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1000 results found for “activating transcription factor”

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  • View Data Sheet

    Description:

    Phenylalanyl-tRNA Synthetase 2 Human Recombinant

    Phenylalanyl-tRNA synthetase mitochondrial, Phenylalanine--tRNA ligase, PheRS, FARS2, FARS1, HSPC320, dJ520B18.2.

    Product # :

    ENZ-111

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    Description

    FARS2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 436 amino acids (37-451 a.a.) and having a molecular mass of 50.6kDa.FARS2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FARS2 solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol, 1mM EDTA and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phenylalanyl-tRNA synthetase 2 mitochondrial (FARS2) is a member of the class II aminoacyl- tRNA synthetase family. FARS2 is a mitochondrial matrix protein. FARS2 when acting as a monomer, catalyzes the ATP-dependent conversion of L-phenylalanine and tRNA (Phe) to L-phenlalanyltRNA (Phe), an event which is vital for proper translation and protein expression.

    • Synonyms

      Phenylalanyl-tRNA synthetase mitochondrial, Phenylalanine--tRNA ligase, PheRS, FARS2, FARS1, HSPC320, dJ520B18.2.

    • 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 MPAAECATQR APGSVVELLG KSYPQDDHSN LTRKVLTRVG RNLHNQQHHP LWLIKERVKE HFYKQYVGRF GTPLFSVYDN LSPVVTTWQN FDSLLIPADH PSRKKGDNYY LNRTHMLRAH TSAHQWDLLH AGLDAFLVVG DVYRRDQIDS QHYPIFHQLE AVRLFSKHEL FAGIKDGESL QLFEQSSRSA HKQETHTMEA VKLVEFDLKQ TLTRLMAHLF GDELEIRWVD CYFPFTHPSF EMEINFHGEW LEVLGCGVME QQLVNSAGAQ DRIGWAFGLG LERLAMILYD IPDIRLFWCE DERFLKQFCV SNINQKVKFQ PLSKYPAVIN DISFWLPSEN YAENDFYDLV RTIGGDLVEK VDLIDKFVHP KTHKTSHCYR ITYRHMERTL SQREVRHIHQ ALQEAAVQLL GVEGRF.

    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.

    Fars2 Human
  • View Data Sheet

    Name :

    GDNF Rat

    Description:

    Glial-Derived Neurotrophic Factor Rat Recombinant

    ATF1, ATF2, HFB1-GDNF, GDNF.

    Product # :

    CYT-403

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    Description

    Glial derived Neurotrophic Factor Rat Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 134 amino acids and having a total molecular mass of 29.8 kDa.

    Source

    Escherichia Coli.

    Formulation

    GDNF was lyophilized from a sterile solution containing 1xPBS, pH 7.4.

    Purity

    Greater than 98.0% as determined by HPLC analysis and by SDS-PAGE.

    Biological Activity

    Recombinant rat GDNF has full biological activity when compared to standards. The ED50, determined by a cell proliferation assay using rat C6 cells, is less than 0.2ng/ml corresponding to a specific activity of more than 5,000,000IU/mg.

    More Info

    • Introduction

      GDNF promotes the survival and differentiation of neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
      GDNF enhances survival and morphological differentiation of neurons and increases their high-affinity uptake.

    • Synonyms

      ATF1, ATF2, HFB1-GDNF, GDNF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SPDKQAALP RRENRNRQAAA ASPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCESAETMYD KILKNLSRSR RLTSDKVGQA CCRPVAFDDD LSFLDDNLVY HILRKHSAKR CGCI

    • Background

      What is the molecular weight/Mw of GDNF RAT Protein?
      GDNF RAT Protein has a total Mw of 29.8kDa.

      What is the source or expression system of GDNF RAT Protein?
      Escherichia Coli.

      What is the Purity of GDNF RAT Protein?
      GDNF RAT Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDNF RAT Protein?
      Recombinant rat GDNF has full biological activity when compared to standards. The ED50, determined by a cell proliferation assay using rat C6 cells, is less than 0.2ng/ml corresponding to a specific activity of more than 5,000,000IU/mg.

      What is the amino acid sequence of GDNF RAT Protein?
      SPDKQAALP RRENRNRQAAA ASPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCESAETMYD KILKNLSRSR RLTSDKVGQA CCRPVAFDDD LSFLDDNLVY HILRKHSAKR CGCI

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

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

    Gdnf Rat
  • View Data Sheet

    Description:

    Transforming Growth Factor Beta Receptor II, His Tag Human Recombinant

    AAT3, FAA3, MFS2, RIIC, LDS1B, LDS2B, TAAD2, TGFR-2, TGFbeta-RII, TGFBR-2, TGF-beta receptor type-2, Transforming growth factor-beta receptor type II, TGF-beta receptor type II, TGF-beta type II receptor, TbetaR-II, TGFBR2.

    Product # :

    PKA-088

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    Description

    TGFBR2 Human Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 383 amino acids (23-166a.a) and having a molecular mass of 43.3kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). TGFBR2 is expressed with a 239aa hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The TGFBR2 solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      TGFBR2 is part of the Ser/Thr protein kinase family and the TGFB receptor subfamily. TGFBR2 is a transmembrane protein that has a protein kinase domain, forms a heterodimeric complex with another receptor protein, and binds TGF-beta. This receptor/ligand complex phosphorylates proteins, which then enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation. Mutations in TGFBR2 gene have been associated with Marfan syndrome, Loeys-Deitz Aortic Aneurysm Syndrome, and the development of various types of tumors. TGFBR2 expression is increased in oral squamous cell carcinoma cells. TGFBR2 attenuates the biological activities of TGF-beta in colorectal cancer. TGFBR2 expression is decreased by IL-1beta while inducing Sp3 via NFkappaB. TGFB2 and TGFBR2 are involved in the antiestrogenic activity of tamoxifen metabolites in breast cancer.

    • Synonyms

      AAT3, FAA3, MFS2, RIIC, LDS1B, LDS2B, TAAD2, TGFR-2, TGFbeta-RII, TGFBR-2, TGF-beta receptor type-2, Transforming growth factor-beta receptor type II, TGF-beta receptor type II, TGF-beta type II receptor, TbetaR-II, TGFBR2.

    • 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

      TIPPHVQKSV NNDMIVTDNN GAVKFPQLCK FCDVRFSTCD NQKSCMSNCS ITSICEKPQE VCVAVWRKND ENITLETVCH DPKLPYHDFI LEDAASPKCI MKEKKKPGET FFMCSCSSDE CNDNIIFSEE YNTSNPDLLL VIFQLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH.

    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.

    Tgfbr2 Human His
  • View Data Sheet

    Description:

    Complement C1q Tumor Necrosis Factor-Related Protein 5 Human Recombinant

    CTRP5, MFRP.

    Product # :

    PRO-2599

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    Description

    C1QTNF5 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 253 amino acids (16-243.a.a) and having a molecular mass of 26.4kDa. C1QTNF5 Human is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The C1QTNF5 protein solution (0.25 mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.5) containing 30% glycerol and 0.2M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement C1q Tumor Necrosis Factor-Related Protein 5 (C1QTNF5) encodes a short-chain collagen which is expressed mainly in sub-retinal pigment epithelium, ciliary epithelium and adipose tissue. C1QTNF5 is increased in mtDNA-depleted myocytes and stimulates the phosphorylation of AMP activated protein kinase. C1QTNF5 takespart in the adhesion of the retinal pigment epithelium (RPE) to the Bruch Membrane. Mutations in C1QTNF5 have been associated with late-onset retinal degeneration.

    • Synonyms

      CTRP5, MFRP.

    • 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 MGSHMSPPLD DNKIPSLCPG HPGLPGTPGH HGSQGLPGRD
      GRDGRDGAPG APGEKGEGGR PGLPGPRGDP GPRGEAGPAG PTGPAGECSV PPRSAFSAKR
      SESRVPPPSD APLPFDRVLV NEQGHYDAVT GKFTCQVPGV YYFAVHATVY RASLQFDLVK
      NGESIASFFQ FFGGWPKPAS LSGGAMVRLE PEDQVWVQVG VGDYIGIYAS IKTDSTFSGF LVYSDWHSSP VFA.

    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.

    C1Qtnf5 Human
  • View Data Sheet

    Description:

    Hypoxanthine-Guanine Phosphoribosyltransferase, Human Recombinant, Active

    Hypoxanthine Phosphoribosyltransferase 1, EC 2.4.2.8, HGPRTase, HGPRT, HPRT , Hypoxanthine-Guanine Phosphoribosyltransferase 1, Hypoxanthine-Guanine Phosphoribosyltransferase, Testicular Tissue Protein Li 89, Lesch-Nyhan Syndrome, HPRT1.

    Product # :

    ENZ-1006

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    Description

    HPRT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 238 amino acids (1-218 a.a) and having a molecular mass of 26.7kDa. HPRT1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HPRT1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 15 units/mg and is defined as the amount of enzyme that catalyze the formation of 1 umole of guanosine 5’-monophosphate (GMP) per minute from guanine and phosphoribosyl pyrophosphate at pH 7.5 at 37C.

    More Info

    • Introduction

      HPRT1 has a main part in the generation of purine nucleotides through the purine salvage pathway. HPRT1 primarily functions to salvage purines from degraded DNA to renewed purine synthesis. Therefore, it performs as a catalyst in the reaction between guanine and phosphoribosyl pyrophosphate to form GMP.

    • Synonyms

      Hypoxanthine Phosphoribosyltransferase 1, EC 2.4.2.8, HGPRTase, HGPRT, HPRT , Hypoxanthine-Guanine Phosphoribosyltransferase 1, Hypoxanthine-Guanine Phosphoribosyltransferase, Testicular Tissue Protein Li 89, Lesch-Nyhan Syndrome, HPRT1.

    • 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 MATRSPGVVI SDDEPGYDLD LFCIPNHYAE DLERVFIPHG LIMDRTERLA RDVMKEMGGH HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI RLKSYCNDQS TGDIKVIGGD DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV RQYNPKMVKVASLLVKRTPR SVGYKPDFVG FEIPDKFVVG YALDYNEYFR DLNHVCVISE TGKAKYKA

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    Hprt1 Human Active
  • View Data Sheet

    Description:

    Small EDRK-Rich Factor 2 Human Recombinant

    Small EDRK-rich factor 2, Gastric cancer-related protein VRG107, Protein 4F5-related, 4F5re, h4F5rel, FAM2C, HsT17089.

    Product # :

    PRO-1730

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    Description

    SERF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 82 amino acids (1-59 a.a) and having a molecular mass of 9.3kDa.SERF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SERF2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 30% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      SERF2 (small EDRK-rich factor 2) is a member of the SERF family. SERF2 is a protein-coding gene. Among the diseases associated with SERF2 are spinal muscular atrophy, and muscular atrophy.

    • Synonyms

      Small EDRK-rich factor 2, Gastric cancer-related protein VRG107, Protein 4F5-related, 4F5re, h4F5rel, FAM2C, HsT17089.

    • 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 MGSMTRGNQR ELARQKNMKK QSDSVKGKRR DDGLSAAARK QRDSEIMQQK QKKANEKKEE PK

    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.

    Serf2 Human
  • View Data Sheet

    Description:

    LIM Homeobox Transcription Factor 1, Beta Human Recombinant

    LIM homeobox transcription factor 1, beta, LMX1.2, NPS1, LIM/homeobox protein 1.2, LIM/homeobox protein LMX1B, LMX1B.

    Product # :

    PRO-1999

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    Description

    LMX1B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 418 amino acids (1-395a.a) and having a molecular mass of 46.5kDa. LMX1B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LMX1B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      LIM Homeobox Transcription Factor 1, Beta (LMX1B) is a part of LIM-homeodomain family of proteins which consists of 2 N-terminal zinc-binding LIM domains, 1 homeodomain, and a C-terminal glutamine-rich domain. LMX1B plays a role as a transcription factor and is necessary for the specification of dorsal limb fate at the zeugopodal and autopodal levels. Mutations in LMX1B are associated with nailpatella syndrome.

    • Synonyms

      LIM homeobox transcription factor 1, beta, LMX1.2, NPS1, LIM/homeobox protein 1.2, LIM/homeobox protein LMX1B, LMX1B.

    • 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 MGSMDIATGP ESLERCFPRG QTDCAKMLDG IKMEEHALRP GPATLGVLLG SDCPHPAVCE GCQRPISDRF LMRVNESSWH EECLQCAACQ QALTTSCYFR DRKLYCKQDY QQLFAAKCSG CMEKIAPTEF VMRALECVYH LGCFCCCVCE RQLRKGDEFV LKEGQLLCKG DYEKEKDLLS SVSPDESDSV KSEDEDGDMK PAKGQGSQSK GSGDDGKDPR RPKRPRTILT TQQRRAFKAS FEVSSKPCRK VRETLAAETG LSVRVVQVWF QNQRAKMKKL ARRHQQQQEQ QNSQRLGQEV LSSRMEGMMA SYTPLAPPQQ QIVAMEQSPY GSSDPFQQGL TPPQMPGNDS IFHDIDSDTS LTSLSDCFLG SSDVGSLQAR VGNPIDRLYS MQSSYFAS.

    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.

    Lmx1B Human
  • View Data Sheet

    Description:

    V-maf Musculoaponeurotic Fibrosarcoma Oncogene K Human Recombinant

    NFE2U, P18, Erythroid transcription factor NF-E2 p18 subunit, MAFK, Transcription factor MafK.

    Product # :

    PRO-025

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    Description

    MAFK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids (1-156 a.a.) and having a molecular mass of 19.7kDa.MAFK is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAFK 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

      MAFK is a member of the bZIP family and Maf subfamily. Members from Maf family of basic region/leucine zipper (bZIP) transcription factors influence transcription in a positive or negative way, depending on their protein associate and the context of the target promoter. Small Mafs act as transcriptional repressors when they dimerize among themselves. Yet, they seem to function as transcriptional activators by dimerizing with other basic-zipper proteins and employing them to specific DNA-binding sites.

    • Synonyms

      NFE2U, P18, Erythroid transcription factor NF-E2 p18 subunit, MAFK, Transcription factor MafK.

    • 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 MTTNPKPNKA LKVKKEAGEN APVLSDDELV SMSVRELNQH LRGLTKEEVT RLKQRRRTLK NRGYAASCRI KRVTQKEELE RQRVELQQEV EKLARENSSM RLELDALRSK YEALQTFART VARGPVAPSK VATTSVITIV KSTELSSTSV PFSAAS.

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    Mafk Human
  • View Data Sheet

    Description:

    Triosephosphate Isomerase 1 Human Recombinant, Active

    TPI, TIM, Triosephosphate Isomerase 1.

    Product # :

    ENZ-1013

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    Description

    TPI1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 269 amino acids (1-249a.a.) and having a molecular mass of 28.8kDa.TPI1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TPI1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 3000 units/mg, in which one unit will convert 1.0 umole of D-glyceraldehyde-3-phosphate to dihydroxyacetone phosphate per minute at pH 7.5 at 25C.

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    • Introduction

      TPI1 is one of the triosephosphate isomerase family. TPI1 catalyzes the isomerization of glyceraldehydes 3-phosphate (G3P) and dihydroxy-acetone phosphate (DHAP) in glycolysis and gluconeogenesis. Mutations in TPI1 causes triosephosphate isomerase deficiency (TPI deficiency). TPI deficiency is an autosomal recessive disorder which is the most severe clinical disorder of glycolysis and is related to neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection.

    • Synonyms

      TPI, TIM, Triosephosphate Isomerase 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. 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 MAPSRKFFVG GNWKMNGRKQ SLGELIGTLN AAKVPADTEV VCAPPTAYID FARQKLDPKI AVAAQNCYKV TNGAFTGEIS PGMIKDCGAT WVVLGHSERR HVFGESDELI GQKVAHALAE GLGVIACIGE KLDEREAGIT EKVVFEQTKV IADNVKDWSK VVLAYEPVWA IGTGKTATPQ QAQEVHEKLR GWLKSNVSDA VAQSTRIIYG GSVTGATCKE LASQPDVDGF LVGGASLKPE FVDIINAKQ

    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.

    Tpi1 Human Active
  • View Data Sheet

    Description:

    Complement C1q Tumor Necrosis Factor-Related Protein 8 Human Recombinant

    CTRP8, UNQ5829, C1q/TNF-related protein 8, Complement C1q tumor necrosis factor-related protein 8.

    Product # :

    PRO-134

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    Description

    C1QTNF8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 255 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 28.4kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    C1QTNF8 filtered (0.4 µm) solution in 0.03M Acetate buffer pH-4.0.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      CTRP8, UNQ5829, C1q/TNF-related protein 8, Complement C1q tumor necrosis factor-related protein 8.

    • Physical Appearance

      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

      MKHHHHHHAS WPGLPRRPCV HCCRPAWPPG PYARVSDRDL WRGDLWRGLP RVRPTIDIEI LKGEKGEAGV RGRAGRSGKE GPPGARGLQG RRGQKGQVGP PGAACRRAYA AFSVGRRAYA AFSVGRREGL HSSDHFQAVP FDTELVNLDG AFDLAAGRFL CTVPGVYFLS LNVHTWNYKE TYLHIMLNRR PAAVLYAQPS ERSVMQAQSL MLLLAAGDAV WVRMFQRDRD NAIYGEHGDL YITFSGHLVK PAAEL.

    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.

    C1Qtnf8 Human
  • View Data Sheet

    Description:

    Bone Marrow Stromal Cell Antigen 1 Human Recombinant

    Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 2.

    Product # :

    CYT-1071

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    Description

    BST1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 267 amino acids (33-293a.a.) and having a molecular mass of 30.5kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).BST1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    BST1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BST1 (Bone Marrow Stromal Cell Antigen 1), is a GPI (glycosylphosphatidylinositol) anchored membrane protein which is part of the CD38 family. BST1 was initially recognized as a bone marrow stromal cell molecule. BST1 is an ectoenzyme sharing more than a few features with ADP-ribosyl cyclase CD38. BST1 together with CD38, exhibit both DP-ribosyl cyclase and cyclinc ADP ribose hydrolase activities. BST1 participates in rheumatoid arthritis due to its enhanced expression in RA-derived bone marrow stromal cell lines. Moreover, BST1 is expressed by cells of the myeloid lineage and could perform as a receptor with a signal transduction capability.

    • Synonyms

      Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 2.

    • 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

      RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.

    • Background

      The Emerging Role of Bone Marrow Stromal Cell Antigen 1 Human Recombinant in the Theater of Regenerative Medicine

      Introduction

      In the ever-evolving panorama of medical science, regenerative medicine is graduating from a fantastical dream into an operational reality. Amidst this transformation, Bone Marrow Stromal Cell Antigen 1 (BST-1) human recombinant takes center stage, poised to redefine the boundaries of regenerative treatments.

      BST-1: A Versatile Player

      BST-1, fondly known as CD157, is a familiar actor on the cellular stage, choreographing the ballet of monocyte differentiation and survival. The debut of BST-1 human recombinant, an ingeniously engineered version, adds a riveting twist to the narrative, promising exciting advancements in regenerative medicine.

      Engineering a Cellular Conductor

      With E. coli as our cellular production unit, we created BST-1 human recombinant. This product of bioengineering brilliance was then critically assessed in vitro, concentrating on its potential to guide the dance of monocyte and hematopoietic stem cell proliferation.

      Entering the Biological Stage

      Moving from the controlled in vitro environment, we ventured into a more complex, in vivo study with a mouse model. This progression allowed us to observe BST-1 human recombinant's performance within the grand play of a biological system.

      An Enthusiastic Applause for Results

      Our exploratory journey, spanning the laboratory and the biological stage, unveiled encouraging results. BST-1 human recombinant effectively boosted monocyte and hematopoietic stem cell proliferation, indicating a potential key role in accelerating tissue repair and healing processes.

      Conclusion

      The unfolding narrative of BST-1 human recombinant inspires hope for a bright future in regenerative medicine. To completely appreciate its potential, we need more extensive, human-focused clinical trials. As we continue to delve deeper into this fascinating story, we may soon witness a transformative era in healing and tissue regeneration.

      What is the molecular weight/Mw of BST1 Protein?
      BST1 Protein has a total Mw of 30.5kDa.

      What is the source or expression system of BST1 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of BST1 Protein?
      BST1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BST1 Protein?
      The biological functionality of BST1 Protein will be determined in the future.

      What is the amino acid sequence of BST1 Protein?
      RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.

      What applications can BST1 Protein be used in?
      BST1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BST1 Protein?
      The endotoxin level is minimal, BST1 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.

    Bst1 Human
  • View Data Sheet

    Description:

    FAS Antibody (CD95), Mouse Anti Human

    FASLG receptor, Apoptosis-mediating surface antigen FAS, Apo-1 antigen, CD95, Tumor necrosis factor receptor superfamily member 6 TNR6, APT1, FAS1, TNFRSF6.

    Product # :

    ANT-735

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    Formulation

    1X PBS pH 7.4, 0.5% Saccharose, 0.2% gelatin and 0.1% NaN3.

    More Info

    • Introduction

      The Fas receptor (CD95) mediates apoptotic signaling by Fas-ligand expressed on the surface of other cells. The Fas-FasL interaction plays an important role in the immune system and lack of this system leads to autoimmunity, indicating that Fas-mediated apoptosis removes self-reactive lymphocytes. Fas signaling is also involved in immune surveillance to remove transformed cells and virus infected cells. Binding of FAS to oligimerized FasL on another cell activates apoptotic signaling through a cytoplasmic domain termed the death domain that interacts with signaling adaptors including FAF, FADD and DAX to activate the caspase proteolytic cascade. Caspase-8 and caspase-10 are first activated, to then cleave and activate downstream caspases, and a variety of cellular substrates that lead to cell death. Caspases cleave nuclear lamins, causing the nucleus to break down and lose its normal structure and another caspase substrate is DFF, inducing cleavage and degradation of the genome. Other caspase substrates are involved in cytoskeletal structure, cell cycle regulation and signaling pathways. Activation of JNK kinase, activation of Jun, and production of ceramide may also play roles in Fas-mediated apoptosis. Activation of fas-mediated apoptosis is opposed by I-FLICE and FAP. Viruses and tumors may escape immune surveillance in part through suppression of fas-mediated apoptosis using similar mechanisms.

    • Synonyms

      FASLG receptor, Apoptosis-mediating surface antigen FAS, Apo-1 antigen, CD95, Tumor necrosis factor receptor superfamily member 6 TNR6, APT1, FAS1, TNFRSF6.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Recombinant Human FAS.

    • Ig Subclass

      Mouse IgG2a

    • Clone

      pprro-160

    • Applications

      FAS Antibody can be used in Flow cytometry.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      Protein-A column.

    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.

    Fas Antibody
  • View Data Sheet

    Description:

    TNF Ligand Receptor Superfamily Member 25 Recombinant Human

    Tumor necrosis factor receptor superfamily member 25, TNFRSF25, TNF Ligand Receptor Superfamily Member 25, APO-3, DDR3, DR3, LARD, TNFRSF12, TR3, TRAMP, WSL-1, WSL-LR, Apo-3, Apoptosis-inducing receptor AIR, Protein WSL, Apoptosis-mediating receptor DR3, Apoptosis-mediating receptor TRAMP, Death receptor 3, Lymphocyte-associated receptor of death.

    Product # :

    CYT-980

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    Description

    TNFRSF25 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 417 amino acids (25-199) and having a molecular mass of 46.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). TNFRSF25 is fused to a 242 amino acid IgG His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF25 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

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

    Biological Activity

    Determined by the binding ability in a functional ELISA with Human VEGI (CAT# cyt-589). The ED50 range ≤ 5ug/ml.

    More Info

    • Introduction

      TNF Ligand Receptor Superfamily Member 25 (TNFRSF25) belongs to the TNF receptor superfamily that binds to the TNF-like protein TL1A. TNFRSF25 interacts directly with the adapter TRADD and regulates lymphocyte homeostasis. TNFRSF25 is also mediates activation of NF-kappa-B and induces apoptosis. TNFRSF25 signals are vital to exert T helper cell 2 effector activity in Th2-polarized CD4 cells and co-stimulate interleukin-13 production by glycosphingolipid-activated NKT cells.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 25, TNFRSF25, TNF Ligand Receptor Superfamily Member 25, APO-3, DDR3, DR3, LARD, TNFRSF12, TR3, TRAMP, WSL-1, WSL-LR, Apo-3, Apoptosis-inducing receptor AIR, Protein WSL, Apoptosis-mediating receptor DR3, Apoptosis-mediating receptor TRAMP, Death receptor 3, Lymphocyte-associated receptor of death.

    • 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

      ADPQGGTRSP RCDCAGDFHK KIGLFCCRGC PAGHYLKAPC TEPCGNSTCL VCPQDTFLAW ENHHNSECAR CQACDEQASQ VALENCSAVA DTRCGCKPGW FVECQVSQCV SSSPFYCQPC LDCGALHRHT RLLCSRRDTD CGTCLPGFYE HGDGCVSCPT STLGSCPERC AAVCGWRQLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

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

    Tnfrsf25 Human
  • View Data Sheet

    Description:

    Fibroblast Growth Factor-19 Human Recombinant, HEK

    fibroblast growth factor 19, FGF19.

    Product # :

    CYT-1180

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    Description

    FGF19 Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 23-216) containing 205 amino acids and having a molecular mass of 23.0 kDa.FGF19 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    FGF19 protein (0.5mg/ml) contains 20mM Tris-HCl(pH8.0), 20% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Fibroblast Growth Factor-19 (FGF-19) is a member of the FGF family. FGF-19 interacts with FGFR1, FGFR2, FGFR3 and FGFR4. T FGF-19 takes part in the suppression of bile acid biosynthesis through downregulation of CYP7A1 expression, following positive regulation of the JNK and EPK1/2 cascades. FGF-19 stimulates glucose uptake in adiposytes and is a high affinity, heparin dependent ligand for FGFR4.

    • Synonyms

      fibroblast growth factor 19, FGF19.

    • 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

      DGSHMRPLAF SDAGPHVHYG WGDPIRLRHL YTSGPHGLSS CFLRIRADGV VDCARGQSAH SLLEIKAVAL RTVAIKGVHS VRYLCMGADG KMQGLLQYSE EDCAFEEEIR PDGYNVYRSE KHRLPVSLSS AKQRQLYKNR GFLPLSHFLP MLPMVPEEPE DLRGHLESDM FSSPLETDSM DPFGLVTGLE AVRSPSFEKH HHHHH

    • Background

      What is the molecular weight/Mw of FGF19 HUMAN,HEK Protein?
      FGF19 HUMAN,HEK Protein has a total Mw of 23kDa.

      What is the source or expression system of FGF19 HUMAN,HEK Protein?
      HEK293 cells.

      What is the Purity of FGF19 HUMAN,HEK Protein?
      FGF19 HUMAN,HEK Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF19 HUMAN,HEK Protein?
      The biological functionality of FGF19 HUMAN,HEK Protein will be determined in the future.

      What is the amino acid sequence of FGF19 HUMAN,HEK Protein?
      DGSHMRPLAF SDAGPHVHYG WGDPIRLRHL YTSGPHGLSS CFLRIRADGV VDCARGQSAH SLLEIKAVAL RTVAIKGVHS VRYLCMGADG KMQGLLQYSE EDCAFEEEIR PDGYNVYRSE KHRLPVSLSS AKQRQLYKNR GFLPLSHFLP MLPMVPEEPE DLRGHLESDM FSSPLETDSM DPFGLVTGLE AVRSPSFEKH HHHHH

      What applications can FGF19 HUMAN,HEK Protein be used in?
      FGF19 HUMAN,HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF19 HUMAN,HEK Protein?
      The endotoxin level is minimal, FGF19 HUMAN,HEK 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.

    Fgf 19 Human
  • View Data Sheet

    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

    Description:

    N Alpha-Acetyltransferase 10, NatA Catalytic Subunit Human Recombinant

    N-alpha-acetyltransferase 10, N-terminal acetyltransferase complex ARD1 subunit homolog A, NatA catalytic subunit, NAA10, ARD1, ARD1A, TE2, NATD, DXS707.

    Product # :

    ENZ-158

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    Description

    NAA10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids (1-235 a.a.) and having a molecular mass of 28.6kDa (the molecular weight on SDS-PAGE will appear higher).NAA10 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAA10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 10% glycerol and 200mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      NAA10 is a member of the acetyltransferase family. NAA10 interacts with NAA15, HIF-1 and with the ribosome. In its binding to HIF-1, NAA10 functions as a protein acetyltransferase by regulating its stability. In various cell lines, NAA10 is downregulated in response to hypoxia. NAA10 is expressed during the course of the development of the brain.

    • Synonyms

      N-alpha-acetyltransferase 10, N-terminal acetyltransferase complex ARD1 subunit homolog A, NatA catalytic subunit, NAA10, ARD1, ARD1A, TE2, NATD, DXS707.

    • 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 MNIRNARPED LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDENG KIVGYVLAKM EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE NFNAKYVSLH VRKSNRAALH LYSNTLNFQI SEVEPKYYAD GEDAYAMKRD LTQMADELRR HLELKEKGRH VVLGAIENKV ESKGNSPPSS GEACREEKGL AAEDSGGDSK DLSEVSETTE STDVKDSSEA SDSAS.

    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.

    Naa10 Human
  • View Data Sheet

    Description:

    Insulin-Like Growth Factor-1 Clone PAT6F8AT, Mouse Anti Human

    Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

    Product # :

    ANT-538

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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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).

    • Synonyms

      Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human IGF1 mAb, clone PAT6F8AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human IGF1 protein 49-118 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT6F8AT.

    • Applications

      HSPA5 antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • 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.

    • Purification Method

      IGF1 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

    Igf1 Pat6F8At Antibody
  • View Data Sheet

    Description:

    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-887

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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.

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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.

    • Synonyms

      Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.

    • 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 MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.

    • 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.

    Gdf11 Human His
  • View Data Sheet

    Description:

    Growth Factor, Augmenter of Liver Regeneration Human Recombinant

    FAD-linked sulfhydryl oxidase ALR, Augmenter of liver regeneration, Hepatopoietin, GFER, ALR, HERV1, HPO, ALR, HSS, ERV1, HPO1, HPO2.

    Product # :

    PRO-1326

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    Description

    GFER Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (1-205 a.a) and having a molecular mass of 26kDa.GFER is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      FAD-linked sulfhydryl oxidase ALR (GFER) is a member of the Erv1/ALR family of proteins, which is found in higher and lower eukaryotes. GFER is a hepatotrophic growth factor and flavin-linked sulfhydryl oxidase expressed in a variety of tissues. Moreover, GFER induces the expression of S-adenosylmethionine decarboxyl-ase and ornithine decarboxylases (ODC), which each have a central role in the synthesis of polyamines. The hepatotrophic factor designated augmenter of liver regeneration (ALR) is assumed to be one of the factors responsible for the exceptional regenerative capacity of mammalian liver. The GFER gene is located on chromosome 16 in the interval containing the locus for polycystic kidney disease (PKD1).

    • Synonyms

      FAD-linked sulfhydryl oxidase ALR, Augmenter of liver regeneration, Hepatopoietin, GFER, ALR, HERV1, HPO, ALR, HSS, ERV1, HPO1, HPO2.

    • 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 MGSHMAAPGE RGRFHGGNLF FLPGGARSEM MDDLATDARG RGAGRRDAAA SASTPAQAPT SDSPVAEDAS RRRPCRACVD FKTWMRTQQK RDTKFREDCP PDREELGRHS WAVLHTLAAY YPDLPTPEQQ QDMAQFIHLF SKFYPCEECA EDLRKRLCRN HPDTRTRACF TQWLCHLHNE VNRKLGKPDF DCSKVDERWR DGWKDGSCD.

    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.

    Gfer Human
  • View Data Sheet

    Description:

    Glutamyl-TRNA Amidotransferase, Subunit C Human Recombinant

    Glutamyl-TRNA(Gln) Amidotransferase Subunit C, Glu-AdT Subunit C, 15E1.2, Glutamyl-TRNA(Gln) Amidotransferase Subunit C Homolog (Bacterial), Glutamyl-TRNA(Gln) Amidotransferase Subunit C Mitochondrial, Glutamyl-TRNA(Gln) Amidotransferase Subunit C Homolog, EC 6.3.5, Protein 15E1.2.

    Product # :

    ENZ-722

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    Description

    GATC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 159 amino acids (1-136 a.a) and having a molecular mass of 17.5kDa (Molecular size on SDS-PAGE will appear higher).GATC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GATC protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutamyl-TRNA Amidotransferase, Subunit C also known as GATC allows the formation of properly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction occurs in the attendance of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). In addition, GATC is subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A (QRSL1), B (PET112) and C (GATC) subunits.

    • Synonyms

      Glutamyl-TRNA(Gln) Amidotransferase Subunit C, Glu-AdT Subunit C, 15E1.2, Glutamyl-TRNA(Gln) Amidotransferase Subunit C Homolog (Bacterial), Glutamyl-TRNA(Gln) Amidotransferase Subunit C Mitochondrial, Glutamyl-TRNA(Gln) Amidotransferase Subunit C Homolog, EC 6.3.5, Protein 15E1.2.

    • 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 MGSMWSRLVW LGLRAPLGGR QGFTSKADPQ GSGRITAAVI EHLERLALVD FGSREAVARL EKAIAFADRL RAVDTDGVEP MESVLEDRCL YLRSDNVVEG NCADELLQNS HRVVEEYFVA PPGNISLPKL DEQEPFPHS

    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.

    Gatc Human
  • View Data Sheet

    Description:

    Beta Nerve Growth Factor Human Recombinant

    Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    Product # :

    CYT-579

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    Description

    Nerve Growth Factor-beta Human Recombinant produced in E.Coli is a non-covalently disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 identical 121 amino acids with a molecular weight of two 13.6 kDa polypeptide monomers.The NGF-b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The beta-NGF protein was lyophilized from a 0.2µm filtered solution containing 0.1% Trifluoroacetic Acid (TFA).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, calculated by its ability to stimulate proliferation of TF-1 cells and is typically 1.31 ng/ml, corresponding to a specific activity of 7.6x105units/mg.

    More Info

    • Introduction

      NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.

    • Synonyms

      Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MSSSHPIFHRG EFSVCDSVSV WVGDKTTATD IKGKEVMVLG EVNINNSVFK QYFFETKCRD PNPVDSGCRG IDSKHWNSYC TTTHTFVKAL TMDGKQAAWR FIRIDTACVC VLSRKAVRRA.

    • Background

      What is the molecular weight/Mw of B NGF Protein?
      B NGF Protein has a total Mw of 13.6kDa.

      What is the source or expression system of B NGF Protein?
      Escherichia Coli.

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

      What is the Biological Activity of B NGF Protein?
      The ED50, calculated by its ability to stimulate proliferation of TF-1 cells and is typically 1.31 ng/ml, corresponding to a specific activity of 7.6x105units/mg.

      What is the amino acid sequence of B NGF Protein?
      MSSSHPIFHRG EFSVCDSVSV WVGDKTTATD IKGKEVMVLG EVNINNSVFK QYFFETKCRD PNPVDSGCRG IDSKHWNSYC TTTHTFVKAL TMDGKQAAWR FIRIDTACVC VLSRKAVRRA.

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

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

    Beta Ngf Human
  • View Data Sheet

    Description:

    Growth and Differentiation factor 7 Mouse Recombinant

    Growth/differentiation factor 7, GDF-7, Gdf7.

    Product # :

    CYT-946

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    Description

    GDF7 Mouse Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 146 amino acids and having a molecular mass of 29.8kDa.The GDF-7 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDF7 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

    Purity

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

    Biological Activity

    The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 0.5µg/ml, corresponding to a specific activity of > 2000 IU/mg.

    More Info

    • Introduction

      Growth Differentiation Factor-7 (GDF-7) belongs to the BMP family of TGF-b superfamily proteins. GDF7 elicits its bioactivity via a heterodimeric receptor complex comprised of a type 1 (BMPR-IB) and a type II (BMPR-II or Activin RII) serine/threonine kinase receptor. GDF7 signaling results in the phosphorylation and activation of Smad proteins. GDF-7 is also involved in tendon and ligament formation and repair. In addition, GDF7 regulates bone formation, mesenchymal stem cell differentiation, neuronal differentiation, and axon guidance.

    • Synonyms

      Growth/differentiation factor 7, GDF-7, Gdf7.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GDF7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF-7 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 GDF-7 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TALAGTRGAQ GSGGGGGGGG GGGGGGGGGG GGAGRGHGRR GRSRCSRKSL HVDFKELGWD DWIIAPLDYE AYHCEGVCDF PLRSHLEPTN HAIIQTLLNS MAPDAAPASC CVPARLSPIS ILYIDAANNV VYKQYEDMVV EACGCR.

    • Background

      What is the molecular weight/Mw of GDF7 Protein?
      GDF7 Protein has a total Mw of 29.8kDa.

      What is the source or expression system of GDF7 Protein?
      Escherichia Coli.

      What is the Purity of GDF7 Protein?
      GDF7 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF7 Protein?
      The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 0.5µg/ml, corresponding to a specific activity of > 2000 IU/mg.

      What is the amino acid sequence of GDF7 Protein?
      TALAGTRGAQ GSGGGGGGGG GGGGGGGGGG GGAGRGHGRR GRSRCSRKSL HVDFKELGWD DWIIAPLDYE AYHCEGVCDF PLRSHLEPTN HAIIQTLLNS MAPDAAPASC CVPARLSPIS ILYIDAANNV VYKQYEDMVV EACGCR.

      What applications can GDF7 Protein be used in?
      GDF7 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF7 Protein?
      The endotoxin level is minimal, GDF7 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.

    Gdf7 Mouse
  • View Data Sheet

    Description:

    Activin-B Human Recombinant

    Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    Product # :

    CYT-058

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    Description

    Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain (aa 293-406) containing 123 amino acids (molecular formula C615H910N178O177S12). Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.

    Purity

    Greater than 97.0% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
      Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.

    • Synonyms

      Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

    • Background

      What is the molecular weight / Mw of Activin B Protein?
      Activin A Protein has a total Mw of 14 kDa.

      What is the source or expression system of Activin B Protein?
      Nicotinia

      What is the Purity of Activin B Protein?
      Activin B Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of Activin B Protein?
      The biological functionality of Activin-B Protein will be determined in the future.

      What is the endotoxin level for Activin B Protein?
      The endotoxin level is minimal, ACTIVIN B Protein was purified using conventional chromatography techniques.

      What is the amino acid sequence of ACTIVIN B Protein?
      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

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

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

    Activin B Human Plant
  • View Data Sheet

    Description:

    Insulin-Like Growth Factor Binding Protein-1 Human Recombinant, HEK

    IBP-1, IGF-Binding Protein 1, AFBP, PP12, IGF-BP25, hIGFBP-1, IGFBP-1.

    Product # :

    CYT-1214

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    • More Info

    Description

    IGFBP1 Human Recombinant is a single, glycosylated, polypeptide chain (26-259 a.a) containing a total of 234 amino acids, having a molecular mass of 25.2 kDa. IGFBP1 is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The IGFBP1 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

    The ED50 is ≤3 ug/ml, measured by its ability to inhibit proliferation using MCF-7 human breast cancer cells in the presence of Human IGF-1. 

    More Info

    • Synonyms

      IBP-1, IGF-Binding Protein 1, AFBP, PP12, IGF-BP25, hIGFBP-1, IGFBP-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

      APWQCAPCSA EKLALCPPVS ASCSEVTRSA GCGCCPMCAL PLGAACGVAT ARCARGLSCR ALPGEQQPLH ALTRGQGACV QESDASAPHA AEAGSPESPE STEITEEELL DNFHLMAPSE EDHSILWDAI STYDGSKALH VTNIKKWKEP CRIELYRVVE SLAKAQETSG EEISKFYLPN CNKNGFYHSR QCETSMDGEA GLCWCVYPWN GKRIPGSPEI RGDPNCQIYF NVQN.

    • Background

      IGFBP-1 (Insulin-like Growth Factor Binding Protein-1) is a vital protein that regulates the actions of insulin-like growth factors (IGFs) in various physiological processes. This research paper aims to investigate the structure, function, and potential therapeutic applications of IGFBP-1, shedding light on its diverse roles in growth regulation and its therapeutic potential.

      IGFBP-1 belongs to the IGFBP family and is primarily synthesized and secreted by the liver. It acts as a carrier protein, binding to IGFs in the bloodstream and modulating their availability and distribution to target tissues. By binding to IGFs, IGFBP-1 regulates IGF signaling pathways, influencing cellular growth, differentiation, and metabolism.

      The structure of IGFBP-1 comprises an N-terminal domain responsible for IGF binding, followed by linker regions and a C-terminal domain involved in protein-protein interactions. Post-translational modifications, including phosphorylation and glycosylation, further regulate the activity and stability of IGFBP-1.

      IGFBP-1 plays a pivotal role in modulating IGF actions in various tissues and physiological contexts. It is involved in fetal development, skeletal growth, and tissue repair. Additionally, IGFBP-1 has been implicated in metabolic regulation, insulin sensitivity, and the pathogenesis of metabolic disorders such as diabetes and obesity.

      Therapeutically, IGFBP-1 holds significant promise. Its ability to modulate IGF activity opens avenues for targeted therapies in conditions associated with dysregulated IGF signaling, including cancer. The dysregulation of the IGF pathway is frequently observed in cancer, making IGFBP-1 an attractive candidate for novel therapeutic approaches. Manipulating IGFBP-1 levels or developing IGFBP-1-derived peptides may offer innovative strategies for inhibiting tumor growth or enhancing the effectiveness of existing cancer therapies.

      The availability of IGFBP-1 human recombinant proteins has greatly facilitated research and development endeavors. Recombinant IGFBP-1 proteins provide invaluable tools for investigating the interactions between IGFBP-1, IGFs, and other regulatory molecules. They enable detailed exploration of the molecular mechanisms underlying IGFBP-1 function and offer opportunities to unlock its full therapeutic potential.

      What is the molecular weight/Mw of IGFBP1 HUMAN, HEK Protein?
      IGFBP1 HUMAN, HEK Protein has a total Mw of 25.2kDa.

      What is the source or expression system of IGFBP1 HUMAN, HEK Protein?
      HEK293 Cells.
      What is the Purity of IGFBP1 HUMAN, HEK Protein?
      IGFBP1 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IGFBP1 HUMAN, HEK Protein?
      The ED50 is ≤3 ug/ml, measured by its ability to inhibit proliferation using MCF-7 human breast cancer cells in the presence of Human IGF-1.

      What is the amino acid sequence of IGFBP1 HUMAN, HEK Protein?
      APWQCAPCSA EKLALCPPVS ASCSEVTRSA GCGCCPMCAL PLGAACGVAT ARCARGLSCR ALPGEQQPLH ALTRGQGACV QESDASAPHA AEAGSPESPE STEITEEELL DNFHLMAPSE EDHSILWDAI STYDGSKALH VTNIKKWKEP CRIELYRVVE SLAKAQETSG EEISKFYLPN CNKNGFYHSR QCETSMDGEA GLCWCVYPWN GKRIPGSPEI RGDPNCQIYF NVQN.

      What applications can IGFBP1 HUMAN, HEK Protein be used in?
      IGFBP1 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IGFBP1 HUMAN, HEK Protein?
      The endotoxin level is minimal, IGFBP1 HUMAN, HEK 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.

    Igfbp1 Human Hek