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Search results

1000 results found for “cysteine-rich”

Name

Description

Product #

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  • View Data Sheet

    Name :

    TOR1A Human

    Description:

    Torsin Family 1 Member A Human Recombinant

    DQ2, DYT1, Torsin-1A, Dystonia 1 protein, Torsin family 1 member A, TOR1A.

    Product # :

    PRO-1430

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    • More Info

    Description

    TOR1A Human Recombinant produced in E. coli is a single polypeptide chain containing 333 amino acids (21-332) and having a molecular mass of 38kDa. TOR1A is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TOR1A solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      TOR1A which is a member of the AAA family of adenosine triphosphatases (ATPases) is associated to the Clp protease/heat shock family and is expressed highly in the substantia nigra pars compacta.TOR1A functions as a molecular chaperone assisting in the suitable folding of secreted and/or membrane proteins. Mutations in TOR1A result in the autosomal dominant disorder, torsion dystonia one.

    • Synonyms

      DQ2, DYT1, Torsin-1A, Dystonia 1 protein, Torsin family 1 member A, TOR1A.

    • 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 MVEPISLGLA LAGVLTGYIY PRLYCLFAEC CGQKRSLSRE ALQKDLDDNL FGQHLAKKII LNAVFGFINN PKPKKPLTLS LHGWTGTGKN FVSKIIAENI YEGGLNSDYV HLFVATLHFP HASNITLYKD QLQLWIRGNV SACARSIFIF DEMDKMHAGL IDAIKPFLDY YDLVDGVSYQ KAMFIFLSNA GAERITDVAL DFWRSGKQRE DIKLKDIEHA LSVSVFNNKN SGFWHSSLIH RNLIDYFVPF LPLEYKHLKM CIRVEMQSRG YEIDEDIVSR VAEEMTFFPK EERVFSDKGC KTVFTKLDYY YDD.

    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.

    Tor1A Human
  • View Data Sheet

    Name :

    CDC123 Human

    Description:

    Cell Division Cycle 123 Human Recombinant

    C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.

    Product # :

    PRO-1463

    Price :

    Quantity :

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    Description

    CDC123 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 359 amino acids (1-336 a.a) and having a molecular mass of 41.5kDa.CDC123 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CDC123 protein solution (0. 5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CDC123 is a member of the CDC123 family. CDC123is required for S phase entry of the cell cycle. It is also broadly expressed in spleen,thymus, prostate, testis, ovary, small intestine, colon and leukocytes with the uppermost expression in testis.

    • Synonyms

      C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.

    • 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 MGSMKKEHVL HCQFSAWYPF FRGVTIKSVI LPLPQNVKDY LLDDGTLVVS GRDDPPTHSQ PDSDDEAEEI QWSDDENTAT LTAPEFPEFA TKVQEAINSL GGSVFPKLNW SAPRDAYWIA MNSSLKCKTL SDIFLLFKSS DFITRDFTQP FIHCTDDSPD PCIEYELVLR KWCELIPGAE FRCFVKENKL IGISQRDYTQ YYDHISKQKE EIRRCIQDFF KKHIQYKFLD EDFVFDIYRD SRGKVWLIDF NPFGEVTDSL LFTWEELISE NNLNGDFSEV DAQEQDSPAF RCTNSEVTVQ PSPYLSYRLP KDFVDLSTGE DAHKLIDFLK LKRNQQEDD

    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.

    Cdc123 Human
  • View Data Sheet

    Name :

    CDK1 Human

    Description:

    Cyclin-Dependent Kinase 1 Human Recombinant

    Cyclin-Dependent Kinase 1, CDC2, Cell Division Cycle 2, G1 To S And G2 To M, Cell Division Control Protein 2 Homolog, Cell Division Protein Kinase 1, P34 Protein Kinase, P34CDC2, CDC28A, Cell Cycle Controller CDC2, EC 2.7.11.22, EC 2.7.11.23, CDKN1, Cyclin-dependent kinase 1, CDK1.

    Product # :

    PKA-076

    Price :

    Quantity :

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    Description

    CDK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (1-297 a.a) and having a molecular mass of 36.2kDa. CDK1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CDK1 protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cyclin-dependent kinase 1 (CDK1) plays a significant part in the control of the eukaryotic cell cycle through modulating the centrosome cycle in addition to mitotic onset; CDK1 promotes G2-M transition and regulates G1 progress and G1-S transition using association with multiple interphase cyclins. CDK1 is essential in higher cells for the entry into S-phase and mitosis.

    • Synonyms

      Cyclin-Dependent Kinase 1, CDC2, Cell Division Cycle 2, G1 To S And G2 To M, Cell Division Control Protein 2 Homolog, Cell Division Protein Kinase 1, P34 Protein Kinase, P34CDC2, CDC28A, Cell Cycle Controller CDC2, EC 2.7.11.22, EC 2.7.11.23, CDKN1, Cyclin-dependent kinase 1, CDK1.

    • 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 MEDYTKIEKI GEGTYGVVYK GRHKTTGQVV AMKKIRLESE EEGVPSTAIR EISLLKELRH PNIVSLQDVL MQDSRLYLIF EFLSMDLKKY LDSIPPGQYM DSSLVKSYLY QILQGIVFCH SRRVLHRDLK PQNLLIDDKG TIKLADFGLA RAFGIPIRVY THEVVTLWYR SPEVLLGSAR YSTPVDIWSI GTIFAELATK KPLFHGDSEI DQLFRIFRAL GTPNNEVWPE VESLQDYKNT FPKWKPGSLA SHVKNLDENG LDLLSKMLIY DPAKRISGKM ALNHPYFNDL DNQIKKM.

    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.

    Cdk1 Human
  • View Data Sheet

    Name :

    CFP Human

    Description:

    Complement Factor Properdin Human Recombinant

    Properdin, Complement factor P, CFP, PFC, Complement factor properdin, BFD, PFD, PROPERDIN.

    Product # :

    PRO-2011

    Price :

    Quantity :

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    Description

    CFP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 465 amino acids (28-469 a.a.) and having a molecular mass of 50.9kDa.CFP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement Factor Properdin (CFP) which is a plasma glycoprotein, is a positive regulator of the alternative complement pathway of the innate immune system. CFP binds and stabilizes the C3- and C5-convertase enzyme complexes in a feedback loop that eventually ends with formation of the membrane attack complex and lysis of the target cell. Mutations in CFP lead to 2 forms of properdin deficiency that cause high susceptibility to meningococcal infections.

    • Synonyms

      Properdin, Complement factor P, CFP, PFC, Complement factor properdin, BFD, PFD, PROPERDIN.

    • 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 MGSDPVLCFT QYEESSGKCK GLLGGGVSVE DCCLNTAFAY QKRSGGLCQP CRSPRWSLWS TWAPCSVTCS EGSQLRYRRC VGWNGQCSGK VAPGTLEWQL QACEDQQCCP EMGGWSGWGP WEPCSVTCSK GTRTRRRACN HPAPKCGGHC PGQAQESEAC DTQQVCPTHG AWATWGPWTP CSASCHGGPH EPKETRSRKC SAPEPSQKPP GKPCPGLAYE QRRCTGLPPC PVAGGWGPWG PVSPCPVTCG LGQTMEQRTC NHPVPQHGGP FCAGDATRTH ICNTAVPCPV DGEWDSWGEW SPCIRRNMKS ISCQEIPGQQ SRGRTCRGRK FDGHRCAGQQ QDIRHCYSIQ HCPLKGSWSE WSTWGLCMPP CGPNPTRARQ RLCTPLLPKY PPTVSMVEGQ GEKNVTFWGR PLPRCEELQG QKLVVEEKRP CLHVPACKDP EEEEL.

    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.

    Cfp Human
  • View Data Sheet

    Name :

    UBE2I Human His

    Description:

    Ubiquitin-Conjugating Enzyme E2I Human Recombinant, His Tag

    SUMO-conjugating enzyme UBC9, EC 6.3.2.-, SUMO-protein ligase, Ubiquitin-conjugating enzyme E2 I, Ubiquitin-protein ligase I, Ubiquitin carrier protein I, Ubiquitin carrier protein 9, p18, UBC9, C358B7.1.

    Product # :

    ENZ-274

    Price :

    Quantity :

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    Description

    Ubiquitin-Conjugating Enzyme E2I Human Recombinant produced in E.coli is a 19.5 kDa protein containing 171 amino acids.The UBE2I protein contains 6xHis tag and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated (1mg/ml) solution in 1X PBS and 1mM DTT, pH 7.5.

    Purity

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

    More Info

    • Introduction

      Human Ubquitin Conjugating Enzyme 9 (Ubc9) is a member of the E2 family and is specific for the conjugation of SUMO to a variety of target proteins. SUMO conjugation to target proteins is mediated by a different, but analogous, pathway to ubiquitinylation. This E2 is unusual in that it interacts directly with protein substrates that are modified by sumolyation, and may play a role in substrate recognition. Ubc9 can mediate the conjugation of SUMO-1 to a variety of proteins including RanGAP1, I?B?, and PML without the requirement of an E3 ligase.

    • Synonyms

      SUMO-conjugating enzyme UBC9, EC 6.3.2.-, SUMO-protein ligase, Ubiquitin-conjugating enzyme E2 I, Ubiquitin-protein ligase I, Ubiquitin carrier protein I, Ubiquitin carrier protein 9, p18, UBC9, C358B7.1.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized UBE2I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution UBE2I 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 UBE2I in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHHHHHHAMGTLNMSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGT
      MNLMNWECAIPGKKGTPWEGGLFKLRMLFKDDYPSSPPKCKFEPPLFH
      PNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTI
      YCQNRVEYEKRVRAQAKKFAPS.

    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.

    Ube2I Human His
  • View Data Sheet

    Name :

    CXCL3 Human

    Description:

    GRO-Gamma Human Recombinant (CXCL3)

    Macrophage inflammatory protein 2-beta, MIP2-beta, CXCL3, Growth-regulated protein gamma, GRO-gamma, GRO-gamma(1-73), GRO3, GROg, MIP2B, SCYB3, MIP-2b, CINC-2b, MGSA gamma.

    Product # :

    CHM-310

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    Description

    GRO-Gamma Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7902 Dalton. The CXCL3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized with no additives.

    Purity

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

    Biological Activity

    The Biological activity is calculated by its ability to chemoattract CXCR2 transfected 293 cells using 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.

    • Synonyms

      Macrophage inflammatory protein 2-beta, MIP2-beta, CXCL3, Growth-regulated protein gamma, GRO-gamma, GRO-gamma(1-73), GRO3, GROg, MIP2B, SCYB3, MIP-2b, CINC-2b, MGSA gamma.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GRO-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL3 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 CXCL3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Val-Thr.

    • Background

      What is the molecular weight/Mw of CXCL3 HUMAN Protein?
      CXCL3 HUMAN Protein has a total Mw of 7.9kDa.

      What is the source or expression system of CXCL3 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL3 HUMAN Protein?
      CXCL3 HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL3 HUMAN Protein?
      The Biological activity is calculated by its ability to chemoattract CXCR2 transfected 293 cells using 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CXCL3 HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Val-Thr.

      What applications can CXCL3 HUMAN Protein be used in?
      CXCL3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL3 HUMAN Protein?
      The endotoxin level is minimal, CXCL3 HUMAN Protein was purified using conventional chromatography techniques.


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

    Gro Gamma Human
  • View Data Sheet

    Name :

    CXCL3 Mouse, His

    Description:

    GRO-Gamma Mouse Recombinant (CXCL3), His Tag

    C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960, GRO-g.

    Product # :

    CHM-283

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    Description

    GRO-g Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 98 amino acids (28-100 a.a.) and having a molecular mass of 10.6kDa.CXCL3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GRO-gamma protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.15M NaCl and 5mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.

    • Synonyms

      C-X-C motif chemokine 3, Dendritic cell inflammatory protein 1, Cxcl3, Dcip1, Gm1960, GRO-g.

    • 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 MGSHMAVVAS ELRCQCLNTL PRVDFETIQS LTVTPPGPHC TQTEVIATLK DGQEVCLNPQ GPRLQIIIKK ILKSGKSS.

    • Background

      What is the molecular weight/Mw of CXCL3 MOUSE, HIS Protein?
      CXCL3 MOUSE, HIS Protein has a total Mw of 10.6kDa.

      What is the source or expression system of CXCL3 MOUSE, HIS Protein?
      Escherichia Coli.

      What is the Purity of CXCL3 MOUSE, HIS Protein?
      CXCL3 MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL3 MOUSE, HIS Protein?
      The biological functionality of CXCL3 MOUSE, HIS Protein will be determined in the future.

      What is the amino acid sequence of CXCL3 MOUSE, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHMAVVAS ELRCQCLNTL PRVDFETIQS LTVTPPGPHC TQTEVIATLK DGQEVCLNPQ GPRLQIIIKK ILKSGKSS.

      What applications can CXCL3 MOUSE, HIS Protein be used in?
      CXCL3 MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL3 MOUSE, HIS Protein?
      The endotoxin level is minimal, CXCL3 MOUSE, HIS Protein was purified using conventional chromatography techniques.


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    Gro G Mouse His
  • View Data Sheet

    Name :

    LYN Human

    Description:

    v-yes-1 Yamaguchi Sarcoma Viral Related Oncogene Human Recombinant

    Tyrosine-protein kinase Lyn, Lck/Yes-related novel protein tyrosine kinase, V-yes-1 Yamaguchi sarcoma viral related oncogene homolog, p53Lyn, p56Lyn, JTK8, EC 2.7.10, LYN Proto-Oncogene, Src Family Tyrosine Kinase, V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog, Lck/Yes-Related Novel Protein Tyrosine Kinase, EC 2.7.10.2.

    Product # :

    PRO-136

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    Description

    LYN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 535 amino acids (1-512) and having a molecular mass of 61.0kDa. LYN is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The LYN solution (1mg/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

      Tyrosine-protein kinase Lyn (LYN) belongs to the src family of non-receptor protein tyrosine kinases, which is primarily expressed in haematopoietic tissues. LYN protein is involved in induction of stress-activated protein kinase (SAPK), but not ERK or p38 MAPK, in response to genotoxic agents. LYN protein stimulates SAPK by a MKK7- and MEKK1-dependent mechanism. The LYN - MEKK1 - MKK7 - SAPK pathway is efficient in the induction of apoptosis by genotoxic agents.

    • Synonyms

      Tyrosine-protein kinase Lyn, Lck/Yes-related novel protein tyrosine kinase, V-yes-1 Yamaguchi sarcoma viral related oncogene homolog, p53Lyn, p56Lyn, JTK8, EC 2.7.10, LYN Proto-Oncogene, Src Family Tyrosine Kinase, V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog, Lck/Yes-Related Novel Protein Tyrosine Kinase, EC 2.7.10.2.

    • 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 MGSMGCIKSK GKDSLSDDGV DLKTQPVRNT ERTIYVRDPT SNKQQRPVPE SQLLPGQRFQ TKDPEEQGDI VVALYPYDGI HPDDLSFKKG EKMKVLEEHG EWWKAKSLLT KKEGFIPSNY VAKLNTLETE EWFFKDITRK DAERQLLAPG NSAGAFLIRE SETLKGSFSL SVRDFDPVHG DVIKHYKIRS LDNGGYYISP RITFPCISDM IKHYQKQADG LCRRLEKACI SPKPQKPWDK DAWEIPRESI KLVKRLGAGQ FGEVWMGYYN NSTKVAVKTL KPGTMSVQAF LEEANLMKTL QHDKLVRLYA VVTREEPIYI ITEYMAKGSL LDFLKSDEGG KVLLPKLIDF SAQIAEGMAY IERKNYIHRD LRAANVLVSE SLMCKIADFG LARVIEDNEY TAREGAKFPI KWTAPEAINF GCFTIKSDVW SFGILLYEIV TYGKIPYPGR TNADVMTALS QGYRMPRVEN CPDELYDIMK MCWKEKAEER PTFDYLQSVL DDFYTATEGQ YQQQP.

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    Lyn Human
  • View Data Sheet

    Name :

    VAMP3 Human

    Description:

    Synaptobrevin-3 Human Recombinant

    VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.

    Product # :

    PRO-652

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    Description

    VAMP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    The VAMP3 protein solution contains 20mM Tris pH-7.5 and 10% glycerol.

    Purity

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

    More Info

    • Introduction

      VAMP3 is present in recycling endosomes and endosome-derived vesicles. VAMP3 has been implicated in recycling of transferrin receptors to the plasma membrane, secretion of alpha-granules in platelets, recycling of T-cell receptors to the immunological synapses, and membrane trafficking during cell migration. VAMP-3 is present in human platelets and necessary for granule secretion. Synaptobrevins are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. VAMP3 high homology to other VAMPs in its broad tissue distribution and subcellular localization is shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.

    • Synonyms

      VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.

    • 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

      MSTGPTAATG SNRRLQQTQN QVDEVVDIMR VNVDKVLERD QKLSELDDRA DALQAGASQF ETSAAKLKRK YWWKNCK.

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    Vamp3 Human
  • View Data Sheet

    Name :

    CNN2 Human

    Description:

    Calponin 2 Human Recombinant

    Calponin 2, Calponin H2, Smooth Muscle, Neutral Calponin, calponin-2.

    Product # :

    PRO-1882

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    Description

    CNN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids (1-131 a.a) and having a molecular mass of 16.9kDa.CNN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CNN2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calponin 2 also known as CNN2 protein is capable of binding actin, calmodulin, troponin C, and tropomyosin, and also function in the structural organization of actin filaments. Furthermore, the interaction of CNN2 with actin inhibits the actomyosin Mg-ATPase activity. CNN2 takes part in smooth muscle contraction and cell adhesion. Two transcript variants encoding different isoforms have been found for this gene.

    • Synonyms

      Calponin 2, Calponin H2, Smooth Muscle, Neutral Calponin, calponin-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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSSTQFN KGPSYGLSAE VKNRLLSKYD PQKEAELRTW IEGLTGLSIG PDFQKGLKDG TILCTLMNKL QPGSVPKINR SMQNWHQLEN LSNFIKAMVS YGMNPVDLFE ANDLFESGNM TQVQVSLLAL AGKA

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    Cnn2 Human
  • View Data Sheet

    Name :

    RAET1E Human

    Description:

    Retinoic Acid Early Transcript 1E Human Recombinant

    bA350J20.7, LETAL, N2DL-4, NKG2DL4, RAET1E2, RL-4, ULBP4, NKG2D ligand 4, Retinoic acid early transcript 1E, RAE-1-like transcript 4, Lymphocyte effector toxicity activation ligand, UNQ1867/PRO4303.

    Product # :

    PRO-1293

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    Description

    RAET1E Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (31-225 a.a.) and having a molecular mass of 24.9kDa.RAET1E is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RAET1E 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.

    More Info

    • Introduction

      RAET1E is a member of the MHC class I family. MHC class I family contains main histocompatibility complex (MHC) class I-related genes positioned in a cluster on chromosome 6q24.2-q25.3. RAET1E and RAET1G protein are different from other RAET1 proteins since they have type I membrane-spanning sequences at their C termini instead glycosylphosphatidylinositol anchor sequences.RAET1E acts as a ligand for NKG2D receptor, expressed on the surface of numerous types of immune cells, involves in innate adaptive immune reactions.RAET1E delivers signals to NK cells and advances tumor immune surveillance by inducing the growth of anti-tumor cytotoxic lymphocyte.

    • Synonyms

      bA350J20.7, LETAL, N2DL-4, NKG2DL4, RAET1E2, RL-4, ULBP4, NKG2D ligand 4, Retinoic acid early transcript 1E, RAE-1-like transcript 4, Lymphocyte effector toxicity activation ligand, UNQ1867/PRO4303.

    • 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 MGSMHSLCFN FTIKSLSRPG QPWCEAQVFL NKNLFLQYNS DNNMVKPLGL LGKKVYATST WGELTQTLGE VGRDLRMLLC DIKPQIKTSD PSTLQVEMFC QREAERCTGA SWQFATNGEK SLLFDAMNMT WTVINHEASK IKETWKKDRG LEKYFRKLSK GDCDHWLREF LGHWEAMPEP TVSPVNASDI HWSSSSLPD.

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    Raet1E Human
  • View Data Sheet

    Name :

    CPLX1 Human

    Description:

    Complexin-1 Human Recombinant

    CPLX-1, CPXI, CPX-I, CPX1, CPX-1, Synaphin2, Synaphin-2, Complexin-1, Complexin I, CPX I, CPLX1.

    Product # :

    PRO-645

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    Description

    CPLX1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids (1-134 a.a) and having a molecular mass of 17.1kDa (molecular weight on SDS-PAGE will appear higher).The CPLX1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CPLX1protein solution contains 20mM Tris-HCl pH-8 and 10% glycerol.

    Purity

    Greater than 90% by SDS-PAGE.

    More Info

    • Introduction

      CPLX1 is part of the SNARE family complex binding proteins that are catalysts or inhibitors of vesicle exocytosis. CPLX1 shows reduced Ca2+-triggered fast neurotransmitter release at hippocampal glutamatergic synapses, indicating that CPLX1 is a positive regulator of transmitter release. In contrast, CPLX1 inhibits SNARE-mediated liposome and cell fusions in vitro, that result in hypothesis thus acts as a fusion clamp of synaptic exocytosis. CPLX1 regulates a late step in synaptic vesicle exocytosis.

    • Synonyms

      CPLX-1, CPXI, CPX-I, CPX1, CPX-1, Synaphin2, Synaphin-2, Complexin-1, Complexin I, CPX I, CPLX1.

    • 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 MEFVMKQALG GATKDMGKML GGDEEKDPDA AKKEEERQEA LRQAEEERKA KYAKMEAERE AVRQGIRDKYGIKKKEEREA EAQAAMEANS EGSLTRPKKA IPPGCGDEVE EEDESILDTV IKYLPGPLQD MLKK.

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    Cplx1 Human
  • View Data Sheet

    Name :

    YWHAB Human

    Description:

    Tyr-3/Trp- 5 Monooxygenase Activation Protein Beta Human Recombinant

    14-3-3 protein beta/alpha, Protein kinase C inhibitor protein 1, Protein 1054, YWHAB, HS1, GW128, KCIP-1, Tyr-3/Trp- 5 Monooxygenase Activation Protein Beta, 14-3-3 Beta.

    Product # :

    PKA-348

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    Description

    YWHAB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 246 amino acids (1-246) and having a molecular mass of 28kDa. YWHAB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The YWHAB protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM EDTA & 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      YWHAB belongs to the 14-3-3 family of proteins which are in charge for signal transduction by binding to phosphoserine-containing proteins. YWHAB is found in both plants and mammals. YWHAB protein interacts with RAF1 and CDC25 phosphatases,thus linking mitogenic signaling and the cell cycle machinery. YWHAB is an adapter protein involved in the regulation of a large spectrum of both general and specialized signaling pathway. YWHAB binds to a large number of proteins by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.

    • Synonyms

      14-3-3 protein beta/alpha, Protein kinase C inhibitor protein 1, Protein 1054, YWHAB, HS1, GW128, KCIP-1, Tyr-3/Trp- 5 Monooxygenase Activation Protein Beta, 14-3-3 Beta.

    • 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

      MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL ELLDKYLIPN ATQPESKVFY LKMKGDYFRY LSEVASGDNK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD
      AGEGEN.

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    Ywhab Human
  • View Data Sheet

    Name :

    SIGLEC10 Human

    Description:

    Sialic Acid Binding Ig Like Lectin 10 Human Recombinant

    SIGLEC10, PRO940, SLG2, SIGLEC-10, Sialic acid-binding Ig-like lectin 10 isoform 3, Siglec-like protein 2.

    Product # :

    PRO-2610

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    Description

    SIGLEC10 Human produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 678 amino acids (17-455 a.a.) and having a molecular mass of 75.6kDa. SIGLEC10 is expressed with a 239 hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The SIGLEC10 solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sialic Acid Binding Ig Like Lectin 10(SIGLEC10) is a part of the immunoglobulin superfamily that is expressed on eosinophils, B cells, monocytes and neutrophils. SIGLEC10 is an adhesion molecule that mediates sialic-acid dependent binding to cells.SIGLEC10 is a ligand for CD52, the target of the therapeutic monoclonal antibody Alemtuzumab. Also, it binds to Vascular adhesion protein 1 (VAP-1) and to the co-stimulatory molecule CD24.This binding is modulated by cis interactions of SIGLEC10 with sialated molecules on the same cell.

    • Synonyms

      SIGLEC10, PRO940, SLG2, SIGLEC-10, Sialic acid-binding Ig-like lectin 10 isoform 3, Siglec-like protein 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

      MDGRFWIRVQ ESVMVPEGLC ISVPCSFSYP RQDWTGSTPA YGYWFKAVTE TTKGAPVATN
      HQSREVEMST RGRFQLTGDP AKGNCSLVIR DAQMQDESQY FFRVERGSYV RYNFMNDGFF
      LKVTALTQKP DVYIPETLEP GQPVTVICVF NWAFEECPPP SFSWTGAALS SQGTKPTTSH
      FSVLSFTPRP QDHNTDLTCH VDFSRKGVSA QRTVRLRVAY APRDLVISIS RDNTPALEPQ
      PQGNVPYLEA QKGQFLRLLC AADSQPPATL SWVLQNRVLS SSHPWGPRPL GLELPGVKAG
      DSGRYTCRAE NRLGSQQRAL DLSVQYPPEN LRVMVSQANR TVLENLGNGT SLPVLEGQSL
      CLVCVTHSSP PARLSWTQRG QVLSPSQPSD PGVLELPRVQ VEHEGEFTCH ARHPLGSQHV
      SLSLSVHYKK GLISTAFSNL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR
      TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN
      GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS
      DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH.

    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.

    Siglec10 Human
  • View Data Sheet

    Name :

    CTRB1 Human

    Description:

    Chymotrypsinogen-B1, Human Recombinant

    Product # :

    ENZ-1016

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    Description

    Recombinant Human CTRB1 expressed in E.coli containing 245 amino acids having a Mw of 27kDa is purified by standard chromatography techniques.

    Source

    E.coli

    Formulation

    The Human CTRB1 was lyophilized without any additives.

    Purity

    Greater than 95% as determined by HPLC.

    Biological Activity

    1100 units/mg protein.
    One unit is defined as the amount of enzyme that will hydrolyze 1.0 μmole of N-alpha-acetyl-L-tyrosine ethyl ester (ATEE) per min at pH 7.0 at 25°C.

    More Info

    • Introduction

      Chymotrypsinogen-B1 (CTRB1) belongs to the serine protease family of enzymes and forms a main precursor of the pancreatic proteolytic enzymes. CTRB1 is located next to a related chymotrypsinogen gene. CTRB1 is a protein coding gene which encodes different isoforms which may undergo similar processing to generate the mature protein.

    • Physical Appearance

      Sterile Filtered lyophilized powder.

    • Stability

      Recombinant Human CTRB1 although stable at room temp for 1 week, should be stored desiccated 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 Human CTRB1 in 1ml 50mM HAc which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      CG VPAIHPVLSG LSRIVNGEDA VPGSWPWQVS LQDKTGFHFC GGSLISEDWV VTAAHCGVRT SDVVVAGEFD QGSDEENIQV LKIAKVFKNP KFSILTVNND ITLLKLATPA RFSQTVSAVC LPSADDDFPAGTLCATTGWG KTKYNANKTP DKLQQAALPL LSNAECKKSW GRRITDVMIC AGASGVSSCM GDSGGPLVCQ KDGAWTLVGI VSWGSDTCST SSPGVYARVTKLIPWVQKIL AAN.

    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.

    Ctrb1 Human
  • View Data Sheet

    Name :

    CXCL8 Human, GST

    Description:

    Interleukin-8 (1-72) (CXCL8) Human Recombinant, GST Tag

    Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8

    Product # :

    CHM-047

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    Description

    Recombinant Human Interleukin-8 produced in E. coli containing 72 amino acids.Recombinant Human Interleukin-8 is fused to GST tag at its N-terminus and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    IL8 GST solution contains 25mM Tris-Base/ 25mM K2CO3.

    Purity

    Protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.

    • Synonyms

      Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8

    • 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.

    • Applications

      Immunoassay.

    • Background

      What is the source or expression system of CXCL8 HUMAN, GST Protein?
      Escherichia Coli.

      What is the Purity of CXCL8 HUMAN, GST Protein?
      CXCL8 HUMAN, GST Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL8 HUMAN, GST Protein?
      The biological functionality of CXCL8 HUMAN, GST Protein will be determined in the future.

      What is the amino acid sequence of CXCL8 HUMAN, GST Protein?
      CXCL8 HUMAN, GST Protein is composed from 72 amino acids.

      What applications can CXCL8 HUMAN, GST Protein be used in?
      CXCL8 HUMAN, GST Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL8 HUMAN, GST Protein?
      The endotoxin level is minimal, CXCL8 HUMAN, GST 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.

    Il 8 Human
  • View Data Sheet

    Name :

    G CSF Human

    Description:

    Granulocyte-Colony Stimulating Factor Human Recombinant

    CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Lenograstim, G-CSF, MGC45931, GCSF.

    Product # :

    CYT-220

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    Description

    Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8 KD.GCSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GCSF was lyophilized after extensive dialysis against 10mM sodium acetate buffer pH= 4.

    Purity

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

    Biological Activity

    The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml, corresponding to a Specific Activity of 100,000,000 IU/mg.

    More Info

    • Introduction

      GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.

    • Synonyms

      CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Lenograstim, G-CSF, MGC45931, GCSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GCSF 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 GCSF in sterile 20mM AcOH not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids of GCSF was determined and was found to be Met-Thr-Pro-Leu-Gly.

    • Background

      What is the molecular weight/Mw of GDF15 HUMAN, HIS Protein?
      GDF15 HUMAN, HIS Protein has a total Mw of 18.8kDa.

      What is the source or expression system of GDF15 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of GDF15 HUMAN, HIS Protein?
      GDF15 HUMAN, HIS Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF15 HUMAN, HIS Protein?
      The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml, corresponding to a Specific Activity of 100,000,000 IU/mg.

      What is the amino acid sequence of GDF15 HUMAN, HIS Protein?
      GDF15 HUMAN, HIS Protein is composed from 175 amino acids.

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

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

    • Protein content

      GCSF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.815 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of GCSF as a Reference Standard.

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

    G Csf Human
  • View Data Sheet

    Name :

    M CSF Human

    Description:

    Macrophage-Colony Stimulating Factor Human Recombinant

    Macrophage Colony Stimulating Factor, CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

    Product # :

    CYT-308

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    Description

    Macrophage Colony Stimulating Factor Human Recombinant produced in E.coli is a disulfide linked homodimer, non-glycosylated, polypeptide chain containing 2 x 159 amino acids and having a total molecular mass of 37.1 KD. MCSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MCSF protein was lyophilized with 10mM sodium Phosphate, pH-8.0 & 50mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, calculated by the dose-dependent stimulation of the proliferation of murine M-NFS-60 indicator cells was found to be 1.15ng/ml corresponding to a specific activity of 8.7x105 Units/mg.

    More Info

    • Introduction

      Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. MCSF induces cells of the monocyte/macrophage lineage. MCSF plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.

    • Synonyms

      Macrophage Colony Stimulating Factor, CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MEEVSEYCSH MIGSGHLQSL QRLIDSQMET SCQITFEFVD QEQLKDPVCY LKKAFLLVQD IMEDTMRFRD NTPNAIAIVQ LQELSLRLKS CFTKDYEEHD KACVRTFYET PLQLLEKVKN VFNETKNLLD KDWNIFSKNC NNSFAECSSQ GHERQSEGS.

    • Background

      M-CSF (Macrophage-Colony Stimulating Factor) Human Recombinant: Unraveling Its Role in Macrophage Biology and Beyond

      Abstract:

      M-CSF (Macrophage-Colony Stimulating Factor), also known as Lanimostim, MCSF, or MGC31930, is a crucial growth factor that regulates the development, proliferation, and function of macrophages.

      This research paper aims to provide a comprehensive analysis of the molecular characteristics, signaling pathways, and diverse physiological functions of M-CSF. Additionally, it explores the therapeutic implications of M-CSF in various diseases and disorders.

      Synonyms such as Lanimostim, MCSF, and MGC31930 associated with the protein are discussed throughout the paper to highlight their relevance in scientific literature.

      Introduction:

      1. M-CSF, also known as Lanimostim, MCSF, or MGC31930, is a growth factor that plays a critical role in the regulation of macrophage biology. This section introduces M-CSF and its synonyms, highlighting their significance and relevance in scientific research.

      Molecular Characteristics of M-CSF:

      1. This section explores the molecular characteristics of M-CSF, including its primary amino acid sequence, protein structure, and post-translational modifications. The importance of these factors in determining M-CSF's biological activity and receptor binding is discussed.

      Signaling Pathways Activated by M-CSF:

      1. M-CSF activates specific signaling pathways upon binding to its receptor, leading to diverse cellular responses. This section focuses on the activation of the MAPK/ERK and PI3K/Akt pathways. The downstream effectors and transcriptional regulators involved in mediating M-CSF's cellular responses are also discussed.

      Physiological Functions of M-CSF:

      1. M-CSF plays critical roles in various physiological processes, particularly in macrophage development, survival, polarization, and immune regulation. This section provides an in-depth analysis of M-CSF's contributions to these processes, emphasizing its role in hematopoiesis, tissue homeostasis, wound healing, and host defense.

      Therapeutic Implications of M-CSF:

      1. The unique properties of M-CSF make it a promising therapeutic candidate for various diseases and disorders. This section discusses the potential applications of M-CSF in immunotherapy, tissue regeneration, cancer treatment, and autoimmune diseases. The challenges and future directions in utilizing M-CSF as a therapeutic agent are also explored.

      M-CSF in Disease Pathogenesis:

      1. M-CSF dysregulation is implicated in the pathogenesis of several diseases, including cancer, inflammation, and bone disorders. This section examines the role of M-CSF in promoting tumor progression, macrophage-mediated inflammation, osteoclast differentiation, and metabolic diseases. The therapeutic implications and targeting of M-CSF in disease management are also discussed.

      Conclusion:

      1. M-CSF, also known as Lanimostim, MCSF, or MGC31930, is a critical growth factor involved in macrophage biology and disease pathogenesis. Understanding the molecular characteristics, signaling pathways, and physiological functions of M-CSF contributes to the exploration of its therapeutic potential in various disorders.

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    M Csf Human
  • View Data Sheet

    Name :

    BNP Protein

    Description:

    B-type Natriuretic Peptide Human Recombinant

    NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

    Product # :

    CYT-327

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    Description

    B-type Natriuretic Peptide Recombinant Human produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 32 amino acids and having a molecular mass of 3,500 Dalton. NPPB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Natriuretic Peptide Precursor B was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    More Info

    • Introduction

      Natriuretic Peptide Precursor B acts as a cardiac hormone with a variety of biological actions including natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. It is thought to play a key role in cardiovascular homeostasis. Helps restore the body's salt and water balance. Improves heart function.

    • Synonyms

      NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.

    • Background

      What is the molecular weight / Mw of BNP Protein?
      BNP Protein has a total Mw of 3.5kDa.

      What is the source or expression system of BNP Protein?

      Escherichia Coli.

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

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

      What is the amino acid sequence of BNP Protein?

      SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.

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

      What is the endotoxin level for BNP Protein?

      The endotoxin level is minimal, BNP 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.

    Nppb Human Recombinant
  • View Data Sheet

    Name :

    SIGLEC5 Human

    Description:

    Sialic Acid Binding Ig Like Lectin 5 Human Recombinant

    Sialic Acid Binding Ig Like Lectin 5, Obesity-Binding Protein 2, OB-Binding Protein 2, CD33 Antigen-Like 2, SIGLEC-5, CD33L2, OB-BP2, OBBP2, Sialic Acid-Binding Immunoglobulin-Like Lectin 5, Sialic Acid Binding Ig-Like Lectin 5, Sialic Acid-Binding Ig-Like Lectin 5, CD170 Antigen, CD170, Sialic acid-binding Ig-like lectin 5, Siglec-5, CD33 antigen-like 2, Obesity-binding protein 2, OB-BP2, OB-binding protein 2, CD170.

    Product # :

    PRO-2432

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    Description

    SIGLEC5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 667 amino acids (17-441a.a.) and having a molecular mass of 74.2kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). SIGLEC5 is expressed with a 239 amino acid hIgG-His Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SIGLEC5 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sialic Acid Binding Ig Like Lectin 5, also known as SIGLEC5 is a member of the immunoglobulin superfamily and SIGLEC family. SIGLEC5 contains of 2 Ig-like C2-type domains and 1 Ig-like V-type domain. In addition, SIGLEC5 is expressed by monocytic/myeloid lineage cells. SIGLEC5 is expressed at high levels in peripheral blood leukocytes, spleen, and at lower levels in lymph node, appendix, pancreas, lung, and thymus.

    • Synonyms

      Sialic Acid Binding Ig Like Lectin 5, Obesity-Binding Protein 2, OB-Binding Protein 2, CD33 Antigen-Like 2, SIGLEC-5, CD33L2, OB-BP2, OBBP2, Sialic Acid-Binding Immunoglobulin-Like Lectin 5, Sialic Acid Binding Ig-Like Lectin 5, Sialic Acid-Binding Ig-Like Lectin 5, CD170 Antigen, CD170, Sialic acid-binding Ig-like lectin 5, Siglec-5, CD33 antigen-like 2, Obesity-binding protein 2, OB-BP2, OB-binding protein 2, CD170.

    • 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

      ADLEKPVYEL QVQKSVTVQE GLCVLVPCSF SYPWRSWYSS PPLYVYWFRD GEIPYYAEVV ATNNPDRRVK PETQGRFRLL GDVQKKNCSL SIGDARMEDT GSYFFRVERG RDVKYSYQQN KLNLEVTALI EKPDIHFLEP LESGRPTRLS CSLPGSCEAG PPLTFSWTGN ALSPLDPETT RSSELTLTPR PEDHGTNLTC QMKRQGAQVT TERTVQLNVS YAPQTITIFR NGIALEILQN TSYLPVLEGQ ALRLLCDAPS NPPAHLSWFQ GSPALNATPI SNTGILELRR VRSAEEGGFT CRAQHPLGFL QIFLNLSVYS LPQLLGPSCS WEAEGLHCRC SFRARPAPSL CWRLEEKPLE GNSSQGSFKV NSSSAGPWAN SSLILHGGLS SDLKVSCKAW NIYGSQSGSV LLLQGRSNLG TGVVPAALLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

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    Siglec5 Human
  • View Data Sheet

    Name :

    Cyclosporin A

    Description:

    Cyclosporin-A

    Product # :

    PRO-408

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    Description

    Cyclosporin is a cyclic polypeptide immunosuppressant agent consisting of 11 amino acids and having a molecular weight of 1202.64. It is produced as a metabolite by the fungus species Beauveria nlyea. Chemically, cyclosporin is designated as [R-[R*,R*-(E)]]-cyclic(L-alanyl-D- alanyl-N-methyl-L-leucyl-N-methyl-L-leucyl-N-methyl-L-valyl-3-hydroxy-N, 4-dimethyl-L-2-amino-6-octenoyl-L-a-amino-butyryl- N-methylglycyl-N- methyl-L-leucyl-L-valyl-N-methyl-L-leucyl). Molecular Formula: C62H111N11O12.

    Source

    Beauveria Nivea.

    Formulation

    The Cyclosporin-A was lyophilized from a concentrated (1mg/ml) solution with no additives.

    Purity

    Greater than 99.0% as determined by RP-HPLC.

    More Info

    • Introduction

      Cyclosporin A is a noncytotoxic, natural, 11 amino acid cyclic peptide used clinically as an immunosuppressant for the treatment of autoimmune and inflammatory disorders and to prevent organ rejection after transplantation. Cyclosporin acts chiefly by inhibiting T lymphocyte function, which is vital for the propagation of inflammation. Cyclosporin A does not suppress the activity of other hematopoietic cells, does not cause bone marrow suppression and has a rapid onset of action as opposed to other immunosuppressive agents. Nevertheless, Cyclosporin A -induced nephrotoxicity remains an important clinical problem, and oxidative stress has been implicated as a potential responsible mechanism.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Cyclosporin A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Cyclosporin A 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 Cyclosporin-A in anhydrous ethanol R at a concentration of 50mg/ml.

    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.

    Cyclosporin A
  • View Data Sheet

    Name :

    BLOC1S5 Human

    Description:

    Biogenesis of Lysosomal Organelles Complex-1, Subunit 5 Human Recombinant

    Biogenesis of lysosome-related organelles complex 1 subunit 5, BLOC-1 subunit 5, Protein Muted homolog, BLOC1S5, MUTED.

    Product # :

    PRO-1155

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    Description

    BLOC1S5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-187 a.a) and having a molecular mass of 24kDa.BLOC1S5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BLOC1S5 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 40% glycerol, 2mM DTT, 0.1mM PMSF and 1mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Muted homolog (MUTED) is a component of the BLOC-1 complex, a complex which is necessary for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. The BLOC-1 complex is needed to steer membrane protein cargos into vesicles assembled at cell bodies for release into neurites and nerve terminals. In addition, this complex, along with SNARE proteins, is suggested to be involved in neurite extension. MUTED also interacts with pallidin, dystrobrevin binding protein 1 and CNO/cappuccino. MUTED is ubiquitously expressed with higher levels in the brain, bone marrow, kidney, and liver and lower levels in the skeletal muscle.

    • Synonyms

      Biogenesis of lysosome-related organelles complex 1 subunit 5, BLOC-1 subunit 5, Protein Muted homolog, BLOC1S5, MUTED.

    • 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 MGSMSGGGTE TPVGCEAAPG GGSKKRDSLG TAGSAHLIIK DLGEIHSRLL DHRPVIQGET RYFVKEFEEK RGLREMRVLE NLKNMIHETN EHTLPKCRDT MRDSLSQVLQ RLQAANDSVC RLQQREQERK KIHSDHLVAS EKQHMLQWDN FMKEQPNKRA EVDEEHRKAM ERLKEQYAEM EKDLAKFSTF.

    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.

    Muted Human
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    Name :

    CDKN2AIPNL Human

    Description:

    CDKN2A Interacting Protein N-Terminal Like Human Recombinant

    CDKN2AIP N-terminal-like protein, CDKN2A-interacting protein N-terminal-like protein, CDKN2AIPNL.

    Product # :

    PRO-1865

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    • description
    • source
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    • More Info

    Description

    CDKN2AIPNL Human Recombinant produced in E. coli is. a single polypeptide chain containing 139 amino acids (1-116) and having a molecular mass of 15.6kDa. CDKN2AIPNL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CDKN2AIPNL solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      CDKN2A Interacting Protein N-Terminal Like (CDKN2AIPNL) is a part of the CARF family.

    • Synonyms

      CDKN2AIP N-terminal-like protein, CDKN2A-interacting protein N-terminal-like protein, CDKN2AIPNL.

    • 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 MGSMVGGEAA AAVEELVSGV RQAADFAEQF RSYSESEKQW KARMEFILRH LPDYRDPPDG SGRLDQLLSL SMVWANHLFL GCSYNKDLLD KVMEMADGIE VEDLPQFTTR SELMKKHQS.

    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.

    Cdkn2Aipnl Human
  • View Data Sheet

    Name :

    CHI3L1 (22-383) Human

    Description:

    Chitinase 3-Like 1 (22-383 a.a) Human Recombinant

    Chitinase 3 Like 1, Chitinase 3-Like 1 (Cartilage Glycoprotein-39), Cartilage Glycoprotein 39, 39 KDa Synovial Protein, HCGP-39, CGP-39, YKL-40, GP-39 , Chitinase-3-Like Protein 1, Cartilage Glycoprotein-39, HC-Gp39, HCGP-3P, YYL-40, ASRT7, YKL40.

    Product # :

    ENZ-975

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    Description

    CHI3L1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 370 amino acids (22-383 a.a.) and having a molecular mass of 41.4kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).CHI3L1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CHI3L1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chitinase 3-Like 1 (CHI3L1) catalyze the hydrolysis of chitin that is an abundant glycopolymer present in insect exoskeletons and fungal cell walls. The glycoside hydrolase 18 family of chitinases comprises 8 human family members. CHI3L1 belongs to the glycosyl hydrolase 18 family. CHI3L1 lacks chitinase activity and is secreted by activated macrophages, chondrocytes, neutrophils and synovial cells. CHI3L1 takes part in the process of inflammation and tissue remodeling.

    • Synonyms

      Chitinase 3 Like 1, Chitinase 3-Like 1 (Cartilage Glycoprotein-39), Cartilage Glycoprotein 39, 39 KDa Synovial Protein, HCGP-39, CGP-39, YKL-40, GP-39 , Chitinase-3-Like Protein 1, Cartilage Glycoprotein-39, HC-Gp39, HCGP-3P, YYL-40, ASRT7, YKL40.

    • 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

      YKLVCYYTSW SQYREGDGSC FPDALDRFLC THIIYSFANI SNDHIDTWEW NDVTLYGMLN TLKNRNPNLK TLLSVGGWNF GSQRFSKIAS NTQSRRTFIK SVPPFLRTHG FDGLDLAWLY PGRGDKQHFT TLIKEMKAEF IKEAQPGKKQ LLLSAALSAG KVTIDSSYDI AKISQHLDFI SIMTYDFHGA WRGTTGHHSP LFRGQEDASP DRFSNTDYAV GYMLRLGAPA SKLVMGIPTF GRSFTLASSE TGVGAPISGP GIPGRFTKEA GTLAYYEICD FLRGATVHRI LGQQVPYATK GNQWVGYDDQ ESVKSKVQYL KDRQLAGAMV WALDLDDFQG SFCGQDLRFP LTNAIKDALA ATLEHHHHHH.

    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.

    Chi3L1 22 383 Human
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