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Search results

1000 results found for “Calmodulin”

Name

Description

Product #

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Quantity

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  • View Data Sheet

    Name :

    STX1A Human

    Description:

    Syntaxin-1A Human Recombinant

    STX1, HPC-1, p35-1, Syntaxin-1A, Neuron-specific antigen HPC-1, STX-1A, STX1A.

    Product # :

    PRO-574

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    Description

    Syntaxin-1A Human Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids (1-226) and having a molecular mass of 26.1 kDa.Recombinant Human STX1A contains N-terminal domain (Habc) and t_SNARE domain (H3 domain).

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris-HCl pH7.5, 10% glycerol, and 1mM DTT.

    Purity

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

    Citations

    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

      STX1, HPC-1, p35-1, Syntaxin-1A, Neuron-specific antigen HPC-1, STX-1A, STX1A.

    • 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 MLVESQ.

    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.

    Stx1A Human
  • View Data Sheet

    Name :

    BRD3 Human

    Description:

    Bromodomain Containing 3 Human Recombinant

    ORFX, RING3L, Bromodomain-containing protein 3, RING3-like protein, KIAA0043, RING3L.

    Product # :

    PRO-2143

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    Description

    BRD3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (1-416 a.a) and having a molecular mass of 48.1kDa.BRD3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BRD3 protein solution (0.5mg/ml) containing PBS buffer (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Bromodomain Containing 3 (BRD3) was classified based on its homology to the gene encoding the RING3 protein, which is a serine/threonine kinase. The BRD3 protein localizes to 9q34, a region which contains a number of major histocompatibility complex (MHC) genes. The function of the BRD3 protein is unknown.

    • Synonyms

      ORFX, RING3L, Bromodomain-containing protein 3, RING3-like protein, KIAA0043, RING3L.

    • 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 MGSMSTATTV APAGIPATPG PVNPPPPEVS NPSKPGRKTN QLQYMQNVVV KTLWKHQFAW PFYQPVDAIK LNLPDYHKII KNPMDMGTIK KRLENNYYWS ASECMQDFNT MFTNCYIYNK PTDDIVLMAQ ALEKIFLQKV AQMPQEEVEL LPPAPKGKGR KPAAGAQSAG TQQVAAVSSV SPATPFQSVP PTVSQTPVIA ATPVPTITAN VTSVPVPPAA APPPPATPIV PVVPPTPPVV KKKGVKRKAD TTTPTTSAIT ASRSESPPPL SDPKQAKVVA RRESGGRPIK PPKKDLEDGE VPQHAGKKGK LSEHLRYCDS ILREMLSKKH AAYAWPFYKP VDAEALELHD YHDIIKHPMD LSTVKRKMDG REYPDAQGFA ADVRLMFSNC YKYNPPDHEV VAMARKLQDV FEMRFAKMP.

    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.

    Brd3 Human
  • View Data Sheet

    Name :

    KLK10 Human

    Description:

    Kallikrein-10 Human Recombinant

    Kallikrein-Related Peptidase 10, KLK10, PRSSL1, NES1, Normal Epithelial Cell-Specific 1, Protease Serine-Like 1, Kallikrein 10, Breast Normal Epithelial Cell Associated Serine Protease, kallikrein-10, Protease, Serine-Like 1, EC 3.4.21.- , EC 3.4.21, EC 3.4.21.74.

    Product # :

    ENZ-795

    Price :

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    Description

    KLK10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 266 amino acids (34-276) and having a molecular mass of 29.1kDa.KLK10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The KLK10 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Kallikrein-10 (KLK10) is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19. Kallikreins are a subgroup of serine proteases having various physiological functions. KLK10 is secreted and has a role in suppression of tumorigenesis in breast and prostate cancers.

    • Synonyms

      Kallikrein-Related Peptidase 10, KLK10, PRSSL1, NES1, Normal Epithelial Cell-Specific 1, Protease Serine-Like 1, Kallikrein 10, Breast Normal Epithelial Cell Associated Serine Protease, kallikrein-10, Protease, Serine-Like 1, EC 3.4.21.- , EC 3.4.21, EC 3.4.21.74.

    • 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 MGSALLPQND TRLDPEAYGS PCARGSQPWQ VSLFNGLSFH CAGVLVDQSW VLTAAHCGNK PLWARVGDDH LLLLQGEQLR RTTRSVVHPK YHQGSGPILP RRTDEHDLML LKLARPVVLG PRVRALQLPY RCAQPGDQCQ VAGWGTTAAR RVKYNKGLTC SSITILSPKE CEVFYPGVVT NNMICAGLDR GQDPCQSDSG GPLVCDETLQ GILSWGVYPC GSAQHPAVYT QICKYMSWIN KVIRSN.

    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.

    Klk10 Human
  • View Data Sheet

    Name :

    CDC26 Human

    Description:

    Cell Division Cycle  26 Human Recombinant

    Anaphase-promoting complex subunit CDC26, Anaphase-promoting complex subunit 12, APC12, Cell division cycle protein 26 homolog, CDC26, ANAPC12, C9orf17.

    Product # :

    PRO-241

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    Description

    CDC26 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 105 amino acids (1-85 a.a) and having a molecular mass of 11.9kDa.CDC26 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CDC26 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CDC26 is a member of the CDC26 family which arranges progression via mitosis by enhancing cell-cycle regulators with ubiquitin chains. CDC26 is a component of the anaphase promoting complex/cyclosome (APC/C), which is a cell cycle-regulated E3 ubiquitin ligase which directs progression through mitosis and the G1 phase of the cell cycle. The APC/C complex operates by mediating ubiquitination and subsequent degradation of target proteins.

    • Synonyms

      Anaphase-promoting complex subunit CDC26, Anaphase-promoting complex subunit 12, APC12, Cell division cycle protein 26 homolog, CDC26, ANAPC12, C9orf17.

    • 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 MLRRKPTRLE LKLDDIEEFE NIRKDLETRK KQKEDVEVVG GSDGEGAIGL SSDPKSREQM INDRIGYKPQ PKPNNRSSQF GSLEF.

    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.

    Cdc26 Human
  • View Data Sheet

    Name :

    TSFM Human

    Description:

    Ts Translation Elongation Factor Mitochondrial Human Recombinant

    Elongation factor Ts, mitochondrial, Ts Translation Elongation Factor Mitochondrial, TSFM, EF-Ts, EF-TsMt, COXPD3.

    Product # :

    PRO-1971

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    Description

    TSFM Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (46-346 a.a) and having a molecular mass of 32.9kDa.TSFM is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TSFM is a mitochondrial translation elongation factor which is linked with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. TSFM stays bound to the aminoacyl-tRNA.EF-Tu.GTP complex until the GTP hydrolysis stage on the ribosome. Mutations in TSFM are related with combined oxidative phosphorylation deficiency-3 syndrome.

    • Synonyms

      Elongation factor Ts, mitochondrial, Ts Translation Elongation Factor Mitochondrial, TSFM, EF-Ts, EF-TsMt, COXPD3.

    • 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

      MSKELLMKLR RKTGYSFVNC KKALETCGGD LKQAEIWLHK EAQKEGWSKA AKLQGRKTKE GLIGLLQEGN TTVLVEVNCE TDFVSRNLKF QLLVQQVALG TMMHCQTLKD QPSAYSKVQW LTPVNLALWE AEAGGSLEGF LNSSELSGLP AGPDREGSLK DQLALAIGKL GENMILKRAA WVKVPSGFYV GSYVHGAMQS PSLHKLVLGK YGALVICETS EQKTNLEDVG RRLGQHVVGM APLSVGSLDD EPGGEAETKM LSQPYLLDPS ITLGQYVQPQ GVSVVDFVRF ECGEGEEAAE TE.

    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.

    Tsfm Human
  • View Data Sheet

    Name :

    TXN2 Yeast

    Description:

    Thioredoxin-2 Yeast Recombinant

    Thioredoxin-2, TRX2, TRX-2, TXN-2, TXN2.

    Product # :

    PRO-333

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    Description

    Thioredoxin-2 Yeast Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 12.6kDa.

    Source

    Escherichia Coli.

    Formulation

    Each mg of TRX2 protein contains 20mM phosphate buffer pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    TXN2 activity is assayed by measuring the change in absorbance at 650 nm at 25°C 
    The specific activity was found to be 3 units/mg.

    Citations

    More Info

    • Introduction

      Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by 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. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation.

    • Synonyms

      Thioredoxin-2, TRX2, TRX-2, TXN-2, TXN2.

    • Physical Appearance

      Sterile Lyophilized Powder.

    • Stability

      TXN2 although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized TXN2 in sterile 18MΩ-cm H2O.

    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.

    Trx1 Yeast
  • View Data Sheet

    Name :

    CIAPIN1 Human

    Description:

    Cytokine Induced Apoptosis Inhibitor 1 Human Recombinant

    DRE2, PRO0915, Anamorsin, Cytokine-induced apoptosis inhibitor 1, Fe-S cluster assembly protein DRE2 homolog, CIAPIN1.

    Product # :

    PRO-024

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    Description

    CIAPIN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-312 a.a.) and having a molecular mass of 36kDa.CIAPIN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CIAPIN1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Anamorsin, ( CIAPIN) is a member of anamorsin family. CIAPIN mainly expressed in the cytoplasm of liver, pancreas and heart tissue cells and does not show any homology to known apoptosis regulatory molecules of the Bcl-2 or CASP families, or to signal transduction molecules. CIAPIN1 Expression is reliant on growth factor stimulation. It is a ubiquitously expressed protein, and when it is overexpressed, it grants apoptotic resistance.

    • Synonyms

      DRE2, PRO0915, Anamorsin, Cytokine-induced apoptosis inhibitor 1, Fe-S cluster assembly protein DRE2 homolog, CIAPIN1.

    • 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 MGSMADFGIS AGQFVAVVWD KSSPVEALKG LVDKLQALTG NEGRVSVENI KQLLQSAHKE SSFDIILSGL VPGSTTLHSA EILAEIARIL RPGGCLFLKE PVETAVDNNS KVKTASKLCS ALTLSGLVEV KELQREPLTP EEVQSVREHL GHESDNLLFV QITGKKPNFE VGSSRQLKLS ITKKSSPSVK PAVDPAAAKL WTLSANDMED DSMDLIDSDE LLDPEDLKKP DPASLRAASC GEGKKRKACK NCTCGLAEEL EKEKSREQMS SQPKSACGNC YLGDAFRCAS CPYLGMPAFK PGEKVLLSDS NLHDA.

    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.

    Ciapin1 Human
  • View Data Sheet

    Name :

    Vaspin Human

    Description:

    Vaspin Recombinant Human

    Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    Product # :

    CYT-1132

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    Description

    Vaspin Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 394 amino acids and having a molecular mass of 45.1kDa. Vaspin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 150mM NaCl and 0.02 % Tween-20.

    Purity

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

    Citations

    More Info

    • Introduction

      Vaspin (visceral adipose-specific SERPIN) is a newly identified adipokine, which is a member of serine protease inhibitor family. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism.

    • Synonyms

      Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      LKPSFSPRNY KALSEVQGWK QRMAAKELAR QNMDLGFKLL KKLAFYNPGR NIFLSPLSIS TAFSMLCLGA QDSTLDEIKQ GFNFRKMPEK DLHEGFHYII HELTQKTQDL KLSIGNTLFI DQRLQPQRKF LEDAKNFYSA ETILTNFQNL EMAQKQINDF ISQKTHGKIN NLIENIDPGT VMLLANYIFF RARWKHEFDP NVTKEEDFFL EKNSSVKVPM MFRSGIYQVG YDDKLSCTIL EIPYQKNITA IFILPDEGKL KHLEKGLQVD TFSRWKTLLS RRVVDVSVPR LHMTGTFDLK KTLSYIGVSK IFEEHGDLTK IAPHRSLKVG EAVHKAELKM DERGTEGAAG TGAQTLPMET PLVVKIDKPY LLLIYSEKIP SVLFLGKIVN PIGK.

    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.

    Vaspin Protein
  • View Data Sheet

    Name :

    Vaspin Human, His

    Description:

    Vaspin Human Recombinant, His Tag

    Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    Product # :

    CYT-459

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    Description

    Vaspin Human Recombinant produced in E.Coli is a single, non-glycosylated, His Tag, polypeptide chain containing 415 amino acids and having a molecular mass of 47 kDa.The Vaspin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Vaspin in 20mM Tris pH-8, 0.2mM PMSF and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Vaspin (visceral adipose-specific SERPIN), a newly identified adipokine, which is a member of serine protease inhibitor family. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism.

    • Synonyms

      Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Liquid Vaspin although stable at 10°C for 1 week, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MLKPSFSPRN YKALSEVQGW KQRMAAKELA RQNMDLGFKL LKKLAFYNPG RNIFLSPLSI STAFSMLCLG AQDSTLDEIK QGFNFRKMPE KDLHEGFHYI IHELTQKTQD LKLSIGNTLF IDQRLQPQRK FLEDAKNFYS AETILTNFQN LEMAQKQIND FISQKTHGKI NNLIENIDPG TVMLLANYIF FRARWKHEFD PNVTKEEDFF LEKNSSVKVP MMFRSGIYQV GYDDKLSCTI LEIPYQKNIT AIFILPDEGK LKHLEKGLQV DTFSRWKTLL SRRVVDVSVP RLHMTGTFDL KKTLSYIGVS KIFEEHGDLT KIAPHRSLKV GEAVHKAELK MDERGTEGAA GTGAQTLPME TPLVVKIDKP YLLLIYSEKI PSVLFLGKIV NPIGK.

    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.

    Vaspin Human
  • View Data Sheet

    Name :

    RAB7A Human

    Description:

    RAB7A, Member RAS Oncogene Family Human Recombinant

    RAB7A member RAS oncogene family, RAB7, ras-related protein Rab-7a, FLJ20819, PSN, CMT2B, PRO2706.

    Product # :

    PRO-077

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    Description

    RAB7A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-207a.a.) and having a molecular mass of 25.6kDa.RAB7A is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RAB7A protein solution (0.5mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 100mM NaCl and 30% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      RAB7A belongs to the Ras superfamily of small Rab GTPases. RAB7A connects with the RIPL effector protein to regulator membrane trafficking from early to late endosome and to lysosomes. RAB7A can also regulate growth receptor endocytic trafficking, degradation, maturation of phagosome and autophagic vacuoles.

    • Synonyms

      RAB7A member RAS oncogene family, RAB7, ras-related protein Rab-7a, FLJ20819, PSN, CMT2B, PRO2706.

    • 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 MTSRKKVLLK VIILGDSGVG KTSLMNQYVN KKFSNQYKAT IGADFLTKEV MVDDRLVTMQ IWDTAGQERF QSLGVAFYRG ADCCVLVFDV TAPNTFKTLD SWRDEFLIQA SPRDPENFPF VVLGNKIDLE NRQVATKRAQ AWCYSKNNIP YFETSAKEAI
      NVEQAFQTIA RNALKQETEV ELYNEFPEPI KLDKNDRAKA SAESCSC.

    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.

    Rab7A Human
  • View Data Sheet

    Name :

    Visfatin Human

    Description:

    Visfatin Human Recombinant

    PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.

    Product # :

    CYT-318

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    Description

    Visfatin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 466 amino acids. The total molecular mass is 52.6kDa (calculated). The Visfatin is purified by Flag-affinity chromatography.

    Source

    Escherichia Coli.

    Formulation

    Visfatin was lyophilized with no additives.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The activity is determined by its ability to induce IL-6, IL-1 beta and TNF alpha production from human PBMCs at 100ng/ml.

    Citations

    More Info

    • Introduction

      Excess adiposity is the most important risk in the development of type 2 diabetes mellitus (T2DM). Adipose tissue produces several proteins (adipocytokines) such as leptin, adiponectin, resistin, tumor necrosis factor-a, and IL-6, that modulate sensitivity and appear to play an important role in the pathogenesis, diabetes, dyslipidemia, inflammation, and atherosclerosis. Visfatin, also known as pre-B cell colony-enhancing factor (PBEF), is a cytokine that is highly expressed in visceral fat and was originally isolated as a secreted factor that synergizes with IL-7 and stem cell factors to promote the growth of B cell precursors. Visfatin homologs have been identified in carp, invertebrate mollusks, and bacteria, as well as in vertebrates, including humans and the mouse. It has been postulated to play a role in innate immunity.
      Visfatin exerts mimetic effects that are dose-dependent and quantitatively similar to stimulating muscle and adipocyte glucose transport, and in inhibiting hepatocyte glucose production. Intravenous injection of recombinant visfatin in mice decreased plasma glucose in a dose-dependent fashion. In keeping with its mimetic effects, visfatin was as effective in reducing hyperglycemia in deficient diabetic mice. Visfatin was also found to be bound to and activate receptor, causing receptor phosphorylation and the activation of downstream signaling molecules. However, visfatin did not compete for binding to the receptor, indicating that the two proteins were recognized by different regions of the receptor. Thus, visfatin might play a role in glucose homeostasis and dysregulation in biosynthesis or signal transduction, and might contribute to the pathogenesis of diabetes.

    • Synonyms

      PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Visfatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Visfatin 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

      Centrifuge vial before opening. When reconstituting the product, gently pipet and wash down the sides of the vial to ensure full recovery of the protein into solution. It is recommended to reconstitute the lyophilized product with 20 mM HCl at a concentration of 0.1 mg/mL, which can be further diluted into other aqueous solutions. Wait several minutes for full reconstitution and solubility.

    • Amino Acid Sequence

      MPPNTSKVYS YFECREKKTE NSKLRKVKYE ETVFYGLQYI LNKYLKGKVV TKEKIQEAKD VYKEHFQDDV FNEKGWNYIL EKYDGHLPIE IKAVPEGFVI PRGNVLFTVE NTDPECYWLT NWIETILVQS WYPITVATNS REQKKILAKY LLETSGNLDG LEYKLHDFGY RGVSSQETAG IGASAHLVNF KGTDTVAGLA LIKKYYGTKD PVPGYSVPAA EHSTITAWGK DHEKDAFEHI VTQFSSVPVS VVSDSYDIYN ACEKIWGEDL RHLIVSRSTQ APLIIRPDSG NPLDTVLKVL EILGKKFPVT ENSKGYKLLP PYLRVIQGDG VDINTLQEIV EGMKQKMWSI ENIAFGSGGG LLQKLTRDLL NCSFKCSYVV TNGLGINVFK DPVADPNKRS KKGRLSLHRT PAGNFVTLEE GKGDLEEYGQ DLLHTVFKNG KVTKSYSFDE IRKNAQLNIE LEAAHH.

    • Background

      About Visfatin Human


      Visfatin is a cytokine expressed in visceral fat that was originally isolated as a secreted
      element that synergized with stem cell factors and IL-7. One of its main functions is to
      enhance the development of B cell precursors.

      The cytokine is also known as the “Pre-B Cell Colony-Enhancing Factor (PBEF).” It has been
      identified in vertebrates, including mice and humans, and it’s being studied due to its link
      to inflammatory conditions, beta cell function, and cardiovascular disease.


      What’s the Function of Visfatin Human Recombinant?

      Visfatin human recombinant is produced in E. Coli. It’s a single, non-glycosylated,
      polypeptide chain that contains 466 amino acids, it’s purified by FLAG-affinity
      chromatography, and it contains a total molecular mass of 52.6 kDa.


      What Are the Main Applications of Visfatin Human Recombinant?

      The cytokine is being researched because of its involvement in glucose homeostasis,
      dysregulation in biosynthesis and signal transduction, and the pathogenesis of diabetes.
      Visfatin human recombinant is tailored exclusively for laboratory research, ensuring
      experts can get further answers regarding the cytokine’s involvement in different
      processes, including pathogenesis, diabetes, inflammation, dyslipidemia, and
      atherosclerosis.

      Findings can also help during the identification of high-risk people for cardiovascular
      disease and diabetes.

    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.

    Visfatin Human
  • View Data Sheet

    Name :

    RELM g Mouse, His

    Description:

    RELM-Gamma Mouse Recombinant, His Tag

    Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.

    Product # :

    CYT-455

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    Description

    RELM-gamma Mouse Recombinant is a His -Tagged Fusion Protein having a molecular weight of 11 kDa containing 86 amino acid residues of the RELM-gamma Mouse and 16 additional amino acid residues – HisTag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      RELM-gamma is a novel member of the resistin-like molecule/found in inflammatory zone (RELM/FIZZ) family in mice and rats. Microarray and real-time RT-PCR experiments revealed a repression of RELMgamma mRNA in nasal respiratory epithelium of cigarette smoke-exposed versus untreated rats. The analysis of the physiological tissue-specific expression revealed highest expression in hematopoietic tissues, suggesting a cytokine-like role for RELM-gamma. RELM-gamma-mRNA is detectable in bone marrow, spleen, and lung as well as in peripheral blood granulocytes. Promyelocytic HL60 cells transfected with a RELM-gamma expression plasmid have an increased proliferation rate compared to mock-transfected cells and display an altered response to retinoic acid-induced granulocytic differentiation. Taken together, these data provide the first experimental evidence that RELM-gamma is a secreted molecule with a restricted expression pattern that may play a role in promyelocytic differentiation.

    • Synonyms

      Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.The lyophilized protein remains stable until the expiry date when stored at -20°C.

    • Solubility

      It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MRGSHHHHHH GMASHMTLES IVEKKVKELL ANRDDCPSTV TKTFSCTSIT ASGRLASCPS GMTVTGCACG YGCGSWDIRD GNTCHCQCST MDWATARCCQ LA.

    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.

    Relm Gamma Mouse
  • View Data Sheet

    Name :

    Midkine Human

    Description:

    Midkine Human Recombinant

    NEGF-2, Neurite Growth-Promoting Factor 2, MK, Neurite outgrowth-promoting protein, Midgestation and kidney protein, Amphiregulin-associated protein, ARAP, Neurite outgrowth-promoting factor 2, FLJ27379, Midkine, MK1, NEGF2.

    Product # :

    CYT-192

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    Description

    Midkine Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 123 amino acids and having a molecular mass of 13.4kDa. The Midkine is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract human neutrophils using a concentration range of 0.1-10 ng/ml corresponding to a specific activity of 100,000-10,000,000IU/mg.

    Citations

    More Info

    • Introduction

      Midkine (MK) is the product of a retinoic acid responsive gene. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
      Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
      The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
      Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
      Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
      Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis.

    • Synonyms

      NEGF-2, Neurite Growth-Promoting Factor 2, MK, Neurite outgrowth-promoting protein, Midgestation and kidney protein, Amphiregulin-associated protein, ARAP, Neurite outgrowth-promoting factor 2, FLJ27379, Midkine, MK1, NEGF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      VAKKKDKVKK GGPGSECAEW AWGPCTPSSK DCGVGFREGT CGAQTQRIRC RVPCNWKKEF GADCKYKFEN WGACDGGTGT KVRQGTLKKA RYNAQCQETI RVTKPCTPKT KAKAKAKKGK GKD.

    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.

    Midkine Human
  • View Data Sheet

    Name :

    AIFM1 Human

    Description:

    Apoptosis-Inducing Factor, Mitochondrion-Associated, 1 Human Recombinant

    Apoptosis-inducing factor 1, mitochondrial, Programmed cell death protein 8, AIFM1, AIF, PDCD8, CMTX4, COWCK, COXPD6, isoform 2 precursor, Apoptosis-Inducing Factor, Mitochondrion-Associated, 1.

    Product # :

    PRO-1898

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    Description

    AIFM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 537 amino acids (98-609) and having a molecular mass of 58.5 kDa.AIFM1 is fused to a 25 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AIFM1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Apoptosis-Inducing Factor, Mitochondrion-Associated, 1 (AIFM1) is a mitochondrial protein which translocates to the nucleus once apoptosis has been initiated. AIFM1 causes DNA fragmentation and chromatin condensation and also triggers the release of cytochrome c and caspase-9 from mitochondria. Bcl-2 overexpression prevents the release of AIFM1 from mitochondria, but doesn’t block its apoptogenic activity.

    • Synonyms

      Apoptosis-inducing factor 1, mitochondrial, Programmed cell death protein 8, AIFM1, AIF, PDCD8, CMTX4, COWCK, COXPD6, isoform 2 precursor, Apoptosis-Inducing Factor, Mitochondrion-Associated, 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 MGSEFLGLTP EQKQKKAALS ASEGEEVPQD KAPSHVPFLL IGGGTAAFAA ARSIRARDPG ARVLIVSEDP ELPYMRPPLS KELWFSDDPN VTKTLRFKQW NGKERSIYFQ PPSFYVSAQD LPHIENGGVA VLTGKKVVQL DVRDNMVKLN DGSQITYEKC LIATGGTPRS LSAIDRAGAE VKSRTTLFRK IGDFRSLEKI SREVKSITII GGGFLGSELA CALGRKARAL GTEVIQLFPE KGNMGKILPE YLSNWTMEKV RREGVKVMPN AIVQSVGVSS GKLLIKLKDG RKVETDHIVA AVGLEPNVEL AKTGGLEIDS DFGGFRVNAE LQARSNIWVA GDAACFYDIK LGRRRVEHHD HAVVSGRLAG ENMTGAAKPY WHQSMFWSDL GPDVGYEAIG LVDSSLPTVG VFAKATAQDN PKSATEQSGT GIRSESETES EASEITIPPS TPAVPQAPVQ GEDYGKGVIF YLRDKVVVGI VLWNIFNRMP IARKIIKDGE QHEDLNEVAK LFNIHED.

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    Aifm1 Human
  • View Data Sheet

    Name :

    SHH Rat

    Description:

    Sonic HedgeHog Rat Recombinant

    SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.

    Product # :

    CYT-1099

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    Description

    Sonic HedgeHog Recombinant Rat produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.9kDa. SHH is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SHH is lyophilized from a sterile (0.2 µm) filtered solution containing 10 mM sodium phosphate, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog helps in guiding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is necessary for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.

    • Synonyms

      SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MIIGPGRGFG KRQHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKITRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKARI HCSVKAENSV AAKSDG.

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    Shh Rat
  • View Data Sheet

    Name :

    GDF15 Mouse

    Description:

    Growth and Differentiation factor 15 Mouse Recombinant

    Growth/differentiation factor 15, GDF-15.

    Product # :

    CYT-857

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    Description

    GDF15 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (189-303 a.a) and having a molecular mass of 14.9kDa. GDF15 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDF15 protein solution (1.0mg/ml) containing 20mM Phosphate buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    GDF15 Mouse SDS-PAGE - Product image 1

    Citations

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    • Introduction

      GDF15 is part of the TGF-Beta superfamily which is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.

    • Synonyms

      Growth/differentiation factor 15, GDF-15.

    • 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 MGSSAHAHPR DSCPLGPGRC CHLETVQATL EDLGWSDWVL SPRQLQLSMC VGECPHLYRS ANTHAQIKAR LHGLQPDKVP APCCVPSSYT PVVLMHRTDS GVSLQTYDDL VARGCHCA.

    • Background

      What is the molecular weight/Mw of GDF15 MOUSE Protein?
      GDF15 MOUSE Protein has a total Mw of 14.9kDa.

      What is the source or expression system of GDF15 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of GDF15 MOUSE Protein?
      GDF15 MOUSE Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF15 MOUSE Protein?
      The biological functionality of GDF15 MOUSE Protein will be determined in the future.

      What is the amino acid sequence of GDF15 MOUSE Protein?
      MGSSHHHHHH SSGLVPRGSH MGSSAHAHPR DSCPLGPGRC CHLETVQATL EDLGWSDWVL SPRQLQLSMC VGECPHLYRS ANTHAQIKAR LHGLQPDKVP APCCVPSSYT PVVLMHRTDS GVSLQTYDDL VARGCHCA.

      What applications can GDF15 MOUSE Protein be used in?
      GDF15 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF15 MOUSE Protein?
      The endotoxin level is minimal, GDF15 MOUSE Protein was purified using conventional chromatography techniques.

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    Gdf15 Mouse
  • View Data Sheet

    Name :

    DNAJC15 Human

    Description:

    DnaJ (Hsp40) Homolog, Subfamily C, Member 15 Human Recombinant

    DnaJ homolog subfamily C member 15, Cell growth-inhibiting gene 22 protein, Methylation-controlled J protein, MCJ, DNAJC15, DNAJD1, GIG22, HSD18.

    Product # :

    HSP-057

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    Description

    DNAJC15 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 116 amino acids (58-150 a.a.) and having a molecular mass of 12.8 kDa.DNAJC15 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DNAJC15 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

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    • Introduction

      DNAJC15 which is expressed ubiquitously and located on the membrane contains 1 J domain. In many advanced cases of ovarian adenocarcinoma DNAJC15 is absent or down-regulated, due to hypermethylation and allelic loss. Loss of expression correlates with increased resistance to antineoplastic drugs, such as cisplatin. DNAJC15is a crucial component of the TIM23 translocase complex and stimulates the ATPase activity of HSPA9.

    • Synonyms

      DnaJ homolog subfamily C member 15, Cell growth-inhibiting gene 22 protein, Methylation-controlled J protein, MCJ, DNAJC15, DNAJD1, GIG22, HSD18.

    • 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 MGSFRIWKPL EQVITETAKK ISTPSFSSYY KGGFEQKMSR REAGLILGVS PSAGKAKIRT AHRRVMILNH PDKGGSPYVA AKINEAKDLL ETTTKH.

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    Dnajc15 Human
  • View Data Sheet

    Name :

    SYT4 Human

    Description:

    Synaptotagmin IV Human Recombinant

    HsT1192, KIAA1342, Synaptotagmin-4, Synaptotagmin IV, SytIV, SYT4.

    Product # :

    PRO-1375

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    Description

    SYT4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (38-425a.a) and having a molecular mass of 46.1kDa. SYT4 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    SYT4 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      Synaptotagmin-4 (SYT4) is a part of the synaptotagmin proteins family. Synaptotagmins are a large gene family of synaptic vesicle type III integral membrane proteins that operate as regulators of both exocytosis and endocytosis and are involved in neurotransmitter secretion from small secretory vesicles. SYT4 is expressed in neuronal tissues, and has the highest mRNA levels in the hippocampus. The proximity of the SYT4 gene to markers of several psychiatric disorders implies an involvement of SYT4 in human disease such as pheochromocytoma, and parkinson's disease.

    • Synonyms

      HsT1192, KIAA1342, Synaptotagmin-4, Synaptotagmin IV, SytIV, SYT4.

    • 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 MCQRKSSKSN KTPPYKFVHV LKGVDIYPEN LNSKKKFGAD DKNEVKNKPA VPKNSLHLDL EKRDLNGNFP KTNLKPGSPS DLENATPKLF LEGEKESVSP ESLKSSTSLT SEEKQEKLGT LFFSLEYNFE RKAFVVNIKE ARGLPAMDEQ SMTSDPYIKM TILPEKKHKV KTRVLRKTLD PAFDETFTFY GIPYTQIQEL ALHFTILSFD RFSRDDIIGE VLIPLSGIEL SEGKMLMNRE IIKRNVRKSS GRGELLISLC YQSTTNTLTV VVLKARHLPK SDVSGLSDPY VKVNLYHAKK RISKKKTHVK KCTPNAVFNE LFVFDIPCEG LEDISVEFLV LDSERGSRNE VIGQLVLGAA AEGTGGEHWK EICDYPRRQI AKWHVLCDG.

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    Syt4 Human
  • View Data Sheet

    Name :

    FCER1A Human, HEK

    Description:

    Fc-Epsilon RI-Alpha Human Recombinant, HEK

    FCERIA, FCERA, Fc epsilon receptor Ia, Fcepsilon RI-alpha, Fc epsilon RI alpha chain, FcERI, High affinity immunoglobulin epsilon receptor subunit alpha isoform1, IgE Fc receptor subunit alpha, FCER1A, FCE1A.

    Product # :

    PRO-2779

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    Description

    FCER1A Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 186 amino acids (26-205aa) and having a molecular mass of 21.8kDa. FCER1A is fused to a 6 His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293.

    Formulation

    FCER1A protein solution (1mg/ml) containing 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range ≤ 0.01 ug/ml and is measured by its binding ability in a functional ELISA with Human IgE.

    Citations

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    • Synonyms

      FCERIA, FCERA, Fc epsilon receptor Ia, Fcepsilon RI-alpha, Fc epsilon RI alpha chain, FcERI, High affinity immunoglobulin epsilon receptor subunit alpha isoform1, IgE Fc receptor subunit alpha, FCER1A, FCE1A.

    • 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

      VPQKPKVSLN PPWNRIFKGE NVTLTCNGNN FFEVSSTKWF HNGSLSEETN SSLNIVNAKF EDSGEYKCQH QQVNESEPVY LEVFSDWLLL QASAEVVMEG QPLFLRCHGW RNWDVYKVIY YKDGEALKYW YENHNISITN ATVEDSGTYY CTGKVWQLDY ESEPLNITVI KAPREKYWLQ HHHHHH

    • Background

      The FCER1A gene encodes the alpha subunit of the high-affinity immunoglobulin E (IgE) receptor, known as FCER1A. This receptor is primarily expressed on mast cells and basophils, and its activation plays a pivotal role in allergic and inflammatory responses. This research aims to explore the significance of FCER1A and its potential implications in allergic disorders and immune-mediated diseases. By investigating the functions and regulation of FCER1A, we can gain insights into its role in immune responses and identify potential therapeutic targets.

      The FCER1A receptor is responsible for the binding of IgE antibodies, initiating a cascade of signaling events upon allergen exposure. Crosslinking of IgE-bound FCER1A leads to the release of various inflammatory mediators, such as histamine, cytokines, and leukotrienes, which contribute to the clinical manifestations of allergic reactions. Understanding the molecular mechanisms underlying FCER1A activation and downstream signaling is crucial for comprehending allergic diseases.

      In addition to its role in allergies, FCER1A has been implicated in immune-mediated inflammatory diseases, including asthma, atopic dermatitis, and autoimmune conditions. Dysregulation of FCER1A expression and signaling pathways can lead to exaggerated immune responses and chronic inflammation. Investigating the genetic and epigenetic factors influencing FCER1A expression and the interplay between FCER1A and other immune molecules can provide valuable insights into disease pathogenesis.

      This research will delve into the molecular mechanisms governing FCER1A expression, activation, and downstream signaling pathways. The paper will explore the regulatory effects of FCER1A on mast cell and basophil activation, the release of inflammatory mediators, and the recruitment of other immune cells. Additionally, it will examine the impact of FCER1A dysregulation in allergic and immune-mediated diseases and discuss the potential of FCER1A as a therapeutic target for intervention.

      The study will also investigate the diagnostic and prognostic value of FCER1A in various allergic and immune disorders. Understanding the expression patterns and alterations of FCER1A in different diseases and patient populations may aid in disease stratification, treatment selection, and monitoring of treatment response.

      By unraveling the molecular mechanisms underlying FCER1A's functions in allergic and inflammatory responses, this research aims to contribute to our understanding of immune-mediated diseases. Furthermore, it highlights the potential of FCER1A as a target for therapeutic interventions and emphasizes the need for further investigations to develop novel treatments and improve patient outcomes.

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    Fcer1A Protein
  • 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.

    Citations

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    • 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.

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    Thioredoxin Mouse
  • View Data Sheet

    Name :

    NRP1 Rat

    Description:

    Neuropilin 1 Rat Recombinant

    Neuropilin-1, Vascular endothelial cell growth factor 165 receptor, CD304, Nrp1.

    Product # :

    CYT-973

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    Description

    NRP1 Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 842 amino acids (22-855 a.a.) and having a molecular mass of 94.8kDa (Migrates at 100-150kDa on SDS-PAGE under reducing conditions).NRP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    NRP1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      Neuropilin 1 (Nrp1) is a transmembrane glycoprotein which functions as a co-receptor for several extracellular ligands including class III/IV semaphorins, some isoforms of vascular endothelial growth factor and transforming growth factor beta. Nrp1 binds vascular endothelial growth factor (VEGF)-A and is believed to serve as a coreceptor for kinase insert domain-containing receptor (KDR) by connecting with KDR and enhancing VEGF signaling. Nrp1 is a marker of regulatory T cells.

    • Synonyms

      Neuropilin-1, Vascular endothelial cell growth factor 165 receptor, CD304, Nrp1.

    • 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

      FRSDKCGGTI KIENPGYLTS PGYPHSYHPS EKCEWLIQAP EPYQRIMINF NPHFDLEDRD CKYDYVEVID GENEGGRLWG KFCGKIAPSP VVSSGPFLFI KFVSDYETHG AGFSIRYEIF KRGPECSQNY TAPTGVIKSP GFPEKYPNSL ECTYIIFAPK MSEIILEFES FDLEQDSNPP GGVFCRYDRL EIWDGFPEVG PHIGRYCGQK TPGRIRSSSG ILSMVFYTDS AIAKEGFSAN YSVLQSSISE DFKCMEALGM ESGEIHSDQI TASSQYGTNW SVERSRLNYP ENGWTPGEDS YREWIQVDLG LLRFVTAVGT QGAISKETKK KYYVKTYRVD ISSNGEDWIT LKEGNKAIIF QGNTNPTDVV FGVFPKPLIT RFVRIKPASW ETGISMRFEV YGCKITDYPC SGMLGMVSGL ISDSQITASN QGDRNWMPEN IRLVTSRTGW ALPPSPHPYI NEWLQVDLGD EKIVRGVIIQ GGKHRENKVF MRKFKIAYSN NGSDWKMIMD DSKRKAKSFE GNNNYDTPEL RAFTPLSTRF IRIYPERATH SGLGLRMELL GCEVEVPTAG PTTPNGNPVD ECDDDQANCH SGTGDDFQLT GGTTVLATEK PTIIDSTIQS EFPTYGFNCE FGWGSHKTFC HWEHDSHAQL RWRVLTSKTG PIQDHTGDGN FIYSQADENQ KGKVARLVSP VVYSQSSAHC MTFWYHMSGS HVGTLRVKLH YQKPEEYDQL VWMVVGHQGD HWKEGRVLLH KSLKLYQVIF EGEIGKGNLG GIAVDDISIN NHIPQEDCAK PTDLDKKNTE IKIDETGSTP GYEEGKGDKN ISRKPGNVLK TLDPLEHHHH HH

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    Nrp1 Rat
  • View Data Sheet

    Name :

    EGF Long Human

    Description:

    Epidermal Growth Factor Long Human Recombinant

    Urogastrone, URG, EGF.

    Product # :

    CYT-798

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    Description

    Recombinant Human EGF Long produced in E.coli cells is a single non-glycosylated, polypeptide chain containing 106 amino acids and having a molecular mass of 12.3kDa. The EGF Long is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EGF Long was lyophilized from a 0.2µm filtered concentrated solution in 10mM HCl.

    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 a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 106 IU/mg.

    Citations

    More Info

    • Introduction

      Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Long EGF is a recombinant analog of Human EGF developed as a replacement for use in therapeutic cell culture applications as a like-for-like supplement for Recombinant Human or native EGF. It includes the Human EGF amino acid sequence plus a 53 amino acid N-terminal extension peptide.

    • Synonyms

      Urogastrone, URG, EGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized EGF Long although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF Long 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 EGF Long in sterile 100mM AcOH (acetic Acid) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR

    • Background

      What is the molecular weight/Mw of EGF Protein?
      EGF Protein has a total Mw of 12.3kDa.

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

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

      What is the Biological Activity of EGF Protein?
      The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 106 IU/mg.

      What is the amino acid sequence of EGF Protein?
      MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR

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

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

    Egf Long Human
  • View Data Sheet

    Name :

    FGF 9 Rat

    Description:

    Fibroblast Growth Factor-9 Rat Recombinant

    GAF (Glia-activating factor), HBGF-9, MGC119914, MGC119915, FGF-9.

    Product # :

    CYT-558

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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

    Description

    Rat FGF9 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids and having a molecular mass of 23.3kDa.The FGF-9 Mouse Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FGF-9 was lyophilized from a concentrated (1mg/ml) sterile solution containing 10mM NaP, pH-7.5 &, 75mM Ammonium Sulfate.

    Purity

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

    Biological Activity

    The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2,000,000 Units/mg.

    Citations

    More Info

    • Introduction

      Rat and mouse FGF-9 show a very high homology to human FGF-9. The transcripts for FGF-9 have been found in brain and in kidney tissue. Fibroblast Growth Factor-9 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF9 was isolated as a secreted factor that exhibits a growth-stimulating effect on cultured glial cells. In nervous system, this protein is produced mainly by neurons and may be important for glial cell development. Expression of the mouse homolog of this gene was found to be dependent on Sonic hedgehog (Shh) signaling. Mice lacking the homolog gene displayed a male-to-female sex reversal phenotype, which suggested a role in testicular embryogenesis Fibroblast Growth Factor 9 may have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors.

    • Synonyms

      GAF (Glia-activating factor), HBGF-9, MGC119914, MGC119915, FGF-9.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Rat Fibroblast Growth Factor-9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF9 Rat Recombinant 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 Rat FGF-9 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MPLGEVGSYFG VQDAVPFGNV PVLPVDSPVL LNDHLGQSEA GGLPRGPAVT DLDHLKGILR RRQLYCRTGF HLEIFPNGTI QGTRKDHSRF GILEFISIAV GLVSIRGVDS GLYLGMNEKG ELYGSEKLTQ ECVFREQFEE NWYNTYSSNL YKHVDTGRRY YVALNKDGTP REGTRTKRHQ KFTHFLPRPV DPDKVPELYK DILSQS.

    • Background

      What is the molecular weight/Mw of FGF9 Protein?
      FGF9 Protein has a total Mw of 23.3kDa.

      What is the source or expression system of FGF9 Protein?
      Escherichia Coli.

      What is the Purity of FGF9 Protein?
      FGF9 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF9 Protein?
      The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2,000,000 Units/mg.

      What is the amino acid sequence of FGF9 Protein?
      MPLGEVGSYFG VQDAVPFGNV PVLPVDSPVL LNDHLGQSEA GGLPRGPAVT DLDHLKGILR RRQLYCRTGF HLEIFPNGTI QGTRKDHSRF GILEFISIAV GLVSIRGVDS GLYLGMNEKG ELYGSEKLTQ ECVFREQFEE NWYNTYSSNL YKHVDTGRRY YVALNKDGTP REGTRTKRHQ KFTHFLPRPV DPDKVPELYK DILSQS.

      What applications can FGF9 Protein be used in?
      FGF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF9 Protein?
      The endotoxin level is minimal, FGF9 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.

    Fgf9 Rat
  • View Data Sheet

    Name :

    TTC32 Human

    Description:

    Tetratricopeptide Repeat Domain 32 Human Recombinant

    Tetratricopeptide Repeat Domain 32, Tetratricopeptide Repeat Protein 32, TPR Repeat Protein 32.

    Product # :

    PRO-1246

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

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    • source
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    • purity
    • More Info
    • Citations

    Description

    TTC32 Human Recombinant produced in E. coli is a single polypeptide chain containing 174 amino acids (1-151) and having a molecular mass of 19.7 kDa. TTC32 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TTC32 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 2mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TTC32 contains 3 TPR repeats. The tetratricopeptide repeat (TPR) is a structural motif. TPR is observed in organized 3–16 motifs, which form scaffolds to mediate protein–protein interactions and frequently the assembly of multiprotein complexes. TPR-containing proteins include the anaphase-promoting complex subunits cdc16, cdc23 and cdc27, the NADPH oxidase subunit p67-phox, hsp90-binding immunophilins, transcription factors, the major receptor for peroxisomal matrix protein import PEX5, the PKR protein kinase inhibitor and mitochondrial import proteins.

    • Synonyms

      Tetratricopeptide Repeat Domain 32, Tetratricopeptide Repeat Protein 32, TPR Repeat Protein 32.

    • 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 MGSMEGQRQE SHATLTLAQA HFNNGEYAEA EALYSAYIRR CACAASSDES PGSKCSPEDL ATAYNNRGQI KYFRVDFYEA MDDYTSAIEV QPNFEVPYYN RGLILYRLGY FDDALEDFKK VLDLNPGFQD ATLSLKQTIL DKEEKQRRNV AKNY.

    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.

    Ttc32 Human
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