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Search results

1000 results found for “transferrin”

Name

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  • View Data Sheet

    Name :

    NAA30 Human

    Description:

    N Alpha-Acetyltransferase 30, NatC Catalytic Subunit Human Recombinant

    N(Alpha)-Acetyltransferase 30, NatC Catalytic Subunit, C14orf35, NAT12, N-Acetyltransferase 12 (GCN5-Related, Putative), N-Acetyltransferase 12, NatC Catalytic Subunit, MAK3, N-Acetyltransferase MAK3 Homolog, Chromosome 14 Open Reading Frame 35, Mak3p, NAT12P, N-Alpha-Acetyltransferase 30, N-Alpha-Acetyltransferase 30, NatC Catalytic Subunit, Putative N-Acetyltransferase, EC 2.3.1.88.

    Product # :

    ENZ-720

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    Description

    NAA30 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 385 amino acids (1-362 a.a) and having a molecular mass of 41.7kDa.NAA30 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAA30 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      N-alpha-acetyltransferase 30 (NAA30) is catalytic subunit of the N-terminal acetyltransferase C (NatC) complex. NAA30 catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly. In addition, NAA30 is essential for the lysosomal localization and function of ARL8B. The disease Eastern equine encephalitis has been associated with NAA30.

    • Synonyms

      N(Alpha)-Acetyltransferase 30, NatC Catalytic Subunit, C14orf35, NAT12, N-Acetyltransferase 12 (GCN5-Related, Putative), N-Acetyltransferase 12, NatC Catalytic Subunit, MAK3, N-Acetyltransferase MAK3 Homolog, Chromosome 14 Open Reading Frame 35, Mak3p, NAT12P, N-Alpha-Acetyltransferase 30, N-Alpha-Acetyltransferase 30, NatC Catalytic Subunit, Putative N-Acetyltransferase, EC 2.3.1.88.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAEVPPG PSSLLPPPAP PAPAAVEPRC PFPAGAALAC CSEDEEDDEE HEGGGSRSPA GGESATVAAK GHPCLRCPQP PQEQQQLNGL ISPELRHLRA AASLKSKVLS VAEVAATTAT PDGGPRATAT KGAGVHSGER PPHSLSSNAR TAVPSPVEAA AASDPAAARN GLAEGTEQEE EEEDEQVRLL SSSLTADCSL RSPSGREVEP GEDRTIRYVR YESELQMPDI MRLITKDLSE PYSIYTYRYF IHNWPQLCFL AMVGEECVGA IVCKLDMHKK MFRRGYIAML AVDSKYRRNG IGTNLVKKAI YAMVEGDCDE VVLETEITNK SALKLYENLG FVRDKRLFRY YLNGVDALRL KLWLR

    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.

    Naa30 Human
  • View Data Sheet

    Name :

    SNX1 Human

    Description:

    Sorting Nexin 1 Human Recombinant

    HsT17379, SNX1A, Vps5.

    Product # :

    PRO-665

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    Description

    SNX1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 415 amino acids (146-522 a.a.) and having a molecular mass of 48 kDa. SNX1 is fused to 38 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SNX1 0.25mg/ml solution contains 20mM Tris-HCl buffer pH-8, 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SNX1 belongs to the large family of hydrophilic proteins that interact with a range of receptor types that participate in intracellular trafficking. SNX1 and the associated splice variant, SNX1A, bind the EGFR, enable its transport to the lysosome, and thus contribute to the degradation of the receptor. SNX1 is related with cellular membranes, and they, also, associate with EGF, PDGF and the receptor tyrosine kinases.

    • Synonyms

      HsT17379, SNX1A, Vps5.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      SNX1 although stable at 4°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.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGGSMTV GITDPEKIGD GMNAYVAYKV TTQTSLPLFR SKQFAVKRRF SDFLGLYEKL
      SEKHSQNGFI VPPPPEKSLI GMTKVKVGKE DSSSAEFLEK RRAALERYLQ RIVNHPTMLQ DPDVREFLEK EELPRAVGTQ TLSGAGLLKM
      FNKATDAVSK MTIKMNESDI WFEEKLQEVE CEEQRLRKLH AVVETLVNHR KELALNTAQF AKSLAMLGSS EDNTALSRAL SQLAEVEEKI
      EQLHQEQANN DFFLLAELLS DYIRLLAIVR AAFDQRMKTW QRWQDAQATL QKKREAEARL LWANKPDKLQ QAKDEILEWE SRVTQYERDF
      ERISTVVRKE VIRFEKEKSK DFKNHVIKYL ETLLYSQQQL AKYWEAFLPE AKAIS.

    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.

    Snx1 Human
  • View Data Sheet

    Name :

    EFNB2 Mouse

    Description:

    Ephrin- B2 Mouse Recombinant

    Ephrin-B2, ELF-2, EPH-related receptor tyrosine kinase ligand 5, LERK-5, HTK ligand, HTK-L, Elf2, Eplg5, Htkl, Lerk5, Efnb2, ELF-2, Epl5, Eplg5, Htk-L, Lerk5, NLERK-1, EFNB2.

    Product # :

    PRO-2246

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    Description

    EFNB2 Mouse Recombinant produced in Sf9 Baculovirus cells is a single polypeptide chain containing 212 amino acids (29-232) and having a molecular mass of 23.4kDa.(Molecular size on SDS-PAGE will appear at approximately 28-40KDa).EFNB2 is fused to 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The EFNB2 solution (0.5mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ephrin-B2 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors contain the largest subfamily of receptor protein-tyrosine kinases and have been associated with mediating developmental events, particularly in the nervous system and in erythropoiesis. Based upon their structures and sequence relationships, ephrins are allocated into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. Ephrin-B2 binds to the EPHB4 and EPHA3 receptors.

    • Synonyms

      Ephrin-B2, ELF-2, EPH-related receptor tyrosine kinase ligand 5, LERK-5, HTK ligand, HTK-L, Elf2, Eplg5, Htkl, Lerk5, Efnb2, ELF-2, Epl5, Eplg5, Htk-L, Lerk5, NLERK-1, EFNB2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      RSIVLEPIYW NSSNSKFLPG QGLVLYPQIG DKLDIICPKV DSKTVGQYEY YKVYMVDKDQ ADRCTIKKEN TPLLNCARPD QDVKFTIKFQ EFSPNLWGLE FQKNKDYYII STSNGSLEGL DNQEGGVCQT RAMKILMKVG QDASSAGSAR NHGPTRRPEL EAGTNGRSST TSPFVKPNPG SSTDGNSAGH SGNNLLGSEV ALFALEHHHH HH.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Efnb2 Mouse
  • View Data Sheet

    Name :

    Erythropoietin Human, Active

    Description:

    Erythropoietin Receptor Human Recombinant, Active

    EPO-R, EPOR, Erythropoietin Receptor.

    Product # :

    CYT-997

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    Description

    EPOR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 232 amino acids (25-250a.a.) and having a molecular mass of 25.6kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).EPOR is expressed with a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    EPOR protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    Measured by its ability to inhibit EPO dependent proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect less or equal to 70ng/ml.

    More Info

    • Introduction

      Erythropoietin receptor, also known as EPOR arbitrates erythropoietin-induced erythroblast proliferation as well as differentiation. During EPO binding, EPOR activates Jak2 tyrosine kinase which activates various intracellular pathways including: Ras/MAP kinase, phosphatidylinositol 3-kinase and STAT transcription factors. Furthermore, stimulated EPOR has a function in erythroid cell survival. Mutations in EPOR may possibly produce erythroleukemia and familial erythrocytosis. In addition, dysregulation of EPOR can affect on the growth of selected tumors.

    • Synonyms

      EPO-R, EPOR, Erythropoietin Receptor.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      APPPNLPDPK FESKAALLAA RGPEELLCFT ERLEDLVCFW EEAASAGVGP GNYSFSYQLE DEPWKLCRLH QAPTARGAVR FWCSLPTADT SSFVPLELRV TAASGAPRYH RVIHINEVVL LDAPVGLVAR LADESGHVVL RWLPPPETPM TSHIRYEVDV SAGNGAGSVQ RVEILEGRTE CVLSNLRGRT RYTFAVRARM AEPSFGGFWS AWSEPVSLLT PSDLDPHHHH HH.

    • Background

      What is the molecular weight/Mw of ERYTHROPOIETIN Protein?
      ERYTHROPOIETIN Protein has a total Mw of 25.6kDa.

      What is the source or expression system of ERYTHROPOIETIN Protein?
      Sf9, Baculovirus cells.

      What is the Purity of ERYTHROPOIETIN Protein?
      ERYTHROPOIETIN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of ERYTHROPOIETIN Protein?
      Measured by its ability to inhibit EPO dependent proliferation assay using TF-1 human erythroleukemic cells. The ED50 for this effect less or equal to 70ng/ml.

      What is the amino acid sequence of ERYTHROPOIETIN Protein?
      APPPNLPDPK FESKAALLAA RGPEELLCFT ERLEDLVCFW EEAASAGVGP GNYSFSYQLE DEPWKLCRLH QAPTARGAVR FWCSLPTADT SSFVPLELRV TAASGAPRYH RVIHINEVVL LDAPVGLVAR LADESGHVVL RWLPPPETPM TSHIRYEVDV SAGNGAGSVQ RVEILEGRTE CVLSNLRGRT RYTFAVRARM AEPSFGGFWS AWSEPVSLLT PSDLDPHHHH HH.

      What applications can ERYTHROPOIETIN Protein be used in?
      ERYTHROPOIETIN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for ERYTHROPOIETIN Protein?
      The endotoxin level is minimal, ERYTHROPOIETIN 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.

    Epor Human Sf9
  • View Data Sheet

    Name :

    STX1A (1-265) Human

    Description:

    Syntaxin-1A (1-265 a.a) Human Recombinant

    Syntaxin 1A, Neuron-Specific Antigen HPC-1, Syntaxin 1A (Brain), STX1, Syntaxin-1A, HPC-1, P35-1, SYN1A.

    Product # :

    PRO-2335

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    Description

    STX1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 265 amino acids (1-265 a.a) and having a molecular mass of 30.7kDa. STX1A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STX1A protein solution (1mg/ml) containing phosphate buffered saline (pH 7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Syntaxin is membrane integrated Q-SNARE protein participating in exocytosis. Syntaxin is composed of an N-terminal regulatory domain (Habc), a SNARE domain (known as H3), and a single C-terminal transmembrane domain. The SNARE (H3) domain binds to both synaptobrevin and SNAP-25 forming the core SNARE complex. Synaptic vesicles store neurotransmitters that are released during calcium-regulated exocytosis. The specificity of neurotransmitter release requires the localization of both synaptic vesicles and calcium channels to the presynaptic active zone. Syntaxins function in this vesicle fusion process. Syntaxins also serve as a substrate for botulinum neurotoxin type C, a metalloprotease that blocks exocytosis and has high affinity for a molecular complex that includes the alpha-latrotoxin receptor which produces exocytosis.

    • Synonyms

      Syntaxin 1A, Neuron-Specific Antigen HPC-1, Syntaxin 1A (Brain), STX1, Syntaxin-1A, HPC-1, P35-1, SYN1A.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MKDRTQELRT AKDSDDDDDV AVTVDRDRFM DEFFEQVEEI RGFIDKIAEN VEEVKRKHSA ILASPNPDEK TKEELEELMS DIKKTANKVR SKLKSIEQSI EQEEGLNRSS ADLRIRKTQH STLSRKFVEV MSEYNATQSD YRERCKGRIQ RQLEITGRTT TSEELEDMLE SGNPAIFASG IIMDSSISKQ ALSEIETRHS EIIKLENSIR ELHDMFMDMA MLVESQGEMI DRIEYNVEHA VDYVERAVSD TKKAVKYQSK ARRKK.

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    Stx1A 1 265 Human
  • View Data Sheet

    Name :

    PCSK1N Human

    Description:

    Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor Human Recombinant

    ProSAAS precursor, Proprotein convertase subtilisin/kexin type 1 inhibitor, PROSAAS; SAAS, PCSK1N.

    Product # :

    PRO-1819

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    Description

    PCSK1N Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 251 amino acids (34-260) and having a molecular mass of 26.6 kDa.PCSK1N is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PCSK1N solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor (PCSK1N) takes part in the control of the neuroendocrine secretory pathway. PCSK1N inhibits prohormone convertase 1, which regulates the proteolytic cleavage of neuroendocrine peptide precursors. PCSK1Nslows down convertase-mediated processing of proopiomelanocortin and proenkephalin and also monitors the intracellular timing of PCSK1.

    • Synonyms

      ProSAAS precursor, Proprotein convertase subtilisin/kexin type 1 inhibitor, PROSAAS; SAAS, PCSK1N.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMARPVKE PRGLSAASPP LAETGAPRRF RRSVPRGEAA GAVQELARAL AHLLEAERQE RARAEAQEAE DQQARVLAQL LRVWGAPRNS DPALGLDDDP DAPAAQLARA LLRARLDPAA LAAQLVPAPV PAAALRPRPP VYDDGPAGPD AEEAGDETPD VDPELLRYLL GRILAGSADS EGVAAPRRLR RAADHDVGSE LPPEGVLGAL LRVKRLETPA PQVPARRLLP P.

    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.

    Pcsk1N Human
  • View Data Sheet

    Name :

    IL18RAP Human

    Description:

    Interleukin 18 Receptor Accessory Protein Human Recombinant

    Interleukin-18 receptor accessory protein, IL-18 receptor accessory protein, IL-18RAcP, Accessory protein-like, AcPL, CD218 antigen-like family member B, CDw218b, IL-1R accessory protein-like, IL-1RAcPL, Interleukin-1 receptor 7, IL-1R-7, IL-1R7, Interleukin-18 receptor accessory protein-like, Interleukin-18 receptor beta, IL-18R-beta, IL-18Rbeta, CD218b, IL1R7.

    Product # :

    CYT-1050

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    Description

    IL18RAP produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 576 amino acids (20-356 a.a.) and having a molecular mass of 65.4kDa.IL18RAP is expressed with an 239 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    IL18RAP protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) AND 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Interleukin-18 receptor accessory protein (IL18RAP), belongs to the IL-1 family of cytokines which holds multiple immunoregulatory functions. It has been found that IL18RAP does not mediate IL18-binding, however, IL18RAP is involved in IL18-dependent signal transduction, which leads to NF-kappa-B and JNK activation. IL18R1 as well as IL18RAP polymorphisms have been linked with the following diseases: schizophrenia, HSV1 seropositivity and atopic asthma.

    • Synonyms

      Interleukin-18 receptor accessory protein, IL-18 receptor accessory protein,
      IL-18RAcP, Accessory protein-like, AcPL, CD218 antigen-like family member B, CDw218b, IL-1R accessory protein-like, IL-1RAcPL, Interleukin-1 receptor 7, IL-1R-7, IL-1R7, Interleukin-18 receptor accessory protein-like, Interleukin-18 receptor beta, IL-18R-beta, IL-18Rbeta, CD218b, IL1R7.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      FNISGCSTKK LLWTYSTRSE EEFVLFCDLP EPQKSHFCHR NRLSPKQVPE HLPFMGSNDL SDVQWYQQPS NGDPLEDIRK SYPHIIQDKC TLHFLTPGVN NSGSYICRPK MIKSPYDVAC CVKMILEVKP QTNASCEYSA SHKQDLLLGS TGSISCPSLS CQSDAQSPAV TWYKNGKLLS VERSNRIVVD EVYDYHQGTY VCDYTQSDTV SSWTVRAVVQ VRTIVGDTKL KPDILDPVED TLEVELGKPL TISCKARFGF ERVFNPVIKW YIKDSDLEWE VSVPEAKSIK STLKDEIIER NIILEKVTQR DLRRKFVCFV QNSIGNTTQS VQLKEKRLEP 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.

    Il18Rap Human
  • View Data Sheet

    Name :

    CAMP Human

    Description:

    Cathelicidin Antimicrobial Peptide Human Recombinant

    CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.

    Product # :

    PRO-1405

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    Description

    CAMP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (34-173 a.a.) and having a molecular mass of 18.4kDa.CAMP is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    CAMP protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CAMP belongs to the antimicrobial peptide family, contains highly conserved N-terminal signal peptide, a cathelin domain and a structurally variable cationic antimicrobial peptide that produced by extracellular proteolysis from the C-terminus. CAMP has numerous functions besides the antimicrobial activity such as: cell chemotaxis, immune mediator induction and inflammatory response regulation.

    • Synonyms

      CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSQVLSYKE AVLRAIDGIN QRSSDANLYR LLDLDPRPTM DGDPDTPKPV SFTVKETVCP RTTQQSPEDC DFKKDGLVKR CMGTVTLNQA RGSFDISCDK DNKRFALLGD FFRKSKEKIG KEFKRIVQRI KDFLRNLVPR TES.

    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.

    Camp Human
  • View Data Sheet

    Name :

    LPCAT1 Human

    Description:

    Lysophosphatidylcholine Acyltransferase Human Recombinant

    AYTL2, lpcat, PFAAP3, Lysophosphatidylcholine acyltransferase 1, LPC acyltransferase 1, LPCAT-1, LysoPC acyltransferase 1, 1-acylglycerophosphocholine O-acyltransferase, 1-alkylglycerophosphocholine O-acetyltransferase, Acetyl-CoA:lyso-platelet-activating factor acetyltransferase, Acetyl-CoA:lyso-PAF acetyltransferase, Lyso-PAF acetyltransferase, LysoPAFAT, Acyltransferase-like 2, Phosphonoformate immuno-associated protein 3.

    Product # :

    ENZ-695

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    Description

    LPCAT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 479 amino acids (79-534a.a) and having a molecular mass of 53.4kDa. LPCAT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LPCAT1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lysophosphatidylcholine acyltransferase 1 (LPCAT1) is a part of the 1-acyl-sn-glycerol-3-phosphate acyltransferase family. LPCAT1 is a key enzyme for remodeling phospholipids, including phosphatidylcholine. LPCAT1 possesses both acyltransferase and acetyltransferase activities and also mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC). LPCAT1 presents a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively. LPCAT1 synthesizes phosphatidylcholine in pulmonary surfactant and therefore playing an important role in respiratory physiology.

    • Synonyms

      AYTL2, lpcat, PFAAP3, Lysophosphatidylcholine acyltransferase 1, LPC acyltransferase 1, LPCAT-1, LysoPC acyltransferase 1, 1-acylglycerophosphocholine O-acyltransferase, 1-alkylglycerophosphocholine O-acetyltransferase, Acetyl-CoA:lyso-platelet-activating factor acetyltransferase, Acetyl-CoA:lyso-PAF acetyltransferase, Lyso-PAF acetyltransferase, LysoPAFAT, Acyltransferase-like 2, Phosphonoformate immuno-associated protein 3.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSSAEKEPE QPPALWRKVV DFLLKAIMRT MWFAGGFHRV AVKGRQALPT EAAILTLAPH SSYFDAIPVT MTMSSIVMKA ESRDIPIWGT LIQYIRPVFV SRSDQDSRRK TVEEIKRRAQ SNGKWPQIMI FPEGTCTNRT CLITFKPGAF IPGAPVQPVV LRYPNKLDTI TWTWQGPGAL EILWLTLCQF HNQVEIEFLP VYSPSEEEKR NPALYASNVR RVMAEALGVS VTDYTFEDCQ LALAEGQLRL PADTCLLEFA RLVRGLGLKP EKLEKDLDRY SERARMKGGE KIGIAEFAAS LEVPVSDLLE DMFSLFDESG SGEVDLRECV VALSVVCRPA RTLDTIQLAF KMYGAQEDGS VGEGDLSCIL KTALGVAELT VTDLFRAIDQ EEKGKITFAD FHRFAEMYPA FAEEYLYPDQ THFESCAETS PAPIPNGFCA DFSPENSDAG RKPVRKKLD.

    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.

    Lpcat1 Human
  • View Data Sheet

    Name :

    RARRES2 Human, Sf9

    Description:

    Retinoic Acid Receptor Responder 2 Human Recombinant, Sf9

    Retinoic Acid Receptor Responder 2, Chemerin, Retinoic Acid Receptor Responder (Tazarotene Induced) 2, Tazarotene-Induced Gene 2 Protein, RAR-Responsive Protein TIG2, TIG2, Retinoic Acid Receptor Responder Protein 2, HP10433, Retinoic acid receptor responder protein 2, Chemerin, RAR-responsive protein TIG2, Tazarotene-induced gene 2 protein.

    Product # :

    PRO-2382

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    Description

    RARRES2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 146 amino acids (21-157a.a.) and having a molecular mass of 16.9kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). RARRES2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    RARRES2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RARRES2 is a secreted chemotactic protein that initiates chemotaxis through the ChemR23 G protein-coupled seven-transmembrane domain ligand. RARRES2 is upregulated by the synthetic retinoid tazarotene and found in a vast variety of tissues. RARRES2 acts as an adipokine, and is truncated on both termini from the proprotein. RARRES2 is structurally related to the cathelicidin precursors, cystatin C and kininogens. RARRES2 promotes calcium mobilization and chemotaxis of immature dendritic cells and macrophages. RARRES2 is secreted as a precursor of little biological activity, which requires proteolytic cleavage of its COOH-terminal domain to be exchangeed into a potent and highly specific agonist of ChemR23. RARRES2 signals via its receptor, ChemR23 (CMKLR1), as a positive regulator of adipocyte differentiation and metabolic function. The Chemerin receptor acts as a coreceptor for SIV and some primary HIV-1 strains. The Chemerin receptor has another ligand, called tazarotene-induced gene.

    • Synonyms

      Retinoic Acid Receptor Responder 2, Chemerin, Retinoic Acid Receptor Responder (Tazarotene Induced) 2, Tazarotene-Induced Gene 2 Protein, RAR-Responsive Protein TIG2, TIG2, Retinoic Acid Receptor Responder Protein 2, HP10433, Retinoic acid receptor responder protein 2, Chemerin, RAR-responsive protein TIG2, Tazarotene-induced gene 2 protein.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPELTEAQR RGLQVALEEF HKHPPVQWAF QETSVESAVD TPFPAGIFVR LEFKLQQTSC RKRDWKKPEC KVRPNGRKRK CLACIKLGSE DKVLGRLVHC PIETQVLREA EEHQETQCLR VQRAGEDPHS FYFPGQFAFS 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.

    Rarres2 Human Sf9
  • View Data Sheet

    Name :

    ZWINT Human

    Description:

    ZW10 Interacting Kinetochore Protein Human Recombinant

    ZW10 Interacting Kinetochore Protein, ZWINT, ZW10 Interactor, HZwint-1, KNTC2AP, ZWINT1, Human ZW10 Interacting Protein-1, ZW10 Interactor Kinetochore Protein zwint-1, Zwint-1, ZW10-Interacting Protein 1.

    Product # :

    PRO-1944

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    Description

    ZWINT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 253 amino acids (1-230) and having a molecular mass of 27.9 kDa (Molecular size on SDS-PAGE will appear higher).ZWINT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ZWINT solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ZW10 Interacting Kinetochore Protein (ZWINT) is involved in kinetochore function. ZWINT is part of the MIS12 complex, which is essential for kinetochore formation and spindle checkpoint activity. ZWINT is localized to the cytoplasm during interphase and to kinetochores from late prophase to anaphase. ZWINT interacts with ZW10 (Zeste White 10) and regulates the association between ZW10 and kinetochores. ZWINT gene defects are linked with the pathogenesis of Roberts’s syndrome, an autosomal recessive disorder characterized by growth retardation due to premature chromosome separation.

    • Synonyms

      ZW10 Interacting Kinetochore Protein, ZWINT, ZW10 Interactor, HZwint-1, KNTC2AP, ZWINT1, Human ZW10 Interacting Protein-1, ZW10 Interactor Kinetochore Protein zwint-1, Zwint-1, ZW10-Interacting Protein 1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMEAAETE AEAAALEVLA EVAGILEPVG LQEEAELPAK ILVEFVVDSQ KKDKLLCSQL QVADFLQNIL AQEDTAKGLD PLASEDTSRQ KAIAAKEQWK ELKATYREHV EAIKIGLTKA LTQMEEAQRK RTQLREAFEQ LQAKKQMAME KRRAVQNQWQ LQQEKHLQHL AEVSAEGKLL FPEAEAEAEN LPDDKPQQPT RPQEQSTGDT MGRDPGVSFK AVGLQPAGDV NLP.

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    Zwint Human
  • View Data Sheet

    Name :

    IL-10 Human, Sf9

    Description:

    Interleukin 10 Human Recombinant, Sf9, Active

    Interleukin-10, IL-10, Cytokine synthesis inhibitory factor, CSIF, IL10, GVHDS, IL10A, TGIF, T-Cell Growth Inhibitory Factor.

    Product # :

    CYT-1147

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    Description

    IL-10 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 166 amino acids (19-178 aa) and having a molecular mass of 19.4kDa. IL-10 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The IL-10 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using MC/9 mouse mast cells. The ED50 range < 5 ng/ml.

    More Info

    • Introduction

      Interleukin 10 or IL-10 or human cytokine synthesis inhibitory factor, is a cytokine (anti-inflammatory). IL10 gene is coding for il-10 In humans. Interleukin 10 has a receptor complex that is built from a couple of IL-10 receptor-1 and a couple of IL-10 receptor-2 proteins. therfore, the whole receptor unit consists of four IL-10 receptor molecules. IL-10 binds the receptor and causes STAT3 signalling through the phosphorylation of the cytoplasmic ends of IL-10 receptor 1 and IL-10 receptor 2 through JAK1 and Tyk2.

    • Synonyms

      Interleukin-10, IL-10, Cytokine synthesis inhibitory factor, CSIF, IL10, GVHDS, IL10A, TGIF, T-Cell Growth Inhibitory Factor.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      SPGQGTQSEN SCTHFPGNLP NMLRDLRDAF SRVKTFFQMK DQLDNLLLKE SLLEDFKGYL GCQALSEMIQ FYLEEVMPQA ENQDPDIKAH VNSLGENLKT LRLRLRRCHR FLPCENKSKA VEQVKNAFNK LQEKGIYKAM SEFDIFINYI EAYMTMKIRN HHHHHH.

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    Il10 Protein
  • View Data Sheet

    Name :

    IFNW1 Human

    Description:

    IFN-Omega 1 Human Recombinant

    IFN omega-1, IFN alpha-II-1, IFNW1.

    Product # :

    CYT-040

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    Description

    IFN-Omega 1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 19.9kDa.The IFN-Omega 1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 was determined by a cytotoxicity assay using Human TF-1 cells is < 0.01 ng/ml, corresponding to a specific activity of > 100,000,000 units/mg.

    More Info

    • Introduction

      IFN-Omega 1 is a type I IFN, that can be induced by virus-infected leukocytes. Type I IFN family members, which include IFN-alpha, IFN-beta, and IFN-omega, signal through IFNAR-1/IFNAR-2 receptor complex, and wield antiviral and antiproliferative activities. IFNW1 exhibits about 75% sequence homology with IFN-a, and contains 2 conserved disulfide bonds, which are essential for full biological activity.

    • Synonyms

      IFN omega-1, IFN alpha-II-1, IFNW1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IFNW1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFNW1 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 IFNW1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MCDLPQNHGL LSRNTLVLLH QMRRISPFLC LKDRRDFRFP QEMVKGSQLQ KAHVMSVLHE MLQQIFSLFH TERSSAAWNM TLLDQLHTGL HQQLQHLETC LLQVVGEGES AGAISSPALT LRRYFQGIRV YLKEKKYSDC AWEVVRMEIM KSLFLSTNMQ ERLRSKDRDL GSS.

    • Background

      What is the molecular weight/Mw of IFNW1 HUMAN Protein?
      IFNW1 HUMAN Protein has a total Mw of 19.9kDa.

      What is the source or expression system of IFNW1 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IFNW1 HUMAN Protein?
      IFNW1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNW1 HUMAN Protein?
      The ED50 was determined by a cytotoxicity assay using Human TF-1 cells is < 0.01 ng/ml, corresponding to a specific activity of > 100,000,000 units/mg.

      What is the amino acid sequence of IFNW1 HUMAN Protein?
      MCDLPQNHGL LSRNTLVLLH QMRRISPFLC LKDRRDFRFP QEMVKGSQLQ KAHVMSVLHE MLQQIFSLFH TERSSAAWNM TLLDQLHTGL HQQLQHLETC LLQVVGEGES AGAISSPALT LRRYFQGIRV YLKEKKYSDC AWEVVRMEIM KSLFLSTNMQ ERLRSKDRDL GSS.

      What applications can IFNW1 HUMAN Protein be used in?
      IFNW1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFNW1 HUMAN Protein?
      The endotoxin level is minimal, IFNW1 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.

    Ifnw1 Human
  • View Data Sheet

    Name :

    TGFA Human

    Description:

    Transforming Growth Factor-Alpha Human Recombinant

    Transforming Growth Factor Alpha, Protransforming Growth Factor Alpha, TGF-Alpha, TGFA.

    Product # :

    CYT-871

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    Description

    TGFA Human Recombinant (40-89) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 50 amino acids and having a molecular mass of 5.6kDa. The TGFA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in 0.1% TFA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured in a proliferation assay using mouse BALB/c 3T3 cells, is 0.395ng/ml.

    More Info

    • Introduction

      Transforming Growth Factor-Alpha (TGF-alpha) belongs to the EGF family of cytokines. TGFA soluble form is discharged from the membrane by proteolytic cleavage. Membrane-bound proTGF-alpha is biologically active and has a role in cell-cell adhesion or in the stimulation of adjacent cells. TGFA expression is common in transformed cells. Additionally, TGFA is expressed in normal tissues during embryogenesis and in adult cells/tissues, including the pituitary, keratinocytes, and macrophages.

    • Synonyms

      Transforming Growth Factor Alpha, Protransforming Growth Factor Alpha, TGF-Alpha, TGFA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TGFA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFA 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 TGFA in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VVSHFNDCPD SHTQFCFHGT CRFLVQEDKP ACVCHSGYVG ARCEHADLLA.

    • Background

      Title: Transforming Growth Factor-Alpha Human Recombinant, Yeast: A Versatile Biopharmaceutical for Therapeutic Applications

      Abstract:


      Transforming Growth Factor-Alpha (TGF-α) is a potent growth factor involved in numerous physiological processes, including cell proliferation, differentiation, and tissue repair. The development of TGF-α human recombinant using yeast expression systems has provided a valuable biopharmaceutical tool for therapeutic applications. This research paper explores the production process, characteristics, and potential therapeutic applications of TGF-α human recombinant derived from yeast, highlighting its versatility and clinical significance.

      Introduction:


      TGF-α is a crucial growth factor that regulates cellular functions and plays a vital role in tissue development and repair. Harnessing the therapeutic potential of TGF-α has been limited by challenges in its production and stability. However, the development of TGF-α human recombinant using yeast expression systems has overcome these limitations, making it an attractive biopharmaceutical for therapeutic interventions.

      Production Process and Characteristics:


      TGF-α human recombinant derived from yeast is produced through recombinant DNA technology, utilizing yeast cells as expression hosts. Yeast expression systems offer several advantages, including high expression yields, cost-effectiveness, and the ability to produce correctly folded and biologically active TGF-α. The resulting TGF-α human recombinant closely resembles native TGF-α in terms of structure and function, allowing for effective therapeutic intervention.

      Therapeutic Applications:


      TGF-α human recombinant derived from yeast has shown promise in various therapeutic applications. It has been investigated for its wound-healing properties, where it promotes tissue regeneration and accelerates the healing process. Additionally, TGF-α has been explored in tissue engineering and regenerative medicine, playing a crucial role in stimulating cell proliferation and tissue development. Furthermore, TGF-α has been studied in the context of cancer research, as it is involved in tumor growth and angiogenesis, making it a potential target for anticancer therapies.

      Advantages and Challenges:


      The use of yeast expression systems for producing TGF-α human recombinant offers several advantages, including scalability, cost-effectiveness, and the ability to produce bioactive protein. However, challenges remain, such as optimizing production processes, purification methods, and ensuring product consistency and stability. Further research is needed to address these challenges and maximize the clinical potential of TGF-α human recombinant derived from yeast.

      Conclusion:


      TGF-α human recombinant derived from yeast represents a versatile biopharmaceutical tool with significant therapeutic potential. Its production using yeast expression systems offers advantages in terms of scalability, cost-effectiveness, and bioactivity. The therapeutic applications of TGF-α human recombinant extend to wound healing, tissue engineering, and cancer research. Continued research and development efforts are crucial to optimizing production processes, overcoming challenges, and fully exploiting the clinical benefits of TGF-α human recombinant as a therapeutic agent.

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    Tgfa Human
  • View Data Sheet

    Name :

    TXN Mouse

    Description:

    Thioredoxin Mouse Recombinant

    TRX1, TRX2, Thioredoxin-1, Thioredoxin I, TR-I, Thioredoxin-2, Thioredoxin-1, ADF, Surface associated sulphydryl protein, TXN protein, ATL derived factor, DKFZp686B1993, MGC61975, SASP, Thioredoxin, TRDX, TRX, TRX 1, TXN.

    Product # :

    PRO-2607

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    Description

    TXN Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (1-105 a.a.) and having a molecular mass of 14.1kDa. TXN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TXN protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >60 A650/cm/min/mg, obtained by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.

    More Info

    • Introduction

      Thioredoxin or TRX contains a single disulfide active site and serves as a general protein disulphide oxidoreductase.Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that are found in all the kingdoms of living organisms. The proteinis involved in the first unique step in DNA synthesis; It interacts with a wide range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, along with the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant.

    • Synonyms

      TRX1, TRX2, Thioredoxin-1, Thioredoxin I, TR-I, Thioredoxin-2, Thioredoxin-1, ADF, Surface associated sulphydryl protein, TXN protein, ATL derived factor, DKFZp686B1993, MGC61975, SASP, Thioredoxin, TRDX, TRX, TRX 1, TXN.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMVKLIES KEAFQEALAA AGDKLVVVDF SATWCGPCKM IKPFFHSLCD KYSNVVFLEV DVDDCQDVAA DCEVKCMPTF QFYKKGQKVG EFSGANKEKL EASITEYA.

    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.

    Thioredoxin Mouse
  • View Data Sheet

    Name :

    RLN2 Human, Sf9

    Description:

    Relaxin-2 Human Recombinant, Sf9

    Relaxin 2, Relaxin, Ovarian, Of Pregnancy, Prorelaxin H2, Relaxin H2, H2-Preprorelaxin, Relaxin 2 (H2), BA12D24.1.1, BA12D24.1.2, H2-RLX, RLXH2, H2.

    Product # :

    PRO-2406

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    Description

    RLN2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 170 amino acids (25-185a.a.) and having a molecular mass of 19.3kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).RLN2 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    RLN2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Prorelaxin H2 (RLN2) is a member of the insulin gene superfamily. This family which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. It may also have other roles in boosting sperm motility, regulating blood pressure, controlling heart rate and releasing oxytocin and vasopressin. RLN2 is a peptide hormone linked to several therapeutically relevant physiological effects, including regulation of collagen metabolism and multiple vascular control pathways. The active form of the RLN2 protein consists of an A chain and a B chain linked by disulfide bonds.

    • Synonyms

      Relaxin 2, Relaxin, Ovarian, Of Pregnancy, Prorelaxin H2, Relaxin H2, H2-Preprorelaxin, Relaxin 2 (H2), BA12D24.1.1, BA12D24.1.2, H2-RLX, RLXH2, H2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPDSWMEEV IKLCGRELVR AQIAICGMST WSKRSLSQED APQTPRPVAE IVPSFINKDT ETINMMSEFV ANLPQELKLT LSEMQPALPQ LQQHVPVLKD SSLLFEEFKK LIRNRQSEAA DSSPSELKYL GLDTHSRKKR QLYSALANKC CHVGCTKRSL ARFCHHHHHH.

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    Rln2 Human Sf9
  • View Data Sheet

    Name :

    TNFRSF17 Human, Sf9

    Description:

    B-Cell Maturation Antigen, Sf9 Human Recombinant

    BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen

    Product # :

    CYT-1148

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    Description

    TNFRSF17 Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 296 amino acids (1-54 aa) and having a molecular mass of 33.1Da.TNFRSF17 is fused to a 242 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF17 protein (0.5mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      B-Cell Maturation Antigen or TNFRSF17 or tumor necrosis factor receptor superfamily member 17, is part of the TNF receptor protein family. This protein is a TNFSF13B/BLyS/BAFF, TNFSF13/APRIL & promotes B-cell survival receptor. TNFRSF17 has a crucial part in the humoral immunity regulation. This protein is responsible for the activation of NF-kappa-B & JNK.

    • Synonyms

      BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPMLQMAGQ CSQNEYFDSL LHACIPCQLR CSSNTPPLTC QRYCNASVTN SVKGTNALEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH

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    Bcma Protein
  • View Data Sheet

    Name :

    Pentagastrin

    Description:

    Pentagastrin

    Product # :

    HOR-045

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    Description

    Pentagastrin Synthetic is a single, non-glycosylated polypeptide chain containing 5 amino acids, having a molecular mass of 768 Dalton and a Molecular formula of C37H49N7O9S .

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Pentagastrin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pentagastrin 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 Pentagastrin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      Boc-β-Ala-Trp-Met-Asp-Phe-NH2.

    • Background

      Pentagastrin is a synthetic peptide that has long been recognized for its significant influence on gastric physiology. Its ability to stimulate gastric acid secretion and regulate various aspects of gastrointestinal function has made it a valuable tool in both basic research and clinical practice.

      This research aims to comprehensively investigate the multifaceted effects of pentagastrin on the gastrointestinal system, shedding light on its mechanisms of action and potential clinical applications.
      The primary objective of this study is to elucidate the mechanisms underlying pentagastrin-induced gastric acid secretion.

      In vitro experiments using isolated gastric cells or tissue preparations will be conducted to explore the signaling pathways activated by pentagastrin. This will include investigations into the role of intracellular messengers, such as cyclic AMP (cAMP), calcium ions (Ca2+), and protein kinases, in mediating the secretory response.

      The second objective is to assess the impact of pentagastrin on gastrointestinal motility. In vivo studies using animal models or human volunteers will be employed to investigate its effects on gastric emptying, intestinal transit, and colonic motility. These experiments may provide insights into the potential use of pentagastrin in the management of gastrointestinal motility disorders.

      The third objective is to explore the clinical applications of pentagastrin. Clinical trials and studies involving human subjects will be conducted to evaluate its potential therapeutic uses, such as in the diagnosis and treatment of gastric acid-related disorders, including peptic ulcers and gastroesophageal reflux disease (GERD). Additionally, the safety and efficacy of pentagastrin as an adjunct to medical imaging techniques, such as gastric scintigraphy, will be examined.

      By investigating the diverse effects of pentagastrin on the gastrointestinal system, this research aims to enhance our understanding of gastric physiology and its clinical relevance. The findings may lead to improved diagnostic and therapeutic strategies for gastrointestinal disorders, ultimately benefiting patients affected by these conditions.

    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.

    Pentagastrin
  • View Data Sheet

    Name :

    tPA Human

    Description:

    Tissue Plasminogen Activator Human Recombinant

    Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148.

    Product # :

    ENZ-263

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    Description

    Tissue Plasminogen Activator Human Recombinant produced in CHO cells is a single, glycosylated polypeptide chain containing 527 amino acids and having a molecular mass of 59008.71 Dalton. tPA is a serine protease enzyme that converts plasminogen to plasmin. The tPA is purified by proprietary chromatographic techniques.

    Source

    Chinese Hamster Ovary Cells (CHO)

    Formulation

    Each mg of t-PA contains 1.7 gr L-arginine, 0.5 gr phosphoric acid and 4 mg tween 80.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
      This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism.

    • Synonyms

      Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized t-PA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution tPA 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 t-PA in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Enzymatic Activity

      580,000 IU/mg.

    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.

    T Pa Human
  • View Data Sheet

    Name :

    THYN1 Human

    Description:

    Thymocyte Nuclear Protein 1 Human Recombinant

    MY105, THY28, Thymocyte Protein Thy28, Cyte Nuclear Protein 1.

    Product # :

    PRO-270

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    Description

    THYN1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 245 amino acids (1-225a.a.) and having a molecular mass of 27.8kDa.THYN1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The THYN1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 100mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      THYN1, is greatly conserved among vertebrates and plant types. TYHN1 takes part in the induction of apoptosis. THYN1 in the thymocytes was primarily found in the nucleus, as shown in lymphoma cells, demonstrating that the THYN1 is localized in the nucleus, regardless of the cyclic or resting stage of the cell cycle.

    • Synonyms

      MY105, THY28, Thymocyte Protein Thy28, Cyte Nuclear Protein 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSRPRKRLAG TSGSDKGLSG KRTKTENSGE ALAKVEDSNP QKTSATKNCL KNLSSHWLMK SEPESRLEKG VDVKFSIEDL KAQPKQTTCW DGVRNYQARN FLRAMKLGEE AFFYHSNCKE PGIAGLMKIV KEAYPDHTQF EKNNPHYDPS SKEDNPKWSM VDVQFVRMMK RFIPLAELKS YHQAHKATGG PLKNMVLFTR QRLSIQPLTQ EEFDFVLSLE EKEPS

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    Thyn1 Human
  • View Data Sheet

    Name :

    RARRES2 Human, His

    Description:

    Retinoic Acid Receptor Responder 2 Human Recombinant, His Tag

    Chemerin, TIG2, Tazarotene-induced gene 2 protein, Retinoic acid receptor responder protein 2, RAR-responsive protein TIG2, RARRES2, HP10433.

    Product # :

    PRO-1458

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    Description

    RARRES2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids (21-157a.a) and having a total molecular mass of 18 kDa. RARRES2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RARRES2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RARRES2 is a secreted chemotactic protein that initiates chemotaxis through the ChemR23 G protein-coupled seven-transmembrane domain ligand. RARRES2 is upregulated by the synthetic retinoid tazarotene and found in a vast variety of tissues. RARRES2 acts as an adipokine, and is truncated on both termini from the proprotein. RARRES2 is structurally related to the cathelicidin precursors, cystatin C and kininogens. RARRES2 promotes calcium mobilization and chemotaxis of immature dendritic cells and macrophages. RARRES2 is secreted as a precursor of little biological activity, which requires proteolytic cleavage of its COOH-terminal domain to be exchangeed into a potent and highly specific agonist of ChemR23. RARRES2 signals via its receptor, ChemR23 (CMKLR1), as a positive regulator of adipocyte differentiation and metabolic function. The Chemerin receptor acts as a coreceptor for SIV and some primary HIV-1 strains. The Chemerin receptor has another ligand, called tazarotene-induced gene.

    • Synonyms

      Chemerin, TIG2, Tazarotene-induced gene 2 protein, Retinoic acid receptor responder protein 2, RAR-responsive protein TIG2, RARRES2, HP10433.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MELTEAQRRG LQVALEEFHK HPPVQWAFQE TSVESAVDTP FPAGIFVRLE FKLQQTSCRK RDWKKPECKV RPNGRKRKCL ACIKLGSEDK VLGRLVHCPI ETQVLREAEE HQETQCLRVQ RAGEDPHSFY FPGQFAFS.

    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.

    Rarres2 Human His
  • View Data Sheet

    Name :

    GAL Human

    Description:

    Galanin Prepropeptide Human Recombinant

    GALN, GLNN, GMAP, GAL, GAL1.

    Product # :

    PRO-1433

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    Description

    GAL Human Recombinant produced in E. coli is a single polypeptide chain containing 127 amino acids (20-123) and having a molecular mass of 13.9kDa. GAL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GAL solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Galanin Prepropeptide (GAL) which is localized in brain pathways is involved in both cognition and affect, and also inhibits learning and memory by inhibiting neurotransmitter release and neuronal firing rate. GAL is a part of the galanin family and modulates a variety of physiological processed including cognition/memory, sensory/pain processing, neurotransmitter/hormone secretion, and feeding behavior. Galanin Prepropeptide is upregulated in primary afferent and sympathetic neurones and is required for the development of sympathetic perineuronal baskets subsequent to nerve injury.

    • Synonyms

      GALN, GLNN, GMAP, GAL, GAL1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSASAGLWS PAKEKRGWTL NSAGYLLGPH AVGNHRSFSD KNGLTSKREL RPEDDMKPGS FDRSIPENNI MRTIIEFLSF LHLKEAGALD RLLDLPAAASSEDIERS.

    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.

    Gal Human
  • View Data Sheet

    Name :

    IL 32A Human

    Description:

    Interleukin-32 alpha Human Recombinant

    NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.

    Product # :

    CYT-584

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

    Interleukin-32 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 131 amino acids and having a molecular mass of 14.9 kDa.

    Source

    Escherichia Coli.

    Formulation

    IL-32 was lyophilized from a concentrated (1mg/ml) solution in water containing 50mM sodium Phosphate buffer pH=7.5.

    Purity

    Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Human IL-32 alpha activity is measured via the dose-dependent induction of TNF-alpha in the human THP-1 monocytic cell line.

    More Info

    • Introduction

      IL-32 is part of the cytokine family and contains a tyrosine sulfation site, 3 potential N-myristoylation sites, multiple putative phosphorylation sites, and an RGD cell-attachment sequence. IL-32 expression is elevated after the activation of T-cells by mitogens or the activation of NK cells by IL-2. IL-32 induces the production of TNF-a from macrophage cells. IL-32 pro-inflammatory pathway is activated in response to influenza A virus infection. Dysregulation of IL-32 in myelodysplastic syndrome and chronic myelomonocytic leukemia modulates apoptosis and impairs NK function.
      Induction of TNF, IL-1beta, and IL-6 by IL-32 is intervened by p38-MAPK. IL-32 induced monocyte-to-macrophage differentiation is mediated through nonapoptotic, caspase-3-dependent mechanisms. IL32 plays an important role in the pathogenesis of rheumatoid arthritis. IL-32 is involved in activation-induced cell death in T cells, through its intracellular actions. IL-32 is a cell-associated proinflammatory cytokine, which is particularly stimulated by mycobacteria through a caspase-1- and IL-18-dependent production of IFNgamma.
      IL-32 is associated with TNF-a, IL-1beta, and IL-18. IL32 is involved in human rheumatoid arthritis and is a novel target in autoimmune diseases.

    • Synonyms

      NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL32 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL32 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized IL-32 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MCFPKVLSDD MKKLKARMHQ AIERFYDKMQ NAESGRGQVM SSLAELEDDF KEGYLETVAA YYEEQHPELT PLLEKERDGL RCRGNRSPVP DVEDPATEEP GESFCDKSYG APRGDKEELT PQKCSEPQSS 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.

    Il 32 Human
  • View Data Sheet

    Name :

    TACI Human

    Description:

    Tumor Necrosis Factor Receptor 13B Human Recombinant

    CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B. 

    Product # :

    CYT-819

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

    TACI Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids and having a molecular mass of 18.0kDa.

    Source

    Escherichia Coli.

    Formulation

    TACI protein was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by: (a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.

    Biological Activity

    Fully biologically active when compared to standard. The biological activity is determined by its ability to block human BAFF induced T2B cell survival using a concentration range of 1.0-3.0 µg/ml corresponding to a specific activity of 334-1000 IU/mg.

    More Info

    • Introduction

      TNFRSF13B (TACI) is a transmembrane receptor protein found predominantly on the surface of B cells (a significant part of the immune system). TACI was at first discovered owing to its ability to interact with calcium-modulator and cyclophilin ligand (CAML). Later on, it was found that TACI plays a key role in humoral immunity by interacting with two members of the TNF family. Also, TACI controls T cell-independent B cell antibody responses, isotype switching, and B cell homeostasis.

    • Synonyms

      CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TACI although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TACI 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 TACI in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSGLGRSRRG GRSRVDQEER FPQGLWTGVA MRSCPEEQYW DPLLGTCMSC KTICNHQSQR TCAAFCRSLS CRKEQGKFYD HLLRDCISCA SICGQHPKQC AYFCENKLRS PVNLPPELRR QRSGEVENNS DNSGRYQGLE HRGSEASPAL PGLKLSADQV

    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.

    Human Taci
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