSK LESLLEEKIL LQQKVKYLEE QLTNLIQNQP ETPEHPEVTS LKTFVEKQDN SIKDLLQTVE DQYKQLNQQH SQIKEIENQL RRTSIQEPTE ISLSSKPRAP RTTPFLQLNE IRNVKHDGIP AECTTIYNRG EHTSGMYAIR PSNSQVFHVY CDVISGSPWT LIQHRIDGSQ NFNETWENYK YGFGRLDGEF WLGLEKIYSI VKQSNYVLRI ELEDWKDNKH YIEYSFYLGN HETNYTLHLV AITGNVPNAI PENKDLVFST WDHKAKGHFN CPEGYSGGWW WHDECGENNL NGKYNKPRAK SKPERRRGLS WKSQNGRLYS IKSTKMLIHP TDSESFEHHH HHH.
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Background
What is the molecular weight/Mw of ANGPTL3 Protein?
ANGPTL3 Protein has a total Mw of 52.9kDa.
What is the source or expression system of ANGPTL3 Protein?
Sf9, Baculovirus cells.
What is the Purity of ANGPTL3 Protein?
ANGPTL3 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ANGPTL3 Protein?
The biological functionality of ANGPTL3 Protein will be determined in the future.
What is the amino acid sequence of ANGPTL3 Protein?
ADPSRIDQDN SSFDSLSPEP KSRFAMLDDV KILANGLLQL GHGLKDFVHK TKGQINDIFQ KLNIFDQSFY DLSLQTSEIK EEEKELRRTT YKLQVKNEEV KNMSLELNSK LESLLEEKIL LQQKVKYLEE QLTNLIQNQP ETPEHPEVTS LKTFVEKQDN SIKDLLQTVE DQYKQLNQQH SQIKEIENQL RRTSIQEPTE ISLSSKPRAP RTTPFLQLNE IRNVKHDGIP AECTTIYNRG EHTSGMYAIR PSNSQVFHVY CDVISGSPWT LIQHRIDGSQ NFNETWENYK YGFGRLDGEF WLGLEKIYSI VKQSNYVLRI ELEDWKDNKH YIEYSFYLGN HETNYTLHLV AITGNVPNAI PENKDLVFST WDHKAKGHFN CPEGYSGGWW WHDECGENNL NGKYNKPRAK SKPERRRGLS WKSQNGRLYS IKSTKMLIHP TDSESFEHHH HHH.
What applications can ANGPTL3 Protein be used in?
ANGPTL3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ANGPTL3 Protein?
The endotoxin level is minimal, ANGPTL3 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 :
CFB-a HumanDescription:
Complement Factor B Fragment a Human
Complement factor B (EC:3.4.21.47), C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, Complement factor B Ba fragment, Complement factor B Bb fragment, CFB, Complement Factor B, BFD, AHUS4, BF, BFD, CFAB, FB, FBI12, H2-Bf.
Product # :
PRO-2735Price :
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Description
CFB-a Human produced in Human Plasma having a molecular mass of 33 kDa.
Source
Human Plasma.
Formulation
CFB-a solution (1mg/ml) contains Phosphate-buffered saline, pH 7.2.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Complement Factor B, also known as CFB, encodes complement factor B which is a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Once the alternative pathway is activated it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which connects with C3b to form the alternative pathway C3 convertase. Also, Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation.
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Synonyms
Complement factor B (EC:3.4.21.47), C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, Complement factor B Ba fragment, Complement factor B Bb fragment, CFB, Complement Factor B, BFD, AHUS4, BF, BFD, CFAB, FB, FBI12, H2-Bf.
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Physical Appearance
Sterile filtered solution.
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Stability
CFB-a Human is stable at 4°C if entire vial will be used within 2-4 weeks. Store, frozen below -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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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.
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 :
IRF3 HumanDescription:
IFN Regulatory Factor-3 Human Recombinant
IRF-3, IRF3, IFN Regulatory Factor 3.
Product # :
CYT-292Price :
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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
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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.
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Name :
NEFL HumanDescription:
Neurofilament Light Human Recombinant
Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.
Product # :
PRO-2584Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
NEFL Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (2-543 a.a) containing 551 amino acids including a 9 a.a N-terminal His tag. The total molecular mass is 62.5kDa (calculated).
Source
Escherichia Coli.
Formulation
NEFL filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in 15mM Tris and 85mM Glycine, pH 8.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
NEFL or Neurofilament light polypeptide is a protein that is encoded through the NEFL gene. NEFL is correlated to a disease called Charcot–Marie–Tooth. The protein’s light subunit is determined by immunoassays in the plasma and cerebrospinal fluid, if present, it can indicate on axonal damage in neurological diseases. By doing so, NEFL can act as a marker for Huntington's disease, Amyotrophic Lateral Sclerosis and multiple sclerosis.
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Synonyms
Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
MKHHHHHHAS SFSYEPYYST SYKRRYVETP RVHISSVRSG YSTARSAYSS YSAPVSSSLS VRRSYSSSSG SLMPSLENLD LSQVAAISND LKSIRTQEKA QLQDLNDRFA SFIERVHELE QQNKVLEAEL LVLRQKHSEP SRFRALYEQE IRDLRLAAED ATNEKQALQG EREGLEETLR NLQARYEEEV LSREDAEGRL MEARKGADEA ALARAELEKR IDSLMDEISF LKKVHEEEIA ELQAQIQYAQ ISVEMDVTKP DLSAALKDIR AQYEKLAAKN MQNAEEWFKS RFTVLTESAA KNTDAVRAAK DEVSESRRLL KAKTLEIEAC RGMNEALEKQ LQELEDKQNA DISAMQDTIN KLENELRTTK SEMARYLKEY QDLLNVKMAL DIEIAAYRKL LEGEETRLSF TSVGSITSGY SQSSQVFGRS AYGGLQTSSY LMSTRSFPSY YTSHVQEEQI EVEETIEAAK AEEAKDEPPS EGEAEEEEKD KEEAEEEEAA EEEEAAKEES EEAKEEEEGG EGEEGEETKE AEEEEKKVEG AGEEQAAKKK D.
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 :
TNFRSF14 Human, Sf9Description:
HVEM-Fc Human Recombinant, Sf9
Tumor necrosis factor receptor superfamily member 14 isoform 1, TNFRSF14, ATAR, CD270, HVEA, HVEM, LIGHTR, TR2, HVEM-Fc, Sf9, Tumor necrosis factor receptor superfamily member 14, Herpes virus entry mediator A, Herpesvirus entry mediator A, HveA.
Product # :
CYT-981Price :
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Description
TNFRSF14 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 406 amino acids (39-202) and having a molecular mass of 44.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).TNFRSF14 is fused to a 239 amino acid IgG His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TNFRSF14 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by analysis by SDS-PAGE.
Citations
More Info
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Introduction
TNFRSF14, a member of the TNF receptor superfamily, is a type I transmembrane protein. TNFRSF14 is expressed in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. TNFRSF14 operates as a co-stimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Additionally, TNFRSF14 encourages the proliferation of T cells, and triggers apoptosis of various tumor cells.
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Synonyms
Tumor necrosis factor receptor superfamily member 14 isoform 1, TNFRSF14, ATAR, CD270, HVEA, HVEM, LIGHTR, TR2, HVEM-Fc, Sf9, Tumor necrosis factor receptor superfamily member 14, Herpes virus entry mediator A, Herpesvirus entry mediator A, HveA.
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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
ADPLPSCKED EYPVGSECCP KCSPGYRVKE ACGELTGTVC EPCPPGTYIA HLNGLSKCLQ CQMCDPAMGL RASRNCSRTE NAVCGCSPGH FCIVQDGDHC AACRAYATSS PGQRVQKGGT ESQDTLCQNC PPGTFSPNGT LEECQHQTKC SWLVTKAGAG TSSSHWVLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK 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 :
IL1F10 Human HisDescription:
Interleukin 1 Family, Member 10 Human Recombinant, His Tag
Interleukin-1 family member 10, IL-1F10, FIL1 theta, Interleukin-1 HY2, IL-1HY2, Interleukin-1 theta, IL-1 theta, IL1F10, FIL1T, IL1HY2, FKSG75, MGC119831, MGC119832, MGC119833, FIL1-theta.
Product # :
CYT-783Price :
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Shipped with Ice Packs
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Description
IL1F10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (1-152) and having a molecular mass of 19.1kDa.IL1F10 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IL1F10 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Human interleukin family 1, member 10 (IL1F10) belongs to the interleukin 1 cytokine family. IL1F10 is expressed in the fetal skin, spleen and tonsil, generally in the basal epithelia of skin and in proliferating B-cells of the tonsil. IL1F10 binds soluble IL1 receptor type 1 and may be implicated in the regulation of adapted and innate immune responses.
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Synonyms
Interleukin-1 family member 10, IL-1F10, FIL1 theta, Interleukin-1 HY2, IL-1HY2, Interleukin-1 theta, IL-1 theta, IL1F10, FIL1T, IL1HY2, FKSG75, MGC119831, MGC119832, MGC119833, FIL1-theta.
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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 MCSLPMARYY IIKYADQKAL YTRDGQLLVG DPVADNCCAE KICTLPNRGL DRTKVPIFLG IQGGSRCLAC VETEEGPSLQ LEDVNIEELY KGGEEATRFT FFQSSSGSAF RLEAAAWPGW FLCGPAEPQQ PVQLTKESEP SARTKFYFEQ SW
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 :
TROVE2 Bovine, BiotinDescription:
TROVE Domain Family Member 2 Human Recombinant, Biotinlyated
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
Product # :
PRO-2561Price :
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Description
TROVE2 is a biotinlyated natural protein having a molecular mass of 58kDa. TROVE2 is purified from bovine tissues by protein-chemical methods.
Source
Bovine tissues.
Formulation
TROVE2 is supplied in 20mM HEPES buffer pH-8.0, 150mM NaCl and 20% glycerol.
Purity
Greater than 83.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.
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Synonyms
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
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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. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Follistatin HumanDescription:
Follistatin Human Recombinant
FST, FS
Product # :
CYT-232Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Follistatin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids and having a total molecular mass of 31.5kDa.The FST is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.
Citations
More Info
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Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin functions as an ACTV antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
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Synonyms
FST, FS
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Follistatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FST 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 Follistatin 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 Gly-Asn-Cys-Trp-Leu.
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Background
What is the molecular weight/Mw of FOLLISTATIN HUMAN Protein?
FOLLISTATIN HUMAN Protein has a total Mw of 31.5kDa.
What is the source or expression system of FOLLISTATIN HUMAN Protein?
Escherichia Coli.
What is the Purity of FOLLISTATIN HUMAN Protein?
FOLLISTATIN HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FOLLISTATIN HUMAN Protein?
The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.
What is the amino acid sequence of FOLLISTATIN HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.
What applications can FOLLISTATIN HUMAN Protein be used in?
FOLLISTATIN HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FOLLISTATIN HUMAN Protein?
The endotoxin level is minimal, FOLLISTATIN 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 :
TGFB3 (207 a.a.) HumanDescription:
Transforming Growth Factor-Beta 3 (207 a.a.) Human Recombinant
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
Product # :
CYT-319Price :
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Shipping Method :
Shipped with Ice Packs
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Description
TGFB3 Human Recombinant protein encoding amino acids 644-850 and total molecular mass of 50 kDa (Including GST Tag).
Source
Escherichia Coli.
Formulation
100µl purified human TGF Beta 3protein at 100µg/ml in 50mM Tris-Acetate, pH-7.5, 1mM EDTA and 20% Glycerol.
Citations
More Info
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Introduction
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
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Synonyms
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
TGF-beta 3 Human Recombinant although stable at 4°C for 1 week, should be stored at -20°C. 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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Applications
(a) ELISA.
(b) Western Blotting.
(c) Inhibition Assays.
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 :
TRIM28 HumanDescription:
Tripartite Motif Containing 28 Human Recombinant
Transcription intermediary factor 1-beta, TIF1-beta, E3 SUMO-protein ligase TRIM28, KRAB-associated protein 1, KAP-1, KRAB-interacting protein 1, KRIP-1, Nuclear corepressor KAP-1, RING finger protein 96, Tripartite motif-containing protein 28, TRIM28, KAP1, RNF96, TIF1B, Tripartite motif containing 28, RNF96, TF1B.
Product # :
PRO-1697Price :
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Description
TRIM28 Human Recombinant produced in E. coli is a single polypeptide chain containing 460 amino acids (366-802) and having a molecular mass of 48.7 kDa.TRIM28 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TRIM28 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Tripartite Motif Containing 28 (TRIM28) which is a member of the tripartite motif family includes 3 zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. TRIM28 mediates transcriptional control by interaction with the Kruppel-associated box repression domain found in many transcription factors. TRIM28 is restricted to the nucleus and connected with particular chromatin regions.
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Synonyms
Transcription intermediary factor 1-beta, TIF1-beta, E3 SUMO-protein ligase TRIM28, KRAB-associated protein 1, KAP-1, KRAB-interacting protein 1, KRIP-1, Nuclear corepressor KAP-1, RING finger protein 96, Tripartite motif-containing protein 28, TRIM28, KAP1, RNF96, TIF1B, Tripartite motif containing 28, RNF96, TF1B.
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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 MGSKLIYFQL HRALKMIVDP VEPHGEMKFQ WDLNAWTKSA EAFGKIVAER PGTNSTGPAP MAPPRAPGPL SKQGSGSSQP MEVQEGYGFG SGDDPYSSAE PHVSGVKRSR SGEGEVSGLM RKVPRVSLER LDLDLTADSQ PPVFKVFPGS TTEDYNLIVI ERGAAAAATG QPGTAPAGTP GAPPLAGMAI VKEEETEAAI GAPPTATEGP ETKPVLMALA EGPGAEGPRL ASPSGSTSSG LEVVAPEGTS APGGGPGTLD DSATICRVCQ KPGDLVMCNQ CEFCFHLDCH LPALQDVPGE EWSCSLCHVL PDLKEEDGSL SLDGADSTGV VAKLSPANQR KCERVLLALF CHEPCRPLHQ LATDSTFSLD QPGGTLDLTL IRARLQEKLS PPYSSPQEFA QDVGRMFKQF NKLTEDKADV QSIIGLQRFF ETRMNEAFGD.
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 :
KLK3 Human, NativeDescription:
Kallikrein-3 Human
Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1
Product # :
ENZ-1172Price :
Quantity :
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Shipped with Ice Packs
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Description
Human Kallikrein-3 produced in Human seminal fluid having a molecular mass of approximately 30kD.
Source
Human seminal fluid.
Formulation
The protein solution (0.2 µm filtered) is in 0.09% NaN3, 0.05M phosphate buffer, 150mM NaCl, pH 7.5.
Purity
Greater than 96.0%.
Citations
More Info
-
Introduction
Kallikrein-3 (KLK3) is a part of the kallikrein-related peptidase family. Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins take part in carcinogenesis and some may be prospective cancer and other disease biomarkers. Kallikrein-3 is 1 of the 15 kallikrein subfamily members located in a cluster on chromosome 19 and is a protease present in seminal plasma. KLK3 hydrolyzes semenogelin-1 consequently leading to the liquefaction of the seminal coagulum. KLK3 acts normally in the liquefaction of seminal coagulum, probably by hydrolysis of the high molecular mass seminal vesicle protein. Serum level of the KLK3 protein, called PSA in the clinical setting, is beneficial in the diagnosis and monitoring of prostatic carcinoma.
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Synonyms
Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Human Kallikrein-3 should be stored at 2-8°C. Do not freeze!
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Human Virus Test
Starting material donor has been tested and certified negative for antibodies to HIV-1, HIV-2, HCV, HBSAG, Syphilis and HIV/HBV/HCV (PCR).
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 Rat, PEGDescription:
Leptin Quadruple Antagonist, Pegylated Rat Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1241Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Pegylated Quadruple Antagonist Rat Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids. The Rat Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Rat Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Rat 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
Rat 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.
Citations
More Info
-
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Rat 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 rat pegylated leptin antagonist and filter sterilization rat 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 Rat Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin is a hormone which mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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 :
GDF11 Human, HisDescription:
Growth and Differentiation factor 11 Human Recombinant, His Tag
Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.
Product # :
CYT-887Price :
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Description
GDF11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids (299-407a.a) and having a molecular mass of 14.8kDa. GDF11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDF11 protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GDF-11 belongs to the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. GDF-11 is a central developmental factor which controls muscular and neural development. In adults, GDF-11 encourages cardiac hypertrophy reverse by the revival of cardiomyocytes.
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Synonyms
Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.
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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 MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.
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Background
What is the molecular weight/Mw of GDF11 HUMAN, HIS Protein?
GDF11 HUMAN, HIS Protein has a total Mw of 14.8kDa.
What is the source or expression system of GDF11 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of GDF11 HUMAN, HIS Protein?
GDF11 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF11 HUMAN, HIS Protein?
The biological functionality of GDF11 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of GDF11 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.
What applications can GDF11 HUMAN, HIS Protein be used in?
GDF11 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF11 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF11 HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IGF1 Human Des1-3Description:
Insulin-Like Growth Factor 1 Des (1-3) Human Recombinant
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF, Des(1-3), Des1-3, Des 1-3, Des (1-3), IGF-1 (4-70).
Product # :
CYT-518Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IGF-I Des(1-3) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 67 amino acids (aa 4-70) and having a molecular mass of 7368.5 Dalton. IGF-1 Des1-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) was lyophilized was lyophilized from a 0.2µm filtered concentrated solution in 20mM PBS, pH 7.0.
Purity
Greater than 97% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using FDC-P1 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5×105 units/mg.Citations
More Info
-
Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
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Synonyms
Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF, Des(1-3), Des1-3, Des 1-3, Des (1-3), IGF-1 (4-70).
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IGF-I des(1-3) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 des-1-3 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 IGF-I des(1-3) 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
TLCGAELVDA LQFVCGDRGF YFNKPTGYGS SSRRAPQTGI VDECCFRSCD LRRLEMYCAP LKPAKSA.
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Background
What is the molecular weight/Mw of IGF1 HUMAN DES1-3 Protein?
IGF1 HUMAN DES1-3 Protein has a total Mw of 7.3kDa.
What is the source or expression system of IGF1 HUMAN DES1-3 Protein?
Escherichia Coli.
What is the Purity of IGF1 HUMAN DES1-3 Protein?
IGF1 HUMAN DES1-3 Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of IGF1 HUMAN DES1-3 Protein?
The ED50 as determined by a cell proliferation assay using FDC-P1 cells is less than 2.0 ng/ml, corresponding to a specific activity of > 5×105 units/mg.
What is the amino acid sequence of IGF1 HUMAN DES1-3 Protein?
TLCGAELVDA LQFVCGDRGF YFNKPTGYGS SSRRAPQTGI VDECCFRSCD LRRLEMYCAP LKPAKSA.
What applications can IGF1 HUMAN DES1-3 Protein be used in?
IGF1 HUMAN DES1-3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IGF1 HUMAN DES1-3 Protein?
The endotoxin level is minimal, IGF1 HUMAN DES1-3 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 :
KLK3 AntibodyDescription:
Kallikrein-3, Mouse Anti Human
Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1.
Product # :
ANT-088Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
Citations
More Info
-
Introduction
Kallikrein-3 (KLK3) belongs to the kallikrein-related peptidase family. Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins are involved in carcinogenesis and some may be prospective cancer and other disease biomarkers. Kallikrein-3 is 1 of the 15 kallikrein subfamily members located in a cluster on chromosome 19 and is a protease present in seminal plasma. KLK3 hydrolyzes semenogelin-1 consequently leading to the liquefaction of the seminal coagulum. KLK3 is assumed to act normally in the liquefaction of seminal coagulum, probably by hydrolysis of the high molecular mass seminal vesicle protein. Serum level of the KLK3 protein, called PSA in the clinical setting, is beneficial in the diagnosis and monitoring of prostatic carcinoma.
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Synonyms
Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1.
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Immunogen
Anti-human KLK3 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human KLK3 amino acids 25-261 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and ? light chain.
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Clone
P1D10AT.
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Applications
KLK3 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 dilution range for Western blot analysis is 1:500 ~ 1:5000.
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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
KLK3 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.
- View Data Sheet
Name :
Leptin Super Antagonist RatDescription:
Leptin Super Antagonist Rat Recombinant
Product # :
CYT-1240Price :
Quantity :
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Shipped at Room temp
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Description
Super Leptin Antagonist Rat Recombinant is a single polypeptide chain containing 146 amino acids. Super Rat Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A super Rat leptin antagonist that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/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
ProSpec’s super Rat leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Super Rat leptin antagonist also inhibits various leptin effects in several in vitro bioassays.
Citations
More Info
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Super Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of super Rat leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super Rat leptin antagonist can be stored at 4C 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 Super Leptin Antagonist 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-His.
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Background
Leptin is a hormone which takes part in regulating body weight, metabolism and reproductive function and is encoded by the obese gene. Leptin is expressed predominantly by adipocytes, which fits with 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 expressed mainly in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.
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 :
TGFB2 Human, CHODescription:
Transforming Growth Factor-Beta 2 Human Recombinant, CHO
Transforming growth factor beta-2, TGF-beta-2, G-TSF, Tgfb-2, TGFbeta2.
Product # :
CYT-1268Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TGFB2 Human Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.4kDa.
TGFB2 Human Recombinant is purified by proprietary chromatographic techniques.Source
CHO Cells.
Formulation
The protein was lyophilized with 0.1% (v/v) TFA and 35% (v/v) Acetonitrile.
Purity
Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.
Biological Activity
The biological activity was determined by TGFB2 ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is <0.2 ng/ml, corresponding to a specific activity of ≥ 5.0 × 106 units/mg.Citations
More Info
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Synonyms
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transforming Growth Factor-Beta 2 should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Transforming Growth Factor-Beta 2 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHSR VLSLYNTINP EASASPCCVS QDLEPLTILY YIGKTPKIEQ LSNMIVKSCK CS.
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Background
Recombinant TGFB2 protein is used in cell culture to study extracellular matrix remodelling, tissue regeneration, and developmental biology.
TGFB2 takes part in embryonic development and is involved in fibrosis, wound healing, angiogenesis,
What is the molecular weight / Mw of TGFB2 Protein?
TGFB2 Protein has a total Mw of 25.4kDa.
What is the source or expression system of TGFB2 Protein?
CHO Cells
What is the Purity of TGFB2 Protein?
TGFB2 Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of TGFB2 Protein?
Determined by its ability to inhibit the mouse IL4-dependent proliferation of mouse HT2 cells. The expected ED50 for this effect is less than 0.2ng/ml, corresponding to a specific activity of ≥ 5.0 × 106 units/mg.
What is the amino acid sequence of TGFB2 Protein?
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHSR VLSLYNTINP EASASPCCVS QDLEPLTILY YIGKTPKIEQ LSNMIVKSCK CS
What applications can TGFB2 Protein be used in?
TGFB2 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for TGFB2 Protein?
The endotoxin level is minimal, TGFB2 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 :
EIF2S1 AntibodyDescription:
Eukaryotic Translation Initiation Factor 2 Subunit 1 Alpha, Mouse Anti Human
Eukaryotic translation initiation factor 2 subunit 1, Eukaryotic translation initiation factor 2 subunit alpha, eIF-2-alpha, EIF-2alpha, EIF-2A, EIF2, EIF-2, EIF2A, EIF-2A.
Product # :
ANT-059Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
Citations
More Info
-
Introduction
EIF2S1 participates in the premature steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA which binds to a 40S ribosomal subunit, followed by mRNA binding to create a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 should exchange with GTP by way of a reaction catalyzed by eIF-2B.
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Synonyms
Eukaryotic translation initiation factor 2 subunit 1, Eukaryotic translation initiation factor 2 subunit alpha, eIF-2-alpha, EIF-2alpha, EIF-2A, EIF2, EIF-2, EIF2A, EIF-2A.
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Immunogen
Anti-human EIF2S1 mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human EIF2S1 amino acids 1-315 purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and kappa light chain.
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Clone
PEIF2S1AT.
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Applications
EIF2S1 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 1:1,000. -
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
EIF2S1 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.
- View Data Sheet
Name :
KLK8 MouseDescription:
Kallikrein-8 Mouse Recombinant
Ovasin, PRSS19, TADG14, NRPN, NP, Kallikrein 8 (Neuropsin/Ovasin) 2 EC 3.4.21.118, Kallikrein-8, Neuropsin, EC 3.4.21 61, HNP, HK8
Product # :
ENZ-1014Price :
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Shipped with Ice Packs
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Description
KLK8 Mouse Recombinant produced in Sf9 is a single, glycosylated polypeptide chain containing 240 amino acids (29-260) and having a molecular mass of 26.5kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). The KLK8 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
KLK8 protein 0.5mg/ml is supplied in PBS, pH-7.4, and 10% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Kallikrein-8 is a serine protease which degrades various proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. Kallikrein-8 takes part in the formation and maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway, regulates Schaffer-collateral long-term potentiation in the hippocampus and is essential for memory acquisition and synaptic plasticity. Kallikrein-8 participates in the secondary phase of pathogenesis following spinal cord injury and also takes part in skin desquamation and keratinocyte proliferation.
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Synonyms
Ovasin, PRSS19, TADG14, NRPN, NP, Kallikrein 8 (Neuropsin/Ovasin) 2 EC 3.4.21.118, Kallikrein-8, Neuropsin, EC 3.4.21 61, HNP, HK8
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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
QGSKILEGRE CIPHSQPWQA ALFQGERLIC GGVLVGDRWV LTAAHCKKQK YSVRLGDHSL QSRDQPEQEI QVAQSIQHPC YNNSNPEDHS HDIMLIRLQN SANLGDKVKP VQLANLCPKV GQKCIISGWG TVTSPQENFP NTLNCAEVKI YSQNKCERAY PGKITEGMVC AGSSNGADTC QGDSGGPLVC DGMLQGITSW GSDPCGKPEK PGVYTKICRY TTWIKKTMDN RDLEHHHHHH.
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 :
LCAT Human, HEKDescription:
Lecithin-Cholesterol Acyltransferase Human Recombinant, HEK
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.
Product # :
ENZ-254Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
LCAT Human Recombinant produced in HEK is a single, glycosylated, polypeptide chain containing 429 amino acids (25-440) which includes a 13 amino acid Flag Tag fused at N-terminus and having a total molecular mass of 48.5 kDa. LCAT Human Recombinant is purified by proprietary chromatographic techniques.
Source
Human Embryonic Kidney 293 cells
Formulation
The LCAT protein was lyophilized from 0.4um filtered solution at a concentration of 0.5mg/ml containing 20mM Tris buffer, and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
LCAT is an extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. LCAT is a essential enzyme in the extracellular metabolism of plasma lipoproteins.
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Synonyms
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LCAT although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LCAT 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
Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. LCAT HEK 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
HVDYKDDDDK PAGFWLLNVL FPPHTTPKAE LSNHTRPVIL VPGCLGNQLE AKLDKPDVVN WMCYRKTEDF FTIWLDLNMF LPLGVDCWID NTRVVYNRSS GLVSNAPGVQ IRVPGFGKTY SVEYLDSSKL AGYLHTLVQN LVNNGYVRDE TVRAAPYDWR LEPGQQEEYY RKLAGLVEEM HAAYGKPVFL IGHSLGCLHL LYFLLRQPQA WKDRFIDGFI SLGAPWGGSI KPMLVLASGD NQGIPIMSSI KLKEEQRITT TSPWMFPSRM AWPEDHVFIS TPSFNYTGRD FQRFFADLHF EEGWYMWLQS RDLLAGLPAP GVEVYCLYGV GLPTPRTYIY DHGFPYTDPV GVLYEDGDDT VATRSTELCG LWQGRQPQPV HLLPLHGIQH LNMVFSNLTL EHINAILLGA YRQGPPASPT ASPEPPPPE
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 :
OTUB1 HumanDescription:
Ubiquitin Aldehyde Binding 1 Human Recombinant
Ubiquitin thioesterase OTUB1, Otubain-1, OTU domain-containing ubiquitin aldehyde-binding protein 1, Ubiquitin-specific-processing protease OTUB1, Deubiquitinating enzyme OTUB1, OTUB1, OTB1, OTU1, HSPC263, MGC4584, FLJ20113, FLJ40710, MGC111158.
Product # :
PRO-711Price :
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Shipping Method :
Shipped with Ice Packs
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Description
OTUB1 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 291 amino acids (1- 271 a.a.) and having a molecular mass of 33.4kDa.The OTUB1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OTUB1 solution contains 20mM Tris buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Otubain 1 (OTUB1) belongs to the ovarian tumor (OUT) superfamily of predicted cysteine proteases and inhibits cytokine gene transcription in the immune system through its interaction with a ubiquitin protease and E3 ubiquitin ligase. OTUB1 is a highly specific ubiquitin iso-peptidase, it cleaves ubiquitin from branched poly-ubiquitin chains but not from ubiquitinated substrates. OTUB1 is believed to work in specific ubiquitin-dependent pathways, possibly by providing an editing function of polyubiquitin chain growth. OTUB1 is a hydrolase that removes conjugated ubiquitin from proteins in vitro and may therefore have a significant regulatory role in the level of protein turnover by preventing degradation. Additionally, OTUB1 is a regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered impassive to antigen re-challenge and no longer respond to their cognate antigen. OTUB1 acts via its interaction with RNF128/GRAIL, which is an essential inductor of CD4 T-cell anergy.
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Synonyms
Ubiquitin thioesterase OTUB1, Otubain-1, OTU domain-containing ubiquitin aldehyde-binding protein 1, Ubiquitin-specific-processing protease OTUB1, Deubiquitinating enzyme OTUB1, OTUB1, OTB1, OTU1, HSPC263, MGC4584, FLJ20113, FLJ40710, MGC111158.
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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 MAAEEPQQQK QEPLGSDSEG VNCLAYDEAI MAQQDRIQQE IAVQNPLVSE RLELSVLYKE YAEDDNIYQQ KIKDLHKKYS YIRKTRPDGN CFYRAFGFSH LEALLDDSKE LQRFKAVSAK SKEDLVSQGF TEFTIEDFHN TFMDLIEQVE KQTSVADLLA SFNDQSTSDY LVVYLRLLTS GYLQRESKFF EHFIEGGRTV KEFCQQEVEP MCKESDHIHI IALAQALSVS IQVEYMDRGE GGTTNPHIFP EGSEPKVYLL YRPGHYDILY K.
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 :
G CSF Human, HisDescription:
Granulocyte-Colony Stimulating Factor Human Recombinant, His Tag
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Product # :
CYT-476Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Granulocyte Colony Stimulating Factor-His Tag Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids, fragment (31-204) and having a molecular mass of 23.19 kDa with an amino-terminal hexahistidine tag.G-CSF-His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Granulocyte Colony Stimulating Factor His is supplied in 1x PBS and 50% glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
Granulocyte Colony Stimulating Factor is a growth factor and/or cytokine produced by the endothelium, macrophages and a number of other immune cells. GCSF stimulates the bone marrow to produce granulocytes and also to stimulate the survival, proliferation, differentiation and function of neutrophil granulocyte progenator cells and mature neutrophils.
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Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
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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. Please avoid freeze thaw cycles.
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Background
What is the molecular weight/Mw of G CSF Protein?
G CSF Protein has a total Mw of 23.19kDa.
What is the source or expression system of G CSF Protein?
Escherichia Coli.
What is the Purity of G CSF Protein?
G CSF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of G CSF Protein?
The biological functionality of G CSF Protein will be determined in the future.
What is the amino acid sequence of G CSF Protein?
G CSF Protein is composed from 174 amino acids.
What applications can G CSF Protein be used in?
G CSF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for G CSF Protein?
The endotoxin level is minimal, G CSF 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 :
Fibronectin RecombinantDescription:
Fibronectin Human Recombinant
Product # :
PRO-2621Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Fibronectin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 574 amino acids and having a molecular mass of 62.6kDa. The Fibronectin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in 20 mM Tris-HCl, pH 8.0, 150 mM NaCl, with 5 % Trehalose and 0.02 % Tween-20.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Was measured by its ability to support cell attachment and spreading when used as a substratum for cell culture. The recommended concentration in this application for this effect is typically 1-5 μg/cm2. Fibronectin can also be added to the media to support cell spreading at a concentration of 0.5-50 μg/ml. Optimal concentrations will need to be determined for individual user applications.
Citations
More Info
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Introduction
Fibronectin takes part in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion.Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism (VTE) particularly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin consists in 2 main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the etracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin alos takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Fibronectin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibronectin 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 Fibronectin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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 :
IGF1 MouseDescription:
Insulin-Like Growth Factor 1 Mouse Recombinant
Somatomedin C, IGF-I, IGFIA, IGF1.
Product # :
CYT-229Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Insulin-Like Growth Factor I mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7600 Dalton. IGF-I is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 1.0 ng/ml, corresponding to a specific activity of 1MU/mg.Citations
More Info
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Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
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Synonyms
Somatomedin C, IGF-I, IGFIA, IGF1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IGFI although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF-1 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 IGF1 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 Gly-Pro-Glu-Thr-Leu.
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Background
What is the molecular weight/Mw of IGF1 MOUSE Protein?
IGF1 MOUSE Protein has a total Mw of 7.6kDa.
What is the source or expression system of IGF1 MOUSE Protein?
Escherichia Coli.
What is the Purity of IGF1 MOUSE Protein?
IGF1 MOUSE Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of IGF1 MOUSE Protein?
The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 1.0 ng/ml, corresponding to a specific activity of 1MU/mg.
What is the amino acid sequence of IGF1 MOUSE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Pro-Glu-Thr-Leu.
What applications can IGF1 MOUSE Protein be used in?
IGF1 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IGF1 MOUSE Protein?
The endotoxin level is minimal, IGF1 MOUSE Protein was purified using conventional chromatography techniques.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.47 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 calibrated solution of IGF-I 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.